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   24-JAN-2024, entry version 149.
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   GlyCosmos; Q9MZ08; 3 sites, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000012495; -.
DR   PeptideAtlas; Q9MZ08; -.
DR   Ensembl; ENSBTAT00000012495.4; ENSBTAP00000012495.3; ENSBTAG00000009495.4.
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; GYMTIRT; -.
DR   OrthoDB; 4211322at2759; -.
DR   TreeFam; TF330534; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000009495; Expressed in thyroid gland and 102 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005055; F:laminin receptor activity; IBA:GO_Central.
DR   CDD; cd00096; Ig; 3.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   PANTHER; PTHR11973:SF17; BASAL CELL ADHESION MOLECULE; 1.
DR   PANTHER; PTHR11973; CELL SURFACE GLYCOPROTEIN MUC18-RELATED; 1.
DR   Pfam; PF08205; C2-set_2; 1.
DR   Pfam; PF13927; Ig_3; 3.
DR   SMART; SM00409; IG; 5.
DR   SMART; SM00408; IGc2; 4.
DR   SUPFAM; SSF48726; Immunoglobulin; 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
//