P06731 · CEAM5_HUMAN
- ProteinCarcinoembryonic antigen-related cell adhesion molecule 5
- GeneCEACAM5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids702 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Cell surface glycoprotein that plays a role in cell adhesion, intracellular signaling and tumor progression (PubMed:10864933, PubMed:10910050, PubMed:2803308).
Mediates homophilic and heterophilic cell adhesion with other carcinoembryonic antigen-related cell adhesion molecules, such as CEACAM6 (PubMed:2803308).
Plays a role as an oncogene by promoting tumor progression; induces resistance to anoikis of colorectal carcinoma cells (PubMed:10910050).
Mediates homophilic and heterophilic cell adhesion with other carcinoembryonic antigen-related cell adhesion molecules, such as CEACAM6 (PubMed:2803308).
Plays a role as an oncogene by promoting tumor progression; induces resistance to anoikis of colorectal carcinoma cells (PubMed:10910050).
(Microbial infection) Receptor for E.coli Dr adhesins. Binding of E.coli Dr adhesins leads to dissociation of the homodimer.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | apical plasma membrane | |
Cellular Component | basolateral plasma membrane | |
Cellular Component | cell surface | |
Cellular Component | extracellular exosome | |
Cellular Component | extracellular region | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Cellular Component | side of membrane | |
Molecular Function | GPI anchor binding | |
Molecular Function | identical protein binding | |
Molecular Function | protein homodimerization activity | |
Biological Process | apoptotic process | |
Biological Process | heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules | |
Biological Process | homophilic cell adhesion via plasma membrane adhesion molecules | |
Biological Process | homotypic cell-cell adhesion | |
Biological Process | negative regulation of anoikis | |
Biological Process | negative regulation of apoptotic process | |
Biological Process | negative regulation of myotube differentiation |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCarcinoembryonic antigen-related cell adhesion molecule 5
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP06731
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Lipid-anchor, GPI-anchor
Note: Localized to the apical glycocalyx surface.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 63 | No effect on dimerization. Reduced affinity for E.coli Dr adhesins. | ||||
Sequence: F → I | ||||||
Mutagenesis | 63 | Abolishes dimerization. Reduced affinity for E.coli Dr adhesins. | ||||
Sequence: F → R | ||||||
Mutagenesis | 66 | Abolishes dimerization. | ||||
Sequence: S → N | ||||||
Mutagenesis | 68 | Abolishes dimerization. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 68 | No effect on dimerization. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 69 | Abolishes dimerization. | ||||
Sequence: K → A | ||||||
Mutagenesis | 73 | Abolishes dimerization. | ||||
Sequence: V → A | ||||||
Mutagenesis | 74 | No effect on dimerization. | ||||
Sequence: D → A | ||||||
Mutagenesis | 74 | Abolishes dimerization. | ||||
Sequence: D → L or R | ||||||
Mutagenesis | 78 | Abolishes dimerization. Reduced affinity for E.coli Dr adhesins. | ||||
Sequence: Q → L or R | ||||||
Natural variant | VAR_061310 | 80 | in dbSNP:rs12971352 | |||
Sequence: I → V | ||||||
Natural variant | VAR_061311 | 83 | in dbSNP:rs28683503 | |||
Sequence: V → A | ||||||
Mutagenesis | 125 | Abolishes dimerization. Reduced affinity for E.coli Dr adhesins. | ||||
Sequence: I → A | ||||||
Mutagenesis | 129 | No effect on dimerization. Reduced affinity for E.coli Dr adhesins. | ||||
Sequence: L → A or C | ||||||
Mutagenesis | 129 | Abolishes dimerization. Reduced affinity for E.coli Dr adhesins. | ||||
Sequence: L → S | ||||||
Mutagenesis | 133 | Abolishes dimerization. | ||||
Sequence: E → A | ||||||
Natural variant | VAR_056028 | 137 | in dbSNP:rs3815780 | |||
Sequence: Q → P | ||||||
Natural variant | VAR_031091 | 340 | in dbSNP:rs10407503 | |||
Sequence: A → D | ||||||
Natural variant | VAR_024493 | 398 | in dbSNP:rs7249230 | |||
Sequence: E → K | ||||||
Natural variant | VAR_031092 | 664 | in dbSNP:rs10423171 | |||
Sequence: R → S | ||||||
Natural variant | VAR_056029 | 678 | in dbSNP:rs9621 | |||
Sequence: G → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 951 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, lipidation, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-34 | |||||
Sequence: MESPSAPPHRWCIPWQRLLLTASLLTFWNPPTTA | ||||||
Chain | PRO_0000014566 | 35-685 | Carcinoembryonic antigen-related cell adhesion molecule 5 | |||
Sequence: KLTIESTPFNVAEGKEVLLLVHNLPQHLFGYSWYKGERVDGNRQIIGYVIGTQQATPGPAYSGREIIYPNASLLIQNIIQNDTGFYTLHVIKSDLVNEEATGQFRVYPELPKPSISSNNSKPVEDKDAVAFTCEPETQDATYLWWVNNQSLPVSPRLQLSNGNRTLTLFNVTRNDTASYKCETQNPVSARRSDSVILNVLYGPDAPTISPLNTSYRSGENLNLSCHAASNPPAQYSWFVNGTFQQSTQELFIPNITVNNSGSYTCQAHNSDTGLNRTTVTTITVYAEPPKPFITSNNSNPVEDEDAVALTCEPEIQNTTYLWWVNNQSLPVSPRLQLSNDNRTLTLLSVTRNDVGPYECGIQNELSVDHSDPVILNVLYGPDDPTISPSYTYYRPGVNLSLSCHAASNPPAQYSWLIDGNIQQHTQELFISNITEKNSGLYTCQANNSASGHSRTTVKTITVSAELPKPSISSNNSKPVEDKDAVAFTCEPEAQNTTYLWWVNGQSLPVSPRLQLSNGNRTLTLFNVTRNDARAYVCGIQNSVSANRSDPVTLDVLYGPDTPIISPPDSSYLSGANLNLSCHSASNPSPQYSWRINGIPQQHTQVLFIAKITPNNNGTYACFVSNLATGRNNSIVKSITVSASGTSPGLSA | ||||||
Glycosylation | 104 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 115 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 152 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 167↔215 | |||||
Sequence: CEPETQDATYLWWVNNQSLPVSPRLQLSNGNRTLTLFNVTRNDTASYKC | ||||||
Glycosylation | 182 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 197 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 204 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 208 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 246 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 256 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 259↔299 | |||||
Sequence: CHAASNPPAQYSWFVNGTFQQSTQELFIPNITVNNSGSYTC | ||||||
Glycosylation | 274 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 288 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 292 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 309 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 330 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 345↔393 | |||||
Sequence: CEPEIQNTTYLWWVNNQSLPVSPRLQLSNDNRTLTLLSVTRNDVGPYEC | ||||||
Glycosylation | 351 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 360 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 375 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 432 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 437↔477 | |||||
Sequence: CHAASNPPAQYSWLIDGNIQQHTQELFISNITEKNSGLYTC | ||||||
Glycosylation | 466 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 480 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 508 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 523↔571 | |||||
Sequence: CEPEAQNTTYLWWVNGQSLPVSPRLQLSNGNRTLTLFNVTRNDARAYVC | ||||||
Glycosylation | 529 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 553 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 560 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 580 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 612 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 615↔655 | |||||
Sequence: CHSASNPSPQYSWRINGIPQQHTQVLFIAKITPNNNGTYAC | ||||||
Glycosylation | 650 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 665 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Lipidation | 685 | GPI-anchor amidated alanine | ||||
Sequence: A | ||||||
Propeptide | PRO_0000014567 | 686-702 | Removed in mature form | |||
Sequence: GATVGIMIGVLVGVALI |
Post-translational modification
Complex immunoreactive glycoprotein with a MW of 180 kDa comprising 60% carbohydrate.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in columnar epithelial and goblet cells of the colon (at protein level) (PubMed:10436421).
Found in adenocarcinomas of endodermally derived digestive system epithelium and fetal colon
Found in adenocarcinomas of endodermally derived digestive system epithelium and fetal colon
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P06731 | CEACAM5 P06731 | 7 | EBI-3914938, EBI-3914938 | |
XENO | P06731 | S K0BRG7 | 4 | EBI-3914938, EBI-16040613 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 35-144 | Ig-like V-type | ||||
Sequence: KLTIESTPFNVAEGKEVLLLVHNLPQHLFGYSWYKGERVDGNRQIIGYVIGTQQATPGPAYSGREIIYPNASLLIQNIIQNDTGFYTLHVIKSDLVNEEATGQFRVYPEL | ||||||
Domain | 145-232 | Ig-like C2-type 1 | ||||
Sequence: PKPSISSNNSKPVEDKDAVAFTCEPETQDATYLWWVNNQSLPVSPRLQLSNGNRTLTLFNVTRNDTASYKCETQNPVSARRSDSVILN | ||||||
Domain | 240-315 | Ig-like C2-type 2 | ||||
Sequence: PTISPLNTSYRSGENLNLSCHAASNPPAQYSWFVNGTFQQSTQELFIPNITVNNSGSYTCQAHNSDTGLNRTTVTT | ||||||
Domain | 323-410 | Ig-like C2-type 3 | ||||
Sequence: PKPFITSNNSNPVEDEDAVALTCEPEIQNTTYLWWVNNQSLPVSPRLQLSNDNRTLTLLSVTRNDVGPYECGIQNELSVDHSDPVILN | ||||||
Domain | 418-495 | Ig-like C2-type 4 | ||||
Sequence: PTISPSYTYYRPGVNLSLSCHAASNPPAQYSWLIDGNIQQHTQELFISNITEKNSGLYTCQANNSASGHSRTTVKTIT | ||||||
Domain | 501-588 | Ig-like C2-type 5 | ||||
Sequence: PKPSISSNNSKPVEDKDAVAFTCEPEAQNTTYLWWVNGQSLPVSPRLQLSNGNRTLTLFNVTRNDARAYVCGIQNSVSANRSDPVTLD | ||||||
Domain | 593-675 | Ig-like C2-type 6 | ||||
Sequence: PDTPIISPPDSSYLSGANLNLSCHSASNPSPQYSWRINGIPQQHTQVLFIAKITPNNNGTYACFVSNLATGRNNSIVKSITVS |
Sequence similarities
Belongs to the immunoglobulin superfamily. CEA family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P06731-1
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
- Length702
- Mass (Da)76,796
- Last updated2022-02-23 v4
- Checksum6299AE26CDDBDB5C
P06731-2
- Name2
- Differences from canonical
- 320-320: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
M0R3J1 | M0R3J1_HUMAN | CEACAM5 | 194 | ||
M0QX98 | M0QX98_HUMAN | CEACAM5 | 141 | ||
A0A024R0K5 | A0A024R0K5_HUMAN | CEACAM5 | 702 | ||
A0A087WYX0 | A0A087WYX0_HUMAN | CEACAM5 | 524 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_053414 | 320 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 641 | in Ref. 3; AAA62835 | ||||
Sequence: F → L | ||||||
Sequence conflict | 646 | in Ref. 3; AAA62835 | ||||
Sequence: T → Q | ||||||
Sequence conflict | 689 | in Ref. 3; AAA62835 | ||||
Sequence: V → A |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M17303 EMBL· GenBank· DDBJ | AAB59513.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M29540 EMBL· GenBank· DDBJ | AAA51967.1 EMBL· GenBank· DDBJ | mRNA | ||
M59262 EMBL· GenBank· DDBJ | AAA62835.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
M59255 EMBL· GenBank· DDBJ | AAA62835.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
M59256 EMBL· GenBank· DDBJ | AAA62835.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
M59257 EMBL· GenBank· DDBJ | AAA62835.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
M59258 EMBL· GenBank· DDBJ | AAA62835.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
M59259 EMBL· GenBank· DDBJ | AAA62835.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
M59260 EMBL· GenBank· DDBJ | AAA62835.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
M59261 EMBL· GenBank· DDBJ | AAA62835.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
M59709 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
M59710 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC243967 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
X16455 EMBL· GenBank· DDBJ | CAA34474.1 EMBL· GenBank· DDBJ | mRNA | ||
M15042 EMBL· GenBank· DDBJ | AAA51963.1 EMBL· GenBank· DDBJ | mRNA | ||
M16234 EMBL· GenBank· DDBJ | AAA51972.1 EMBL· GenBank· DDBJ | mRNA |