BCAM_BOVIN
ID BCAM_BOVIN Reviewed; 628 AA.
AC Q9MZ08;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Basal cell adhesion molecule;
DE AltName: Full=B-CAM cell surface glycoprotein;
DE AltName: Full=Lutheran antigen;
DE AltName: CD_antigen=CD239;
DE Flags: Precursor;
GN Name=BCAM;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12096143; DOI=10.1074/mcp.t100008-mcp200;
RA Shusta E.V., Boado R.J., Pardridge W.M.;
RT "Vascular proteomics and subtractive antibody expression cloning.";
RL Mol. Cell. Proteomics 1:75-82(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10908043; DOI=10.1097/00004647-200007000-00009;
RA Boado R.J., Li J.Y., Pardridge W.M.;
RT "Selective Lutheran glycoprotein gene expression at the blood-brain barrier
RT in normal brain and in human brain tumors.";
RL J. Cereb. Blood Flow Metab. 20:1096-1102(2000).
CC -!- FUNCTION: Laminin alpha-5 receptor. May mediate intracellular signaling
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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DR EMBL; AF270512; AAF81749.2; -; mRNA.
DR EMBL; BC123496; AAI23497.1; -; mRNA.
DR RefSeq; NP_777166.1; NM_174741.2.
DR AlphaFoldDB; Q9MZ08; -.
DR SMR; Q9MZ08; -.
DR STRING; 9913.ENSBTAP00000012495; -.
DR PaxDb; Q9MZ08; -.
DR PeptideAtlas; Q9MZ08; -.
DR PRIDE; Q9MZ08; -.
DR Ensembl; ENSBTAT00000012495; ENSBTAP00000012495; ENSBTAG00000009495.
DR GeneID; 282862; -.
DR KEGG; bta:282862; -.
DR CTD; 4059; -.
DR VEuPathDB; HostDB:ENSBTAG00000009495; -.
DR VGNC; VGNC:49138; BCAM.
DR eggNOG; ENOG502QWC8; Eukaryota.
DR GeneTree; ENSGT00940000161038; -.
DR HOGENOM; CLU_028888_1_0_1; -.
DR InParanoid; Q9MZ08; -.
DR OMA; CCRRREK; -.
DR OrthoDB; 864786at2759; -.
DR TreeFam; TF330534; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000009495; Expressed in thyroid gland and 102 other tissues.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043236; F:laminin binding; IEA:Ensembl.
DR GO; GO:0005055; F:laminin receptor activity; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 2: Evidence at transcript level;
KW Cell adhesion; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000250"
FT CHAIN 32..628
FT /note="Basal cell adhesion molecule"
FT /id="PRO_0000383337"
FT TOPO_DOM 32..547
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..628
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..142
FT /note="Ig-like V-type 1"
FT DOMAIN 150..253
FT /note="Ig-like V-type 2"
FT DOMAIN 254..355
FT /note="Ig-like C2-type 1"
FT DOMAIN 355..441
FT /note="Ig-like C2-type 2"
FT DOMAIN 448..538
FT /note="Ig-like C2-type 3"
FT REGION 580..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50895"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50895"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50895"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50895"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 172..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 291..337
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 384..424
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 473..522
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 628 AA; 68003 MW; 2128B1F1B73E6A93 CRC64;
MEPPDARAGA RRAPRLLVLA LLLAAPPGSK AEVRLSVPPL VEVMRGESVT LDCSPLGTHD
YFMLEWFLVD RSGARHRLAS AELRGSELRD KELNSRGRSP PYQLDSQGRL VLPEAQVGDE
RDYVCVVKAG AAGTAEATAR LKVFAKPEAP EVSPNKGILS VMDDFAQEIA TCSSRNGNPA
PQIMWYRNGQ PLAVPLEVNS EGYMTTRTVR EASGLLSLTS TLYLRLHKPD REASFHCSVH
YYLPAGQHGR LDGPSFSLTL HYPTEHVLFW LGSQSTAEGW VREGDSVQLL CQGDGSPTPE
YTFFWLQDKQ EDVLKTSLEG NLTLERVQRN QSGTYGCRVE DFDVPEDAEL SKTLELRVAY
LDSLELSAGE ELSLPLHNST TVTCSARGLP TPTLYWTKDS APMGEDPTLS LHSVTFDSAG
TYTCEAYMPR IPLLSRTRSF RLLVQGTPEL KAKETQPKAE GSWTEGDEVT LICYARGYPK
PKLTWSQLGG SPTEPAPGGQ GWVSSSLTLK VTSALSQDGV SCEASNPLGN THHVFHFGTV
APQTSQAGVA VMAVAISVAL LLLVVAVFYC MRRKGRPGCC QWGEKGSPPP GEPKLSHSGS
QRPEQTGLLM GSASGGAKHG SGGFGDEC
