P31809 · CEAM1_MOUSE
- ProteinCarcinoembryonic antigen-related cell adhesion molecule 1
- GeneCeacam1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids521 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Isoform 1
Cell adhesion protein that mediates homophilic cell adhesion in a calcium-independent manner (By similarity).
Plays a role as coinhibitory receptor in immune response, insulin action and functions also as an activator during angiogenesis (PubMed:16680193, PubMed:17081782, PubMed:18544705, PubMed:21029969, PubMed:21081647, PubMed:22496641, PubMed:22962327, PubMed:23696226).
Its coinhibitory receptor function is phosphorylation- and PTPN6 -dependent, which in turn, suppress signal transduction of associated receptors by dephosphorylation of their downstream effectors (PubMed:17081782, PubMed:21029969, PubMed:22496641).
Plays a role in immune response, of T-cells, natural killer (NK) and neutrophils (PubMed:17081782, PubMed:21029969, PubMed:22496641, PubMed:23696226).
Upon TCR/CD3 complex stimulation, inhibits TCR-mediated cytotoxicity by blocking granule exocytosis by mediating homophilic binding to adjacent cells, allowing interaction with and phosphorylation by LCK and interaction with the TCR/CD3 complex which recruits PTPN6 resulting in dephosphorylation of CD247 and ZAP70 (PubMed:22496641).
Also inhibits T-cell proliferation and cytokine production through inhibition of JNK cascade and plays a crucial role in regulating autoimmunity and anti-tumor immunity by inhibiting T-cell through its interaction with HAVCR2 (PubMed:17081782).
Upon natural killer (NK) cells activation, inhibit KLRK1-mediated cytolysis of CEACAM1-bearing tumor cells by trans-homophilic interactions with CEACAM1 on the target cell and lead to cis-interaction between CEACAM1 and KLRK1, allowing PTPN6 recruitment and then VAV1 dephosphorylation (PubMed:23696226).
Upon neutrophils activation negatively regulates IL1B production by recruiting PTPN6 to a SYK-TLR4-CEACAM1 complex, that dephosphorylates SYK, reducing the production of reactive oxygen species (ROS) and lysosome disruption, which in turn, reduces the activity of the inflammasome (PubMed:22496641).
Down-regulates neutrophil production by acting as a coinhibitory receptor for CSF3R by downregulating the CSF3R-STAT3 pathway through recruitment of PTPN6 that dephosphorylates CSF3R (PubMed:21029969).
Also regulates insulin action by promoting INS clearance and regulating lipogenesis in liver through regulating insulin signaling (PubMed:18544705).
Upon INS stimulation, undergoes phosphorylation by INSR leading to INS clearance by increasing receptor-mediated insulin endocytosis. This inernalization promotes interaction with FASN leading to receptor-mediated insulin degradation and to reduction of FASN activity leading to negative regulation of fatty acid synthesis. INSR-mediated phosphorylation also provokes a down-regulation of cell proliferation through SHC1 interaction resulting in decrease coupling of SHC1 to the MAPK3/ERK1-MAPK1/ERK2 and phosphatidylinositol 3-kinase pathways (By similarity).
Functions as activator in angiogenesis by promoting blood vessel remodeling through endothelial cell differentiation and migration and in arteriogenesis by increasing the number of collateral arteries and collateral vessel calibers after ischemia (PubMed:16680193, PubMed:22962327).
Also regulates vascular permeability through the VEGFR2 signaling pathway resulting in control of nitric oxide production (PubMed:21081647).
Down-regulates cell growth in response to EGF through its interaction with SHC1 that mediates interaction with EGFR resulting in decrease coupling of SHC1 to the MAPK3/ERK1-MAPK1/ERK2 pathway (PubMed:15467833).
Negatively regulates platelet aggregation by decreasing platelet adhesion on type I collagen through the GPVI-FcRgamma complex (PubMed:19008452).
Inhibits cell migration and cell scattering through interaction with FLNA; interferes with the interaction of FLNA with RALA (By similarity).
Mediates bile acid transport activity in a phosphorylation dependent manner (By similarity).
Negatively regulates osteoclastogenesis (PubMed:25490771).
Plays a role as coinhibitory receptor in immune response, insulin action and functions also as an activator during angiogenesis (PubMed:16680193, PubMed:17081782, PubMed:18544705, PubMed:21029969, PubMed:21081647, PubMed:22496641, PubMed:22962327, PubMed:23696226).
Its coinhibitory receptor function is phosphorylation- and PTPN6 -dependent, which in turn, suppress signal transduction of associated receptors by dephosphorylation of their downstream effectors (PubMed:17081782, PubMed:21029969, PubMed:22496641).
Plays a role in immune response, of T-cells, natural killer (NK) and neutrophils (PubMed:17081782, PubMed:21029969, PubMed:22496641, PubMed:23696226).
Upon TCR/CD3 complex stimulation, inhibits TCR-mediated cytotoxicity by blocking granule exocytosis by mediating homophilic binding to adjacent cells, allowing interaction with and phosphorylation by LCK and interaction with the TCR/CD3 complex which recruits PTPN6 resulting in dephosphorylation of CD247 and ZAP70 (PubMed:22496641).
Also inhibits T-cell proliferation and cytokine production through inhibition of JNK cascade and plays a crucial role in regulating autoimmunity and anti-tumor immunity by inhibiting T-cell through its interaction with HAVCR2 (PubMed:17081782).
Upon natural killer (NK) cells activation, inhibit KLRK1-mediated cytolysis of CEACAM1-bearing tumor cells by trans-homophilic interactions with CEACAM1 on the target cell and lead to cis-interaction between CEACAM1 and KLRK1, allowing PTPN6 recruitment and then VAV1 dephosphorylation (PubMed:23696226).
Upon neutrophils activation negatively regulates IL1B production by recruiting PTPN6 to a SYK-TLR4-CEACAM1 complex, that dephosphorylates SYK, reducing the production of reactive oxygen species (ROS) and lysosome disruption, which in turn, reduces the activity of the inflammasome (PubMed:22496641).
Down-regulates neutrophil production by acting as a coinhibitory receptor for CSF3R by downregulating the CSF3R-STAT3 pathway through recruitment of PTPN6 that dephosphorylates CSF3R (PubMed:21029969).
Also regulates insulin action by promoting INS clearance and regulating lipogenesis in liver through regulating insulin signaling (PubMed:18544705).
Upon INS stimulation, undergoes phosphorylation by INSR leading to INS clearance by increasing receptor-mediated insulin endocytosis. This inernalization promotes interaction with FASN leading to receptor-mediated insulin degradation and to reduction of FASN activity leading to negative regulation of fatty acid synthesis. INSR-mediated phosphorylation also provokes a down-regulation of cell proliferation through SHC1 interaction resulting in decrease coupling of SHC1 to the MAPK3/ERK1-MAPK1/ERK2 and phosphatidylinositol 3-kinase pathways (By similarity).
Functions as activator in angiogenesis by promoting blood vessel remodeling through endothelial cell differentiation and migration and in arteriogenesis by increasing the number of collateral arteries and collateral vessel calibers after ischemia (PubMed:16680193, PubMed:22962327).
Also regulates vascular permeability through the VEGFR2 signaling pathway resulting in control of nitric oxide production (PubMed:21081647).
Down-regulates cell growth in response to EGF through its interaction with SHC1 that mediates interaction with EGFR resulting in decrease coupling of SHC1 to the MAPK3/ERK1-MAPK1/ERK2 pathway (PubMed:15467833).
Negatively regulates platelet aggregation by decreasing platelet adhesion on type I collagen through the GPVI-FcRgamma complex (PubMed:19008452).
Inhibits cell migration and cell scattering through interaction with FLNA; interferes with the interaction of FLNA with RALA (By similarity).
Mediates bile acid transport activity in a phosphorylation dependent manner (By similarity).
Negatively regulates osteoclastogenesis (PubMed:25490771).
Isoform 2
Cell adhesion protein that mediates homophilic cell adhesion in a calcium-independent manner (PubMed:1633107).
Promotes populations of T-cells regulating IgA production and secretion associated with control of the commensal microbiota and resistance to enteropathogens (PubMed:23123061).
Promotes populations of T-cells regulating IgA production and secretion associated with control of the commensal microbiota and resistance to enteropathogens (PubMed:23123061).
(Microbial infection) In case of murine coronavirus (MHV) infection, serves as receptor for MHV S1 spike glycoprotein.
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCarcinoembryonic antigen-related cell adhesion molecule 1
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP31809
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell projection, microvillus membrane ; Single-pass type I membrane protein
Apical cell membrane ; Single-pass type I membrane protein
Note: Localized to the apical glycocalyx surface (By similarity).
Colocalizes with CEACAM20 at the apical brush border of intestinal cells (PubMed:25908210).
Colocalizes with CEACAM20 at the apical brush border of intestinal cells (PubMed:25908210).
Isoform 1
Cell membrane ; Single-pass type I membrane protein
Note: Canalicular domain of hepatocyte plasma membranes. Found as a mixture of monomer, dimer and oligomer in the plasma membrane. Occurs predominantly as cis-dimers and/or small cis-oligomers in the cell junction regions. Found as dimer in the solution. Predominantly localized to the lateral cell membranes.
Isoform 2
Cell membrane ; Single-pass type I membrane protein
Note: Predominantly localized to the lateral cell membranes. Found as a mixture of monomer, dimer and oligomer in the plasma membrane. Occurs predominantly as cis-dimers and/or small cis-oligomers in the cell junction regions (By similarity).
Co-localizes with ANXA2 in secretory vesicles and with S100A10/p11 at the plasma membrane (By similarity).
Co-localizes with ANXA2 in secretory vesicles and with S100A10/p11 at the plasma membrane (By similarity).
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 35-428 | Extracellular | ||||
Sequence: EVTIEAVPPQVAEDNNVLLLVHNLPLALGAFAWYKGNTTAIDKEIARFVPNSNMNFTGQAYSGREIIYSNGSLLFQMITMKDMGVYTLDMTDENYRRTQATVRFHVHPILLKPNITSNNSNPVEGDDSVSLTCDSYTDPDNINYLWSRNGESLSEGDRLKLSEGNRTLTLLNVTRNDTGPYVCETRNPVSVNRSDPFSLNIIYGPDTPIISPSDIYLHPGSNLNLSCHAASNPPAQYFWLINEKPHASSQELFIPNITTNNSGTYTCFVNNSVTGLSRTTVKNITVLEPVTQPFLQVTNTTVKELDSVTLTCLSNDIGANIQWLFNSQSLQLTERMTLSQNNSILRIDPIKREDAGEYQCEISNPVSVRRSNSIKLDIIFDPTQGGLSDGAIAG | ||||||
Transmembrane | 429-447 | Helical | ||||
Sequence: IVIGVVAGVALIAGLAYFL | ||||||
Topological domain | 448-521 | Cytoplasmic | ||||
Sequence: YSRKSGGGSDQRDLTEHKPSTSNHNLAPSDNSPNKVDDVAYTVLNFNSQQPNRPTSAPSSPRATETVYSEVKKK |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Knockout mice exhibit impairment of insulin clearance and hyperinsulinemia, which cause insulin resistance; develop insulin resistance primarily in liver (PubMed:18544705).
Display normal white blood cell, red blood cell, hemoglobin and platelet. On the other hand, mice have a high number of neutrophils. Display also increased thrombus growth, and enhanced susceptibility to type I collagen induced pulmonary thromboembolism (PubMed:19008452).
Spontaneously develop systemic neutrophilia. Upon Listeria Monocytogenes (LM) infection mice die dramatically faster within 7 days and display an improved bacterial clearance accompanied by severe tissue damage and necrosis in the liver (PubMed:21029969).
Knockout mice present an increased basal permeability (PubMed:21081647).
Knockout mice show a reduced bone mass namely a decreased trabecular bone volume accompanied by a reduction in trabecular number and an increase in trabecular separation (PubMed:25490771).
Display normal white blood cell, red blood cell, hemoglobin and platelet. On the other hand, mice have a high number of neutrophils. Display also increased thrombus growth, and enhanced susceptibility to type I collagen induced pulmonary thromboembolism (PubMed:19008452).
Spontaneously develop systemic neutrophilia. Upon Listeria Monocytogenes (LM) infection mice die dramatically faster within 7 days and display an improved bacterial clearance accompanied by severe tissue damage and necrosis in the liver (PubMed:21029969).
Knockout mice present an increased basal permeability (PubMed:21081647).
Knockout mice show a reduced bone mass namely a decreased trabecular bone volume accompanied by a reduction in trabecular number and an increase in trabecular separation (PubMed:25490771).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 488 | Phosphorylated on tyrosine. Abrogates interaction with PTPN11. Abrogates interaction with PTPN11 and phosphorylation; when associated with F-515. Reduces endothelial cell migration and differentiation. Suppresses T cell proliferation; when associated with F-515. Increases cytokine production; when associated with F-515. Activates JNK cascade; when associated with F-515. Abrogates CEACAM1-L phosphorylation in endothelial cells and decreases amounts of released nitric oxide upon VEGF stimulation. Impairs interaction with and inactivation of SYK; when associated with F-515. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 503 | Reduces endothelial cell migration and differentiation. | ||||
Sequence: S → A | ||||||
Mutagenesis | 515 | Phosphorylated on tyrosine. Abrogates interaction with PTPN11. Abrogates interaction with PTPN11 and phosphorylation; when associated with F-488. Suppresses T cell proliferation; when associated with F-488. Increases cytokine production; when associated with F-488. Activates JNK cascade; when associated with F-488. Abrogates CEACAM1-L phosphorylation in endothelial cells upon VEGF stimulation. Impairs interaction with and inactivation of SYK; when associated with F-488. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 518 | Impairs interaction with PTPN11 and PTPN6. Doesn't affect phosphorylation. | ||||
Sequence: V → A | ||||||
Mutagenesis | 519-521 | Reduces Tyr phosphorylation by at least 50% and almost completely abrogates interaction with PTPN11 and PTPN6. | ||||
Sequence: Missing |
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-34 | |||||
Sequence: MELASAHLHKGQVPWGGLLLTASLLASWSPATTA | ||||||
Chain | PRO_0000014563 | 35-521 | Carcinoembryonic antigen-related cell adhesion molecule 1 | |||
Sequence: EVTIEAVPPQVAEDNNVLLLVHNLPLALGAFAWYKGNTTAIDKEIARFVPNSNMNFTGQAYSGREIIYSNGSLLFQMITMKDMGVYTLDMTDENYRRTQATVRFHVHPILLKPNITSNNSNPVEGDDSVSLTCDSYTDPDNINYLWSRNGESLSEGDRLKLSEGNRTLTLLNVTRNDTGPYVCETRNPVSVNRSDPFSLNIIYGPDTPIISPSDIYLHPGSNLNLSCHAASNPPAQYFWLINEKPHASSQELFIPNITTNNSGTYTCFVNNSVTGLSRTTVKNITVLEPVTQPFLQVTNTTVKELDSVTLTCLSNDIGANIQWLFNSQSLQLTERMTLSQNNSILRIDPIKREDAGEYQCEISNPVSVRRSNSIKLDIIFDPTQGGLSDGAIAGIVIGVVAGVALIAGLAYFLYSRKSGGGSDQRDLTEHKPSTSNHNLAPSDNSPNKVDDVAYTVLNFNSQQPNRPTSAPSSPRATETVYSEVKKK | ||||||
Glycosylation | 71 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 89 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 104 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 148 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 152 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 167↔217 | |||||
Sequence: CDSYTDPDNINYLWSRNGESLSEGDRLKLSEGNRTLTLLNVTRNDTGPYVC | ||||||
Glycosylation | 199 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 206 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 210 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 226 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 258 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 261↔301 | |||||
Sequence: CHAASNPPAQYFWLINEKPHASSQELFIPNITTNNSGTYTC | ||||||
Glycosylation | 290 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 294 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 304 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 317 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 333 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 346↔394 | |||||
Sequence: CLSNDIGANIQWLFNSQSLQLTERMTLSQNNSILRIDPIKREDAGEYQC | ||||||
Glycosylation | 375 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 488 | Phosphotyrosine; by SRC, LCK, INSR and EGFR | ||||
Sequence: Y | ||||||
Modified residue | 503 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 515 | Phosphotyrosine; by INSR, SRC and LCK | ||||
Sequence: Y |
Post-translational modification
Isoform 1
Phosphorylated on serine and tyrosine (By similarity).
Isoform 1 is phosphorylated on tyrosine by Src family kinases like SRC and LCK and by receptor like CSF3R, EGFR and INSR upon stimulation (PubMed:21029969, PubMed:9867848).
Phosphorylated at Ser-503; mediates activity. Phosphorylated at Tyr-488; regulates activity (By similarity).
Phosphorylated at Tyr-488 by EGFR and INSR upon stimulation; this phosphorylation is Ser-503-phosphorylation-dependent; mediates cellular internalization; increases interaction with FASN (By similarity).
Phosphorylated at Tyr-488 and Tyr-515 by LCK; mediates PTPN6 association and is regulated by homophilic ligation of CEACAM1 in the absence of T-cell activation (By similarity).
Phosphorylated at Tyr-515; mediates interaction with PTPN11 (PubMed:9867848).
Isoform 1 is phosphorylated on tyrosine by Src family kinases like SRC and LCK and by receptor like CSF3R, EGFR and INSR upon stimulation (PubMed:21029969, PubMed:9867848).
Phosphorylated at Ser-503; mediates activity. Phosphorylated at Tyr-488; regulates activity (By similarity).
Phosphorylated at Tyr-488 by EGFR and INSR upon stimulation; this phosphorylation is Ser-503-phosphorylation-dependent; mediates cellular internalization; increases interaction with FASN (By similarity).
Phosphorylated at Tyr-488 and Tyr-515 by LCK; mediates PTPN6 association and is regulated by homophilic ligation of CEACAM1 in the absence of T-cell activation (By similarity).
Phosphorylated at Tyr-515; mediates interaction with PTPN11 (PubMed:9867848).
Isoform 2
Phosphorylated on serine and threonine.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in granulocytes, lymphocytes, granulocytes, B cells, and T-cells (PubMed:11994468).
Expressed in bone. Highly expressed in liver and femur (PubMed:25490771).
Highly expressed in neutrophils, and to a lesser extent inmonocytes, and macrophages. Slightly higher expressed in peripheral blood neutrophils (PBNs) (PubMed:21029969).
Intestinal T-cells predominantly express isoform 2 while extraintestinal T-cells mainly express isoform 1 (PubMed:23123061).
Expressed in small intestine and colon (PubMed:25908210).
Expressed in bone. Highly expressed in liver and femur (PubMed:25490771).
Highly expressed in neutrophils, and to a lesser extent inmonocytes, and macrophages. Slightly higher expressed in peripheral blood neutrophils (PBNs) (PubMed:21029969).
Intestinal T-cells predominantly express isoform 2 while extraintestinal T-cells mainly express isoform 1 (PubMed:23123061).
Expressed in small intestine and colon (PubMed:25908210).
Induction
In intestinal epithelium, up-regulated in the presence of Gram-positive commensal gut bacteria (PubMed:25908210).
May also be up-regulated by interferon gamma (IFNG) and TNF (TNF-alpha) (PubMed:25908210).
Isoform 2: Expression is promoted and maintained by the mucosal environment (PubMed:23123061).
Induced by IL2 on natural killer cell (PubMed:23696226).
May also be up-regulated by interferon gamma (IFNG) and TNF (TNF-alpha) (PubMed:25908210).
Isoform 2: Expression is promoted and maintained by the mucosal environment (PubMed:23123061).
Induced by IL2 on natural killer cell (PubMed:23696226).
Developmental stage
Expression increases during the early stages of osteoblast differentiation, and decreases towards terminal osteoblast differentiation. In addition, expression markedly decreases during the course of osteoclastogenesis.
Gene expression databases
Interaction
Subunit
(Microbial infection) Interacts with MHV S1 spike glycoprotein.
Monomer. Oligomer. Heterodimer. Homodimer (By similarity).
Cis-dimer/oligomer (via Ig-like C2-type and/or via cytoplasmic domains); induced by trans-homophilic cell adhesion through an allosteric mechanism transmitted by the Ig-like V-type domain, and is regulated by intracellular calcium and calmodulin. Interacts (via cytoplasmic domain) with calmodulin in a calcium dependent manner; reduces homophilic cell adhesion through dissociation of dimer (By similarity).
Isoform 1 interacts (via cytoplasmic domain) with PTPN11 (preferentially) and PTPN6; cis-homodimer form is preferred; this interaction is decreased by formation of isoform 1 / isoform 2 cis-heterodimers and is dependent on the monomer/dimer equilibrium; this interaction is phosphorylation-dependent (PubMed:9867848).
Isoform 1 interacts with LYN (PubMed:22496641).
Isoform 1 interacts (via cytoplasmic domain) with SRC (via SH2 domain); this interaction is regulated by trans-homophilic cell adhesion (By similarity).
Isoform 1 interacts with LCK; mediates phosphorylation at Tyr-488 and Tyr-515 resulting in PTPN6 association. Isoform 1 interacts with PTPN6; this interaction is phosphorylation-dependent and causes a profound decrease in TCR stimulation-induced CD247 and ZAP70 phosphorylation. Isoform 1 interacts with TCR/CD3 complex through TCR beta chain and CD3E; colocalizes at the cell surface and upon stimulation of the TCR/CD3 complex recruits PTPN6 in the TCR/CD3 complex, resulting in dephosphorylation of CD247 and ZAP70 (By similarity).
Isoform 1 interacts (via cytoplasmic domain) with SHC1 (via SH2 domain); SHC1 mediates interaction with INSR or EGFR in a Ser-503 phosphorylation-dependent manner (PubMed:15467833).
Isoform 1 interacts with EGFR; the interaction is indirect (By similarity).
Isoform 1 interacts with CSF3R; down-regulates the CSF3R-STAT3 pathway through recruitment of PTPN6 that dephosphorylates CSF3R (PubMed:21029969).
Isoform 1 (phosphorylated form) interacts with TLR4 and SYK; recruits PTPN6 that dephosphorylates SYK, reducing the production of reactive oxygen species (ROS) and lysosome disruption, leading to a reduction of the inflammasome activity (PubMed:22496641).
Isoform 1 interacts with FLNA; inhibits cell migration and cell scattering by interfering with the interaction of FLNA with RALA. Isoform 1 interacts (via cytoplasmic domain) with PXN; the interaction is phosphotyrosyl-dependent. Isoform 1 interacts with KLRK1; recruits PTPN6 that dephosphorylates VAV1. Isoform 1 interacts with CEACAM8 (By similarity).
Isoform 1 interacts with FASN; this interaction is insulin and phosphorylation-dependent; reduces fatty-acid synthase activity (By similarity).
Interacts (via Ig-like V-type) with HAVCR2 (via Ig-like V-type); facilitates the maturation and cell surface expression of HAVCR2 thereby regulating T-cell tolerance induction (By similarity) (PubMed:25363763).
Isoform 2 interacts (via the cytoplasmic domain) with ANXA2; this interaction is regulated by phosphorylation and appears in the AIIt complex. Interacts (via Lewis X moieties) with CD209 (via C-type lectin domain); this interaction is regulated by the glycosylation pattern of CEACAM1 on cell types and regulates contact between dendritic cells and neutrophils (By similarity).
Cis-dimer/oligomer (via Ig-like C2-type and/or via cytoplasmic domains); induced by trans-homophilic cell adhesion through an allosteric mechanism transmitted by the Ig-like V-type domain, and is regulated by intracellular calcium and calmodulin. Interacts (via cytoplasmic domain) with calmodulin in a calcium dependent manner; reduces homophilic cell adhesion through dissociation of dimer (By similarity).
Isoform 1 interacts (via cytoplasmic domain) with PTPN11 (preferentially) and PTPN6; cis-homodimer form is preferred; this interaction is decreased by formation of isoform 1 / isoform 2 cis-heterodimers and is dependent on the monomer/dimer equilibrium; this interaction is phosphorylation-dependent (PubMed:9867848).
Isoform 1 interacts with LYN (PubMed:22496641).
Isoform 1 interacts (via cytoplasmic domain) with SRC (via SH2 domain); this interaction is regulated by trans-homophilic cell adhesion (By similarity).
Isoform 1 interacts with LCK; mediates phosphorylation at Tyr-488 and Tyr-515 resulting in PTPN6 association. Isoform 1 interacts with PTPN6; this interaction is phosphorylation-dependent and causes a profound decrease in TCR stimulation-induced CD247 and ZAP70 phosphorylation. Isoform 1 interacts with TCR/CD3 complex through TCR beta chain and CD3E; colocalizes at the cell surface and upon stimulation of the TCR/CD3 complex recruits PTPN6 in the TCR/CD3 complex, resulting in dephosphorylation of CD247 and ZAP70 (By similarity).
Isoform 1 interacts (via cytoplasmic domain) with SHC1 (via SH2 domain); SHC1 mediates interaction with INSR or EGFR in a Ser-503 phosphorylation-dependent manner (PubMed:15467833).
Isoform 1 interacts with EGFR; the interaction is indirect (By similarity).
Isoform 1 interacts with CSF3R; down-regulates the CSF3R-STAT3 pathway through recruitment of PTPN6 that dephosphorylates CSF3R (PubMed:21029969).
Isoform 1 (phosphorylated form) interacts with TLR4 and SYK; recruits PTPN6 that dephosphorylates SYK, reducing the production of reactive oxygen species (ROS) and lysosome disruption, leading to a reduction of the inflammasome activity (PubMed:22496641).
Isoform 1 interacts with FLNA; inhibits cell migration and cell scattering by interfering with the interaction of FLNA with RALA. Isoform 1 interacts (via cytoplasmic domain) with PXN; the interaction is phosphotyrosyl-dependent. Isoform 1 interacts with KLRK1; recruits PTPN6 that dephosphorylates VAV1. Isoform 1 interacts with CEACAM8 (By similarity).
Isoform 1 interacts with FASN; this interaction is insulin and phosphorylation-dependent; reduces fatty-acid synthase activity (By similarity).
Interacts (via Ig-like V-type) with HAVCR2 (via Ig-like V-type); facilitates the maturation and cell surface expression of HAVCR2 thereby regulating T-cell tolerance induction (By similarity) (PubMed:25363763).
Isoform 2 interacts (via the cytoplasmic domain) with ANXA2; this interaction is regulated by phosphorylation and appears in the AIIt complex. Interacts (via Lewis X moieties) with CD209 (via C-type lectin domain); this interaction is regulated by the glycosylation pattern of CEACAM1 on cell types and regulates contact between dendritic cells and neutrophils (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 35-142 | Ig-like V-type | ||||
Sequence: EVTIEAVPPQVAEDNNVLLLVHNLPLALGAFAWYKGNTTAIDKEIARFVPNSNMNFTGQAYSGREIIYSNGSLLFQMITMKDMGVYTLDMTDENYRRTQATVRFHVHP | ||||||
Region | 39-142 | Required for homophilic binding | ||||
Sequence: EAVPPQVAEDNNVLLLVHNLPLALGAFAWYKGNTTAIDKEIARFVPNSNMNFTGQAYSGREIIYSNGSLLFQMITMKDMGVYTLDMTDENYRRTQATVRFHVHP | ||||||
Domain | 147-234 | Ig-like C2-type 1 | ||||
Sequence: PNITSNNSNPVEGDDSVSLTCDSYTDPDNINYLWSRNGESLSEGDRLKLSEGNRTLTLLNVTRNDTGPYVCETRNPVSVNRSDPFSLN | ||||||
Domain | 239-319 | Ig-like C2-type 2 | ||||
Sequence: PDTPIISPSDIYLHPGSNLNLSCHAASNPPAQYFWLINEKPHASSQELFIPNITTNNSGTYTCFVNNSVTGLSRTTVKNIT | ||||||
Domain | 323-411 | Ig-like C2-type 3 | ||||
Sequence: PVTQPFLQVTNTTVKELDSVTLTCLSNDIGANIQWLFNSQSLQLTERMTLSQNNSILRIDPIKREDAGEYQCEISNPVSVRRSNSIKLD | ||||||
Region | 445-457 | Interaction with calmodulin | ||||
Sequence: YFLYSRKSGGGSD | ||||||
Region | 447-521 | Interaction with FLNA | ||||
Sequence: LYSRKSGGGSDQRDLTEHKPSTSNHNLAPSDNSPNKVDDVAYTVLNFNSQQPNRPTSAPSSPRATETVYSEVKKK | ||||||
Region | 455-521 | Disordered | ||||
Sequence: GSDQRDLTEHKPSTSNHNLAPSDNSPNKVDDVAYTVLNFNSQQPNRPTSAPSSPRATETVYSEVKKK | ||||||
Compositional bias | 467-513 | Polar residues | ||||
Sequence: STSNHNLAPSDNSPNKVDDVAYTVLNFNSQQPNRPTSAPSSPRATET | ||||||
Region | 484-521 | Required for interaction with PTPN11 and PTPN6 and for control of phosphorylation level | ||||
Sequence: DDVAYTVLNFNSQQPNRPTSAPSSPRATETVYSEVKKK | ||||||
Region | 515-518 | Essential for interaction with PTPN11 and PTPN6 | ||||
Sequence: YSEV |
Domain
Ig-like V-type domain mediates trans-homophilic cell adhesion through homodimerization and this active process is regulated by tyrosine kinase, PTPN11 and PTPN6. Ig-like C2-type and/or cytoplasmic domains mediate cis-dimer/oligomer.
Sequence similarities
Belongs to the immunoglobulin superfamily. CEA family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 4 isoforms produced by Alternative splicing.
P31809-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsCeacam1-4L, Bgpd
- Length521
- Mass (Da)57,016
- Last updated1993-07-01 v1
- Checksum1C8F71FAC47DD54E
P31809-2
- Name2
- SynonymsCeacam1-4S, Bgpa, mmCGM1a
P31809-3
- Name3
- SynonymsCeacam1-2L, Bgpg
P31809-4
- Name4
- SynonymsCeacam1-2S, Bgpc
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_036040 | 142 | in isoform 3 | |||
Sequence: P → Q | ||||||
Alternative sequence | VSP_058517 | 142-322 | in isoform 4 | |||
Sequence: PILLKPNITSNNSNPVEGDDSVSLTCDSYTDPDNINYLWSRNGESLSEGDRLKLSEGNRTLTLLNVTRNDTGPYVCETRNPVSVNRSDPFSLNIIYGPDTPIISPSDIYLHPGSNLNLSCHAASNPPAQYFWLINEKPHASSQELFIPNITTNNSGTYTCFVNNSVTGLSRTTVKNITVLE → Q | ||||||
Alternative sequence | VSP_036041 | 143-322 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 361-362 | in Ref. 3; CAA47699/CAA47695 | ||||
Sequence: SQ → RE | ||||||
Alternative sequence | VSP_002484 | 455-458 | in isoform 2 and isoform 4 | |||
Sequence: GSDQ → SGSF | ||||||
Alternative sequence | VSP_002485 | 459-521 | in isoform 2 and isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 467-513 | Polar residues | ||||
Sequence: STSNHNLAPSDNSPNKVDDVAYTVLNFNSQQPNRPTSAPSSPRATET |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M77196 EMBL· GenBank· DDBJ | AAA37858.1 EMBL· GenBank· DDBJ | mRNA | ||
X15351 EMBL· GenBank· DDBJ | CAA33409.1 EMBL· GenBank· DDBJ | mRNA | ||
X67278 EMBL· GenBank· DDBJ | CAA47695.1 EMBL· GenBank· DDBJ | mRNA | ||
X67279 EMBL· GenBank· DDBJ | CAA47696.1 EMBL· GenBank· DDBJ | mRNA | ||
X67282 EMBL· GenBank· DDBJ | CAA47699.1 EMBL· GenBank· DDBJ | mRNA |