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P50895 (BCAM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Basal cell adhesion molecule
Alternative name(s):
Auberger B antigen
B-CAM cell surface glycoprotein
F8/G253 antigen
Lutheran antigen
Lutheran blood group glycoprotein
CD_antigen=CD239
Gene names
Name:BCAM
Synonyms:LU, MSK19
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length628 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Laminin alpha-5 receptor. May mediate intracellular signaling. Ref.10

Subcellular location

Membrane; Single-pass type I membrane protein.

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.

Post-translational modification

Epinephrine-stimulated phosphorylation of Ser-621 by PKA enhances adhesion to laminin.

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.

Sequence similarities

Contains 3 Ig-like C2-type (immunoglobulin-like) domains.

Contains 2 Ig-like V-type (immunoglobulin-like) domains.

Sequence caution

The sequence EAW57297.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Ref.1
Chain32 – 628597Basal cell adhesion molecule
PRO_0000014850

Regions

Topological domain32 – 547516Extracellular Potential
Transmembrane548 – 56821Helical; Potential
Topological domain569 – 62860Cytoplasmic Potential
Domain32 – 142111Ig-like V-type 1
Domain147 – 257111Ig-like V-type 2
Domain274 – 35582Ig-like C2-type 1
Domain363 – 44179Ig-like C2-type 2
Domain448 – 54194Ig-like C2-type 3
Region309 – 3124Interaction with laminin alpha5

Amino acid modifications

Modified residue5961Phosphoserine; by GSK3 Ref.12
Modified residue5981Phosphoserine; by CK2 Ref.12
Modified residue6211Phosphoserine; by PKA Ref.12
Glycosylation3211N-linked (GlcNAc...) Potential
Glycosylation3771N-linked (GlcNAc...) Potential
Glycosylation3831N-linked (GlcNAc...) Potential
Glycosylation4191N-linked (GlcNAc...) Potential
Glycosylation4391N-linked (GlcNAc...) Ref.11 Ref.13
Disulfide bond53 ↔ 125 Ref.16
Disulfide bond172 ↔ 237 Ref.16
Disulfide bond291 ↔ 337 Probable
Disulfide bond384 ↔ 424 Probable
Disulfide bond473 ↔ 522 Probable

Natural variations

Natural variant771R → H Defines the Lu(a) antigen. Ref.2
Corresponds to variant rs28399653 [ dbSNP | Ensembl ].
VAR_021348
Natural variant1961V → I. Ref.2
Corresponds to variant rs28399654 [ dbSNP | Ensembl ].
VAR_021349
Natural variant2041M → K. Ref.2
Corresponds to variant rs28399656 [ dbSNP | Ensembl ].
VAR_021350
Natural variant2821R → H. Ref.2
Corresponds to variant rs9967601 [ dbSNP | Ensembl ].
VAR_021351
Natural variant3811V → I. Ref.2
Corresponds to variant rs28399626 [ dbSNP | Ensembl ].
VAR_021352
Natural variant4511K → Q. Ref.2
Corresponds to variant rs28399630 [ dbSNP | Ensembl ].
VAR_021353
Natural variant5391T → A. Ref.1 Ref.6 Ref.7
Corresponds to variant rs1135062 [ dbSNP | Ensembl ].
VAR_021354
Natural variant5811Q → L. Ref.2
Corresponds to variant rs28399659 [ dbSNP | Ensembl ].
VAR_021355

Experimental info

Mutagenesis6211S → A: Dramatically reduced cell adhesion. Ref.12
Sequence conflict225 – 2262RL → PC in CAA56327. Ref.6
Sequence conflict355 – 3562EL → DV in CAA56327. Ref.6
Sequence conflict5321R → L in ABY27636. Ref.7

Secondary structure

............................................. 628
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P50895 [UniParc].

Last modified March 7, 2006. Version 2.
Checksum: C88F4F5C640C3F5B

FASTA62867,405
        10         20         30         40         50         60 
MEPPDAPAQA RGAPRLLLLA VLLAAHPDAQ AEVRLSVPPL VEVMRGKSVI LDCTPTGTHD 

        70         80         90        100        110        120 
HYMLEWFLTD RSGARPRLAS AEMQGSELQV TMHDTRGRSP PYQLDSQGRL VLAEAQVGDE 

       130        140        150        160        170        180 
RDYVCVVRAG AAGTAEATAR LNVFAKPEAT EVSPNKGTLS VMEDSAQEIA TCNSRNGNPA 

       190        200        210        220        230        240 
PKITWYRNGQ RLEVPVEMNP EGYMTSRTVR EASGLLSLTS TLYLRLRKDD RDASFHCAAH 

       250        260        270        280        290        300 
YSLPEGRHGR LDSPTFHLTL HYPTEHVQFW VGSPSTPAGW VREGDTVQLL CRGDGSPSPE 

       310        320        330        340        350        360 
YTLFRLQDEQ EEVLNVNLEG NLTLEGVTRG QSGTYGCRVE DYDAADDVQL SKTLELRVAY 

       370        380        390        400        410        420 
LDPLELSEGK VLSLPLNSSA VVNCSVHGLP TPALRWTKDS TPLGDGPMLS LSSITFDSNG 

       430        440        450        460        470        480 
TYVCEASLPT VPVLSRTQNF TLLVQGSPEL KTAEIEPKAD GSWREGDEVT LICSARGHPD 

       490        500        510        520        530        540 
PKLSWSQLGG SPAEPIPGRQ GWVSSSLTLK VTSALSRDGI SCEASNPHGN KRHVFHFGTV 

       550        560        570        580        590        600 
SPQTSQAGVA VMAVAVSVGL LLLVVAVFYC VRRKGGPCCR QRREKGAPPP GEPGLSHSGS 

       610        620 
EQPEQTGLLM GGASGGARGG SGGFGDEC 

« Hide

References

« Hide 'large scale' references
[1]"The Lutheran blood group glycoprotein, another member of the immunoglobulin superfamily, is widely expressed in human tissues and is developmentally regulated in human liver."
Parsons S.F., Mallinson G., Holmes C.H., Houlihan J.M., Simpson K.L., Mawby W.J., Spurr N.K., Warne D., Barclay A.N., Anstee D.J.
Proc. Natl. Acad. Sci. U.S.A. 92:5496-5500(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 32-67 AND 182-203, VARIANT ALA-539.
Tissue: Placenta.
[2]SeattleSNPs variation discovery resource
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-77; ILE-196; LYS-204; HIS-282; ILE-381; GLN-451 AND LEU-581.
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[6]"Molecular cloning of the B-CAM cell surface glycoprotein of epithelial cancers: a novel member of the immunoglobulin superfamily."
Campbell I.G., Foulkes W.D., Senger G., Trowsdale J., Garin-Chesa P., Rettig W.J.
Cancer Res. 54:5761-5765(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-588, VARIANT ALA-539.
[7]"Molecular basis of Lub(-) individual among Chinese blood donors in Shanghai area."
Wang C., Li Q., Guo Z., Yang Y., Zhu Z.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 492-539, VARIANT ALA-539.
[8]"Use of domain-deletion mutants to locate Lutheran blood group antigens to each of the five immunoglobulin superfamily domains of the Lutheran glycoprotein: elucidation of the molecular basis of the Lu(a)/Lu(b) and the Au(a)/Au(b) polymorphisms."
Parsons S.F., Mallinson G., Daniels G.L., Green C.A., Smythe J.S., Anstee D.J.
Blood 89:4219-4225(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: LU(A)/LU(B) POLYMORPHISM.
[9]"Organization of the human LU gene and molecular basis of the Lu(a)/Lu(b) blood group polymorphism."
El Nemer W., Rahuel C., Colin Y., Gane P., Cartron J.P., Le Van Kim C.
Blood 89:4608-4616(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: LU(A)/LU(B) POLYMORPHISM.
[10]"Basal cell adhesion molecule/lutheran protein. The receptor critical for sickle cell adhesion to laminin."
Udani M., Zen Q., Cottman M., Leonard N., Jefferson S., Daymont C., Truskey G., Telen M.J.
J. Clin. Invest. 101:2550-2558(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Zhang H., Li X.-J., Martin D.B., Aebersold R.
Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-439.
[12]"Protein kinase A-dependent phosphorylation of Lutheran/basal cell adhesion molecule glycoprotein regulates cell adhesion to laminin alpha5."
Gauthier E., Rahuel C., Wautier M.P., El Nemer W., Gane P., Wautier J.L., Cartron J.P., Colin Y., Le Van Kim C.
J. Biol. Chem. 280:30055-30062(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-596; SER-598 AND SER-621, MUTAGENESIS OF SER-621.
[13]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-439.
Tissue: Plasma.
[14]"Different inactivating mutations in the LU genes of three individuals with the Lutheran-null phenotype."
Karamatic Crew V., Mallinson G., Green C., Poole J., Uchikawa M., Tani Y., Geisen C., Oldenburg J., Daniels G.
Transfusion 47:492-498(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN THE LUTHERAN NULL PHENOTYPE.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"The Laminin 511/521-binding site on the Lutheran blood group glycoprotein is located at the flexible junction of Ig domains 2 and 3."
Mankelow T.J., Burton N., Stefansdottir F.O., Spring F.A., Parsons S.F., Pedersen J.S., Oliveira C.L., Lammie D., Wess T., Mohandas N., Chasis J.A., Brady R.L., Anstee D.J.
Blood 110:3398-3406(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 32-262, LAMININ-ALPHA5 BINDING REGION, DISULFIDE BONDS.
+Additional computationally mapped references.

Web resources

dbRBC/BGMUT

Blood group antigen gene mutation database

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X83425 mRNA. Translation: CAA58449.1.
AY845133 Genomic DNA. Translation: AAV88096.1.
AC092306 Genomic DNA. No translation available.
CH471126 Genomic DNA. Translation: EAW57297.1. Sequence problems.
BC050450 mRNA. Translation: AAH50450.1.
X80026 mRNA. Translation: CAA56327.1.
EU307108 Genomic DNA. Translation: ABY27636.1.
EU307109 Genomic DNA. Translation: ABY27637.1.
PIRI37202.
I38000.
RefSeqNP_001013275.1. NM_001013257.2.
NP_005572.2. NM_005581.4.
UniGeneHs.625725.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PETX-ray1.70A32-262[»]
2PF6X-ray2.20A/B32-262[»]
ProteinModelPortalP50895.
SMRP50895. Positions 32-532.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110237. 4 interactions.
MINTMINT-5004331.
STRING9606.ENSP00000270233.

PTM databases

PhosphoSiteP50895.

Polymorphism databases

DMDM92058724.

Proteomic databases

PaxDbP50895.
PRIDEP50895.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000270233; ENSP00000270233; ENSG00000187244.
GeneID4059.
KEGGhsa:4059.
UCSCuc002ozt.2. human.

Organism-specific databases

CTD4059.
GeneCardsGC19P045312.
HGNCHGNC:6722. BCAM.
HPAHPA005654.
MIM111200. phenotype.
247420. phenotype.
612773. gene.
neXtProtNX_P50895.
PharmGKBPA30484.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG150030.
HOGENOMHOG000113409.
InParanoidP50895.
KOK06578.
OMAHYPTEHV.
OrthoDBEOG7GBFWH.
PhylomeDBP50895.
TreeFamTF330534.

Gene expression databases

ArrayExpressP50895.
BgeeP50895.
CleanExHS_BCAM.
GenevestigatorP50895.

Family and domain databases

Gene3D2.60.40.10. 5 hits.
InterProIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PfamPF08205. C2-set_2. 1 hit.
[Graphical view]
SMARTSM00409. IG. 2 hits.
SM00408. IGc2. 2 hits.
[Graphical view]
PROSITEPS50835. IG_LIKE. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBCAM. human.
EvolutionaryTraceP50895.
GeneWikiBCAM.
GenomeRNAi4059.
NextBio15906.
PROP50895.
SOURCESearch...

Entry information

Entry nameBCAM_HUMAN
AccessionPrimary (citable) accession number: P50895
Secondary accession number(s): A8MYF9 expand/collapse secondary AC list , A9YWT5, A9YWT6, Q86VC7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: March 7, 2006
Last modified: April 16, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries

Blood group antigen proteins

Nomenclature of blood group antigens and list of entries