BCAM_RAT
ID BCAM_RAT Reviewed; 624 AA.
AC Q9ESS6;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
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; Synonyms=Lu;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Heart;
RA Taira E., Okumura S., Miki N.;
RT "Rat Lutheran antigen.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; AB035510; BAB16052.1; -; mRNA.
DR EMBL; CH473979; EDM08138.1; -; Genomic_DNA.
DR EMBL; BC072479; AAH72479.1; -; mRNA.
DR RefSeq; NP_113940.1; NM_031752.2.
DR AlphaFoldDB; Q9ESS6; -.
DR SMR; Q9ESS6; -.
DR BioGRID; 249366; 1.
DR IntAct; Q9ESS6; 1.
DR MINT; Q9ESS6; -.
DR STRING; 10116.ENSRNOP00000047809; -.
DR GlyGen; Q9ESS6; 3 sites.
DR iPTMnet; Q9ESS6; -.
DR PhosphoSitePlus; Q9ESS6; -.
DR jPOST; Q9ESS6; -.
DR PaxDb; Q9ESS6; -.
DR PRIDE; Q9ESS6; -.
DR Ensembl; ENSRNOT00000045574; ENSRNOP00000047809; ENSRNOG00000029399.
DR GeneID; 78958; -.
DR KEGG; rno:78958; -.
DR UCSC; RGD:68378; rat.
DR CTD; 4059; -.
DR RGD; 68378; Bcam.
DR eggNOG; ENOG502QWC8; Eukaryota.
DR GeneTree; ENSGT00940000161038; -.
DR HOGENOM; CLU_028888_1_0_1; -.
DR InParanoid; Q9ESS6; -.
DR OMA; CCRRREK; -.
DR OrthoDB; 864786at2759; -.
DR PhylomeDB; Q9ESS6; -.
DR TreeFam; TF330534; -.
DR PRO; PR:Q9ESS6; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000029399; Expressed in lung and 19 other tissues.
DR Genevisible; Q9ESS6; RN.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0043236; F:laminin binding; ISO:RGD.
DR GO; GO:0005055; F:laminin receptor activity; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
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; 3.
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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..624
FT /note="Basal cell adhesion molecule"
FT /id="PRO_0000383339"
FT TOPO_DOM 26..543
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 565..624
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..136
FT /note="Ig-like V-type 1"
FT DOMAIN 141..251
FT /note="Ig-like V-type 2"
FT DOMAIN 268..343
FT /note="Ig-like C2-type 1"
FT DOMAIN 357..436
FT /note="Ig-like C2-type 2"
FT DOMAIN 443..534
FT /note="Ig-like C2-type 3"
FT REGION 477..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50895"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50895"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50895"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
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 47..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 166..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 285..331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 379..419
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 468..518
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 624 AA; 67512 MW; 129A40A015ECE119 CRC64;
MEPPDARAGL LWLTLLLSGY SGAQAELHVS VPPRVEVMRG EQIALDCTPR EHPENYVLEW
LLVDASGARH RLASVEPQGS EFLGTIHNSR GRRPPYKIDS LGRLVIAEAQ VGDERDYVCV
VKAGAAGTSE ATSSVRVFAT PEATEVAPNK GTLSVMEQFA QEIATCSSNN GNPVPRITWY
QNGQRLDVPM ELNSKGYMTS RTVREASGLY SLTSTLYLRL HKEDRDASFH CAAHYDLPSG
QHGRLDSHTF RLTLHYPTEH VEFWVGSPST TEGWVREGDA VQLLCQGDGS PSPEYSFFRE
QGNQEEQLNV NLKGNLTLEG VHRSQSGIYG CRVEDYDADE EVQLVKKLKL HVAYLDPLEL
SVPEEFSVFL NSSGTVVNCS ARGLPAPIVR WTKDSVTVAD GPILSLDSVT FDSAGTYTCE
ASTPTVPLLS RTQSFQLVVQ GAPELKPNEI KPKSGTSWTE GDEVMLTCSA RGFPEPKLTW
SQRGDTTPAE PPFEGRGWMS SSLTLKVTSA LSREGVSCEA SNIHGKNGHV FHFGSVAPQT
AQAGVAVMAV AVSVGLLLLV VAAFYCMRRK GRPGCCQRAE KGAPPAREPE LSHSGSERPE
HTGLLMGGPS GGGRGGNGGF GDEC
