P50895 · BCAM_HUMAN
- ProteinBasal cell adhesion molecule
- GeneBCAM
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids628 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Laminin alpha-5 receptor. May mediate intracellular signaling.
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 | collagen-containing extracellular matrix | |
Cellular Component | external side of plasma membrane | |
Cellular Component | extracellular exosome | |
Cellular Component | extracellular region | |
Cellular Component | plasma membrane | |
Molecular Function | laminin binding | |
Molecular Function | laminin receptor activity | |
Molecular Function | transmembrane signaling receptor activity | |
Biological Process | cell adhesion | |
Biological Process | cell-matrix adhesion | |
Biological Process | signal transduction |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBasal cell adhesion molecule
- 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 accessionP50895
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 32-547 | Extracellular | ||||
Sequence: EVRLSVPPLVEVMRGKSVILDCTPTGTHDHYMLEWFLTDRSGARPRLASAEMQGSELQVTMHDTRGRSPPYQLDSQGRLVLAEAQVGDERDYVCVVRAGAAGTAEATARLNVFAKPEATEVSPNKGTLSVMEDSAQEIATCNSRNGNPAPKITWYRNGQRLEVPVEMNPEGYMTSRTVREASGLLSLTSTLYLRLRKDDRDASFHCAAHYSLPEGRHGRLDSPTFHLTLHYPTEHVQFWVGSPSTPAGWVREGDTVQLLCRGDGSPSPEYTLFRLQDEQEEVLNVNLEGNLTLEGVTRGQSGTYGCRVEDYDAADDVQLSKTLELRVAYLDPLELSEGKVLSLPLNSSAVVNCSVHGLPTPALRWTKDSTPLGDGPMLSLSSITFDSNGTYVCEASLPTVPVLSRTQNFTLLVQGSPELKTAEIEPKADGSWREGDEVTLICSARGHPDPKLSWSQLGGSPAEPIPGRQGWVSSSLTLKVTSALSRDGISCEASNPHGNKRHVFHFGTVSPQTSQA | ||||||
Transmembrane | 548-568 | Helical | ||||
Sequence: GVAVMAVAVSVGLLLLVVAVF | ||||||
Topological domain | 569-628 | Cytoplasmic | ||||
Sequence: YCVRRKGGPCCRQRREKGAPPPGEPGLSHSGSEQPEQTGLLMGGASGGARGGSGGFGDEC |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_021348 | 77 | defines the Lu(a) antigen; dbSNP:rs28399653 | |||
Sequence: R → H | ||||||
Natural variant | VAR_021349 | 196 | in dbSNP:rs28399654 | |||
Sequence: V → I | ||||||
Natural variant | VAR_021350 | 204 | in dbSNP:rs28399656 | |||
Sequence: M → K | ||||||
Natural variant | VAR_021351 | 282 | in dbSNP:rs9967601 | |||
Sequence: R → H | ||||||
Natural variant | VAR_021352 | 381 | in dbSNP:rs28399626 | |||
Sequence: V → I | ||||||
Natural variant | VAR_021353 | 451 | in dbSNP:rs28399630 | |||
Sequence: K → Q | ||||||
Natural variant | VAR_021354 | 539 | in dbSNP:rs1135062 | |||
Sequence: T → A | ||||||
Natural variant | VAR_021355 | 581 | in dbSNP:rs28399659 | |||
Sequence: Q → L | ||||||
Mutagenesis | 621 | Dramatically reduced cell adhesion. | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 834 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-31 | UniProt | |||||
Sequence: MEPPDAPAQARGAPRLLLLAVLLAAHPDAQA | |||||||
Chain | PRO_0000014850 | 32-628 | UniProt | Basal cell adhesion molecule | |||
Sequence: EVRLSVPPLVEVMRGKSVILDCTPTGTHDHYMLEWFLTDRSGARPRLASAEMQGSELQVTMHDTRGRSPPYQLDSQGRLVLAEAQVGDERDYVCVVRAGAAGTAEATARLNVFAKPEATEVSPNKGTLSVMEDSAQEIATCNSRNGNPAPKITWYRNGQRLEVPVEMNPEGYMTSRTVREASGLLSLTSTLYLRLRKDDRDASFHCAAHYSLPEGRHGRLDSPTFHLTLHYPTEHVQFWVGSPSTPAGWVREGDTVQLLCRGDGSPSPEYTLFRLQDEQEEVLNVNLEGNLTLEGVTRGQSGTYGCRVEDYDAADDVQLSKTLELRVAYLDPLELSEGKVLSLPLNSSAVVNCSVHGLPTPALRWTKDSTPLGDGPMLSLSSITFDSNGTYVCEASLPTVPVLSRTQNFTLLVQGSPELKTAEIEPKADGSWREGDEVTLICSARGHPDPKLSWSQLGGSPAEPIPGRQGWVSSSLTLKVTSALSRDGISCEASNPHGNKRHVFHFGTVSPQTSQAGVAVMAVAVSVGLLLLVVAVFYCVRRKGGPCCRQRREKGAPPPGEPGLSHSGSEQPEQTGLLMGGASGGARGGSGGFGDEC | |||||||
Disulfide bond | 53↔125 | UniProt | |||||
Sequence: CTPTGTHDHYMLEWFLTDRSGARPRLASAEMQGSELQVTMHDTRGRSPPYQLDSQGRLVLAEAQVGDERDYVC | |||||||
Disulfide bond | 172↔237 | UniProt | |||||
Sequence: CNSRNGNPAPKITWYRNGQRLEVPVEMNPEGYMTSRTVREASGLLSLTSTLYLRLRKDDRDASFHC | |||||||
Disulfide bond | 291↔337 | UniProt | |||||
Sequence: CRGDGSPSPEYTLFRLQDEQEEVLNVNLEGNLTLEGVTRGQSGTYGC | |||||||
Glycosylation | 321 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 377 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 383 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 384↔424 | UniProt | |||||
Sequence: CSVHGLPTPALRWTKDSTPLGDGPMLSLSSITFDSNGTYVC | |||||||
Glycosylation | 419 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 439 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 473↔522 | UniProt | |||||
Sequence: CSARGHPDPKLSWSQLGGSPAEPIPGRQGWVSSSLTLKVTSALSRDGISC | |||||||
Modified residue | 596 | UniProt | Phosphoserine; by GSK3 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 596 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 598 | UniProt | Phosphoserine; by CK2 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 598 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 600 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 600 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 614 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 621 | UniProt | Phosphoserine; by PKA | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 621 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Epinephrine-stimulated phosphorylation of Ser-621 by PKA enhances adhesion to laminin.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Wide tissue distribution (highest in the pancreas and very low in brain). Closely associated with the basal layer of cells in epithelia and the endothelium of blood vessel walls.
Developmental stage
Is under developmental control in liver and may also be regulated during differentiation in other tissues. Up-regulated following malignant transformation in some cell types.
Gene expression databases
Organism-specific databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P50895 | KLHL2 O95198 | 6 | EBI-10212133, EBI-746999 | |
BINARY | P50895 | KRTAP1-1 Q07627 | 3 | EBI-10212133, EBI-11959885 | |
BINARY | P50895 | KRTAP1-3 Q8IUG1 | 3 | EBI-10212133, EBI-11749135 | |
BINARY | P50895 | MDFI Q99750 | 3 | EBI-10212133, EBI-724076 | |
BINARY | P50895 | NOTCH2NLC P0DPK4 | 3 | EBI-10212133, EBI-22310682 | |
BINARY | P50895 | TRIM7 Q9C029 | 3 | EBI-10212133, EBI-2813981 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 32-142 | Ig-like V-type 1 | ||||
Sequence: EVRLSVPPLVEVMRGKSVILDCTPTGTHDHYMLEWFLTDRSGARPRLASAEMQGSELQVTMHDTRGRSPPYQLDSQGRLVLAEAQVGDERDYVCVVRAGAAGTAEATARLN | ||||||
Domain | 147-257 | Ig-like V-type 2 | ||||
Sequence: PEATEVSPNKGTLSVMEDSAQEIATCNSRNGNPAPKITWYRNGQRLEVPVEMNPEGYMTSRTVREASGLLSLTSTLYLRLRKDDRDASFHCAAHYSLPEGRHGRLDSPTFH | ||||||
Domain | 274-355 | Ig-like C2-type 1 | ||||
Sequence: PSTPAGWVREGDTVQLLCRGDGSPSPEYTLFRLQDEQEEVLNVNLEGNLTLEGVTRGQSGTYGCRVEDYDAADDVQLSKTLE | ||||||
Region | 309-312 | Interaction with laminin alpha5 | ||||
Sequence: EQEE | ||||||
Domain | 363-441 | Ig-like C2-type 2 | ||||
Sequence: PLELSEGKVLSLPLNSSAVVNCSVHGLPTPALRWTKDSTPLGDGPMLSLSSITFDSNGTYVCEASLPTVPVLSRTQNFT | ||||||
Domain | 448-541 | Ig-like C2-type 3 | ||||
Sequence: PELKTAEIEPKADGSWREGDEVTLICSARGHPDPKLSWSQLGGSPAEPIPGRQGWVSSSLTLKVTSALSRDGISCEASNPHGNKRHVFHFGTVS | ||||||
Region | 579-628 | Disordered | ||||
Sequence: CRQRREKGAPPPGEPGLSHSGSEQPEQTGLLMGGASGGARGGSGGFGDEC |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length628
- Mass (Da)67,405
- Last updated2006-03-07 v2
- ChecksumC88F4F5C640C3F5B
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
K7ENU8 | K7ENU8_HUMAN | BCAM | 286 | ||
K7ERB7 | K7ERB7_HUMAN | BCAM | 61 | ||
A0A087WXM8 | A0A087WXM8_HUMAN | BCAM | 588 |
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 225-226 | in Ref. 6; CAA56327 | ||||
Sequence: RL → PC | ||||||
Sequence conflict | 355-356 | in Ref. 6; CAA56327 | ||||
Sequence: EL → DV | ||||||
Sequence conflict | 532 | in Ref. 7; ABY27636 | ||||
Sequence: R → L |
Polymorphism
BCAM is responsible for the Lutheran blood group system (LU) [MIM:111200]. Lutheran is a complex blood group system consisting of 19 antigens. Antigens Lu(a) and Lu(b) are defined by a polymorphism at position 77: Lu(a) has His-77 and Lu(b) has Arg-77.
Inactivating variants in BCAM are responsible for the recessive Lutheran null phenotype Lu(a-b-) of the Lutheran blood group [MIM:247420]. Autosomal recessive inheritance of the Lutheran null blood group phenotype is extremely rare. There is no obvious associated clinical or hematologic pathology, and all patients have been identified through identification of anti-Lu3 antibodies in their serum.
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X83425 EMBL· GenBank· DDBJ | CAA58449.1 EMBL· GenBank· DDBJ | mRNA | ||
AY845133 EMBL· GenBank· DDBJ | AAV88096.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC092306 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471126 EMBL· GenBank· DDBJ | EAW57297.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
BC050450 EMBL· GenBank· DDBJ | AAH50450.1 EMBL· GenBank· DDBJ | mRNA | ||
X80026 EMBL· GenBank· DDBJ | CAA56327.1 EMBL· GenBank· DDBJ | mRNA | ||
EU307108 EMBL· GenBank· DDBJ | ABY27636.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
EU307109 EMBL· GenBank· DDBJ | ABY27637.1 EMBL· GenBank· DDBJ | Genomic DNA |