ID   OPCM_BOVIN              Reviewed;         345 AA.
AC   P11834;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Opioid-binding protein/cell adhesion molecule;
DE            Short=OBCAM;
DE            Short=OPCML;
DE            Short=Opioid-binding cell adhesion molecule;
DE   Flags: Precursor;
GN   Name=OPCML; Synonyms=OBCAM, OCAM;
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], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Brain;
RX   PubMed=2721489; DOI=10.1002/j.1460-2075.1989.tb03402.x;
RA   Schofield P.R., McFarland K.C., Hayflick J.S., Wilcox J.N., Cho T.M.,
RA   Roy S., Lee N.M., Loh H.H., Seeburg P.H.;
RT   "Molecular characterization of a new immunoglobulin superfamily protein
RT   with potential roles in opioid binding and cell contact.";
RL   EMBO J. 8:489-495(1989).
CC   -!- FUNCTION: Binds opioids in the presence of acidic lipids; probably
CC       involved in cell contact.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. IgLON family.
CC       {ECO:0000305}.
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DR   EMBL; X12672; CAA31192.1; -; mRNA.
DR   PIR; S03199; S03199.
DR   RefSeq; NP_776832.1; NM_174407.2.
DR   AlphaFoldDB; P11834; -.
DR   SMR; P11834; -.
DR   STRING; 9913.ENSBTAP00000027678; -.
DR   Ensembl; ENSBTAT00000027678; ENSBTAP00000027678; ENSBTAG00000020769.
DR   GeneID; 281957; -.
DR   KEGG; bta:281957; -.
DR   CTD; 4978; -.
DR   VEuPathDB; HostDB:ENSBTAG00000020769; -.
DR   VGNC; VGNC:32435; OPCML.
DR   eggNOG; KOG3510; Eukaryota.
DR   GeneTree; ENSGT00940000160304; -.
DR   InParanoid; P11834; -.
DR   OMA; FAGTEKW; -.
DR   OrthoDB; 583722at2759; -.
DR   Proteomes; UP000009136; Chromosome 29.
DR   Bgee; ENSBTAG00000020769; Expressed in prefrontal cortex and 45 other tissues.
DR   ExpressionAtlas; P11834; baseline and differential.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 3.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Pfam; PF07679; I-set; 2.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 3.
DR   SUPFAM; SSF48726; SSF48726; 3.
DR   PROSITE; PS50835; IG_LIKE; 3.
PE   1: Evidence at protein level;
KW   Cell adhesion; Cell membrane; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL          1..27
FT   CHAIN           28..322
FT                   /note="Opioid-binding protein/cell adhesion molecule"
FT                   /id="PRO_0000015116"
FT   PROPEP          323..345
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000015117"
FT   DOMAIN          39..126
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          136..219
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          223..310
FT                   /note="Ig-like C2-type 3"
FT   LIPID           322
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        306
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        57..115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        157..202
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        244..296
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   345 AA;  37914 MW;  D1ECC8D9E7D8CB19 CRC64;
     MGVCGSLFQP WKCLVVVSLR LLFLVPTGVP VRSGDATFPK AMDNVTVRQG ESATLRCTID
     DRVTRVAWLN RSTILYAGND KWSIDPRVII LVNTPTQYSI MIQNVDVYDE GPYTCSVQTD
     NHPKTSRVHL IVQVPPQIMN ISSDVTVNEG SSVTLLCLAI GRPEPTVTWR HLSVKEGQGF
     VSEDEYLEIS DIKRDQSGEY ECSALNDVAA PDVRKVKITV NYPPYISKAK NTGVSVGQKG
     ILSCEASAVP MAEFQWFKED TRLATGLDGM RIENKGHIST LTFFNVSEKD YGNYTCVATN
     KLGITNASIT LYGPGAVIDG VNSASRALAC LWLSGTLFAH FFIKF