ID   OPCM_PANTR              Reviewed;         345 AA.
AC   Q5IS61;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
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;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA   Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA   Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT   "Accelerated evolution of nervous system genes in the origin of Homo
RT   sapiens.";
RL   Cell 119:1027-1040(2004).
CC   -!- FUNCTION: Binds opioids in the presence of acidic lipids; probably
CC       involved in cell contact. {ECO:0000250}.
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; AY665267; AAV74305.1; -; mRNA.
DR   RefSeq; NP_001012438.1; NM_001012436.1.
DR   AlphaFoldDB; Q5IS61; -.
DR   SMR; Q5IS61; -.
DR   STRING; 9598.ENSPTRP00000007679; -.
DR   PaxDb; Q5IS61; -.
DR   Ensembl; ENSPTRT00000008316; ENSPTRP00000007679; ENSPTRG00000004489.
DR   GeneID; 466855; -.
DR   KEGG; ptr:466855; -.
DR   CTD; 4978; -.
DR   eggNOG; KOG3510; Eukaryota.
DR   GeneTree; ENSGT00940000160304; -.
DR   HOGENOM; CLU_027228_2_2_1; -.
DR   InParanoid; Q5IS61; -.
DR   OMA; FAGTEKW; -.
DR   OrthoDB; 583722at2759; -.
DR   TreeFam; TF325565; -.
DR   Proteomes; UP000002277; Chromosome 11.
DR   Bgee; ENSPTRG00000004489; Expressed in temporal lobe and 11 other tissues.
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   2: Evidence at transcript level;
KW   Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Immunoglobulin domain; Lipoprotein; Membrane; Reference proteome; Repeat;
KW   Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000250"
FT   CHAIN           28..322
FT                   /note="Opioid-binding protein/cell adhesion molecule"
FT                   /id="PRO_0000015120"
FT   PROPEP          323..345
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000015121"
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:0000255"
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:0000255"
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;  38008 MW;  E7AD17BEA1AA3FF4 CRC64;
     MGVCGYLFLP WKCLVVVSLR LLFLVPTGVP VRSGDATFPK AMDNVTVRQG ESATLRCTID
     DRVTRVAWLN RSTILYAGND KWSIDPRVII LVNTPTQYSI MIQNVDVYDE GPYTCSVQTD
     NHPKTSRVHL IVQVPPQIMN ISSDITVNEG SSVTLLCLAI GRPEPTVTWR HLSVKEGQGF
     VSEDEYLEIS DIKRDQSGEY ECSALNDVAA PDVRKVKITV NYPPYISKAK NTGVSVGQKG
     ILSCEASAVP MAEFQWFKEE TRLATGLDGM RIENKGRMST LTFFNVSEKD YGNYTCVATN
     KLGNTNASIT LYGPGAVIDG VNSASRALAC LWLSGTLLAH FFIKF