OPCM_RAT
ID OPCM_RAT Reviewed; 345 AA.
AC P32736; P32735; Q01653; Q01654;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 134.
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 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 TISSUE=Brain;
RX PubMed=1339369; DOI=10.1016/0378-1119(92)90734-7;
RA Lippman D.A., Lee N.M., Loh H.H.;
RT "Opioid-binding cell adhesion molecule (OBCAM)-related clones from a rat
RT brain cDNA library.";
RL Gene 117:249-254(1992).
RN [2]
RP PROTEIN SEQUENCE OF 33-40; 49-62; 72-87; 171-214; 218-228; 240-258; 263-271
RP AND 302-344, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [3]
RP PROTEIN SEQUENCE OF 195-214, AND GPI-ANCHOR.
RX PubMed=7891157; DOI=10.1523/jneurosci.15-03-02141.1995;
RA Struyk A.F., Canoll P.D., Wolfgang M.J., Rosen C.L., D'Eustachio P.,
RA Salzer J.L.;
RT "Cloning of neurotrimin defines a new subfamily of differentially expressed
RT neural cell adhesion molecules.";
RL J. Neurosci. 15:2141-2156(1995).
CC -!- FUNCTION: Binds opioids in the presence of acidic lipids; probably
CC involved in cell contact.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P32736-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P32736-2; Sequence=VSP_002612;
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. IgLON family.
CC {ECO:0000305}.
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DR EMBL; M88710; AAA40859.1; -; mRNA.
DR EMBL; M88711; AAA40860.1; -; mRNA.
DR EMBL; M88709; AAA40858.1; -; mRNA.
DR PIR; JC1238; JC1238.
DR PIR; JC1239; JC1239.
DR RefSeq; NP_446300.1; NM_053848.1. [P32736-1]
DR AlphaFoldDB; P32736; -.
DR SMR; P32736; -.
DR STRING; 10116.ENSRNOP00000044106; -.
DR GlyGen; P32736; 6 sites, 4 N-linked glycans (4 sites).
DR iPTMnet; P32736; -.
DR PhosphoSitePlus; P32736; -.
DR PaxDb; P32736; -.
DR PRIDE; P32736; -.
DR GeneID; 116597; -.
DR KEGG; rno:116597; -.
DR UCSC; RGD:620635; rat. [P32736-1]
DR CTD; 4978; -.
DR RGD; 620635; Opcml.
DR eggNOG; KOG3510; Eukaryota.
DR InParanoid; P32736; -.
DR OrthoDB; 583722at2759; -.
DR PhylomeDB; P32736; -.
DR Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR PRO; PR:P32736; -.
DR Proteomes; UP000002494; Unplaced.
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 Alternative splicing; Cell adhesion; Cell membrane;
KW Direct protein sequencing; 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_0000015122"
FT PROPEP 323..345
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000015123"
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"
FT VAR_SEQ 1..27
FT /note="MGVCGYLFLPWKCLVVVSLRLLFLVPT -> MYHPAYWIVFSATTALLFIP
FT (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_002612"
SQ SEQUENCE 345 AA; 38068 MW; A3181B0753F9658E CRC64;
MGVCGYLFLP WKCLVVVSLR LLFLVPTGVP VRSGDATFPK AMDNVTVRQG ESATLRCTID
DRVTRVAWLN RSTILYAGND KWSIDPRVII LVNTPTQYSI MIQNVDVYDE GPYTCSVQTD
NHPKTSRVHL IVQVPPQIMN ISSDITVNEI SSVTLLCLAI GRPEPTVTWR HLSVKEGQGF
VSEDEYLEIS DIKRDQSGEY ECSALNDVAA PDVRKVKITV NYPPYISKAK NTGVSVGQKG
ILSCEASAVP MAEFQWFKED TRLATGLDGV RIENKGRIST LTFFNVSEKD YGNYTCVATN
KLGNTNASIT LYGPGAVIDG VNSASRALAC LWLSGTFFAH FFIKF
