Reviewed, UniProtKB/Swiss-Prot P50895 (BCAM_HUMAN)

Names and origin

Protein names

Recommended name:
    Basal cell adhesion molecule
Alternative name(s):
    B-CAM cell surface glycoprotein
    Lutheran antigen
    Lutheran blood group glycoprotein
    Auberger B antigen
    F8/G253 antigen
    CD_antigen=CD239

Gene names

Name:	BCAM
Synonyms:	LU, MSK19

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	628 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Laminin alpha-5 receptor. May mediate intracellular signaling. Ref.8
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	LU is responsible for the Lutheran blood group system.
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.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane
Molecular function	Blood group antigen Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell-matrix adhesion Inferred from mutant phenotype. Source: UniProtKB signal transduction Ref.1 Traceable author statement. Source: ProtInc
Cellular component	external side of plasma membrane Inferred by curator. Source: UniProtKB integral to plasma membrane Ref.1 Traceable author statement. Source: ProtInc
Molecular function	laminin binding Inferred from mutant phenotype. Source: UniProtKB laminin receptor activity Inferred from mutant phenotype. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 31

31

Ref.1

Chain

32 – 628

597

Basal cell adhesion molecule

PRO_0000014850

Regions

Topological domain

32 – 547

516

Extracellular Potential

Transmembrane

548 – 568

21

Potential

Topological domain

569 – 628

60

Cytoplasmic Potential

Domain

32 – 142

111

Ig-like V-type 1

Domain

147 – 257

111

Ig-like V-type 2

Domain

274 – 355

82

Ig-like C2-type 1

Domain

363 – 441

79

Ig-like C2-type 2

Domain

448 – 541

94

Ig-like C2-type 3

Region

309 – 312

4

Interaction with laminin alpha5

Amino acid modifications

Modified residue

596

1

Phosphoserine; by GSK3 Ref.10

Modified residue

598

1

Phosphoserine; by CK2 Ref.10

Modified residue

621

1

Phosphoserine; by PKA Ref.10

Glycosylation

321

1

N-linked (GlcNAc...) Potential

Glycosylation

377

1

N-linked (GlcNAc...) Potential

Glycosylation

383

1

N-linked (GlcNAc...) Potential

Glycosylation

419

1

N-linked (GlcNAc...) Potential

Glycosylation

439

1

N-linked (GlcNAc...) Ref.9 Ref.11

Disulfide bond

53 ↔ 125

Ref.12

Disulfide bond

172 ↔ 237

Ref.12

Disulfide bond

291 ↔ 337

Probable

Disulfide bond

384 ↔ 424

Probable

Disulfide bond

473 ↔ 522

Probable

Natural variations

Natural variant

77

1

R → H: dbSNP rs28399653. Ref.2

VAR_021348

Natural variant

196

1

V → I: dbSNP rs28399654. Ref.2

VAR_021349

Natural variant

204

1

M → K: dbSNP rs28399656. Ref.2

VAR_021350

Natural variant

282

1

R → H: dbSNP rs9967601. Ref.2

VAR_021351

Natural variant

381

1

V → I: dbSNP rs28399626. Ref.2

VAR_021352

Natural variant

451

1

K → Q: dbSNP rs28399630. Ref.2

VAR_021353

Natural variant

539

1

T → A: dbSNP rs1135062. Ref.1 Ref.6 Ref.7

VAR_021354

Natural variant

581

1

Q → L: dbSNP rs28399659. Ref.2

VAR_021355

Experimental info

Mutagenesis

621

1

S → A: Dramatically reduced cell adhesion. Ref.10

Sequence conflict

225 – 226

2

RL → PC in CAA56327. Ref.6

Sequence conflict

355 – 356

2

EL → DV in CAA56327. Ref.6

Sequence conflict

532

1

R → L in ABY27636. Ref.7

Secondary structure

1

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628

Helix Strand Turn

Details...

Beta strand

39 – 44

6

Beta strand

49 – 51

3

Beta strand

60 – 69

10

Beta strand

77 – 84

8

Beta strand

87 – 92

6

Beta strand

110 – 114

5

Helix

117 – 119

3

Beta strand

121 – 128

8

Helix

130 – 132

3

Beta strand

134 – 145

12

Beta strand

151 – 154

4

Beta strand

167 – 179

13

Beta strand

182 – 187

6

Beta strand

200 – 210

11

Beta strand

216 – 224

9

Helix

228 – 232

5

Beta strand

234 – 242

9

Helix

244 – 246

3

Beta strand

248 – 252

5

Sequences

	Sequence		Length	Mass (Da)
	P50895-1 [UniParc]. Last modified March 7, 2006. Version 2. Checksum: C88F4F5C640C3F5B	FASTA	628	67,405
	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

References

	« Hide 'large scale' referencesShow '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: 7777537] [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. , 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: 15057824] [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. , 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: 15489334] [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: 7954395] [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]	"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: 9616226] [Abstract] Cited for: FUNCTION.
[9]	"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: 12754519] [Abstract] Cited for: GLYCOSYLATION AT ASN-439.
[10]	"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: 15975931] [Abstract] Cited for: PHOSPHORYLATION AT SER-596; SER-598 AND SER-621, MUTAGENESIS OF SER-621.
[11]	"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: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-439, MASS SPECTROMETRY. Tissue: Plasma.
[12]	"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: 17638854] [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.

IPI

IPI00002406.

PIR

I37202.
I38000.

RefSeq

NP_001013275.1.
NP_005572.2.

UniGene

Hs.625725

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PET	X-ray	1.70	A	32-262	[»]
2PF6	X-ray	2.20	A/B	32-262	[»]

SMR

P50895. Positions 40-429.

ModBase

Search...

Protein-protein interaction databases

STRING

P50895.

PTM databases

PhosphoSite

P50895.

Proteomic databases

PRIDE

P50895.

Genome annotation databases

Ensembl

ENST00000270233; ENSP00000270233; ENSG00000187244; Homo sapiens. [Genome view]

GeneID

4059.

KEGG

hsa:4059.

UCSC

uc002ozu.1. human.

Organism-specific databases

CTD

4059.

GeneCards

GC19P050005.

H-InvDB

HIX0027520.

HGNC

HGNC:6722. BCAM.

MIM

111200. gene+phenotype.

PharmGKB

PA30484.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12604.

HOVERGEN

P50895.

InParanoid

P50895.

OMA

HYPTEHV.

OrthoDB

EOG9VQD7Z.

PhylomeDB

P50895.

Gene expression databases

ArrayExpress

P50895.

Bgee

P50895.

CleanEx

HS_BCAM.

Genevestigator

P50895.

GermOnline

ENSG00000187244. Homo sapiens.

Family and domain databases

InterPro

IPR013162. CD80_C2-set.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 4 hits.

Pfam

PF08205. C2-set_2. 1 hit.
[Graphical view]

SMART

SM00409. IG. 2 hits.
SM00408. IGc2. 2 hits.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 5 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

15906.

SOURCE

Search...

Entry information

Entry name

BCAM_HUMAN

Accession

Primary (citable) accession number: P50895
Secondary accession number(s): A8MYF9 , A9YWT5, A9YWT6, Q86VC7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	March 7, 2006
Last modified:	January 19, 2010
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.