OPCM_HUMAN
ID OPCM_HUMAN Reviewed; 345 AA.
AC Q14982; B2CZX2; B7ZLQ1; Q17RN7; Q7Z3W6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Opioid-binding protein/cell adhesion molecule;
DE Short=OBCAM;
DE Short=OPCML;
DE Short=Opioid-binding cell adhesion molecule;
DE AltName: Full=IgLON family member 1;
DE Flags: Precursor;
GN Name=OPCML; Synonyms=IGLON1, OBCAM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Occipital cortex;
RX PubMed=7721093; DOI=10.1016/0378-1119(94)00830-l;
RA Shark K.B., Lee N.M.;
RT "Cloning, sequencing and localization to chromosome 11 of a cDNA encoding a
RT human opioid-binding cell adhesion molecule (OBCAM).";
RL Gene 155:213-217(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RA Cui Y., Tao Q.;
RT "Multiple promoters and alternative splicing of OPCML.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain, and Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Brain, and Fetal brain;
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).
RN [7]
RP VARIANT OVARIAN CANCER ARG-95.
RX PubMed=12819783; DOI=10.1038/ng1183;
RA Sellar G.C., Watt K.P., Rabiasz G.J., Stronach E.A., Li L., Miller E.P.,
RA Massie C.E., Miller J., Contreras-Moreira B., Scott D., Brown I.,
RA Williams A.R., Bates P.A., Smyth J.F., Gabra H.;
RT "OPCML at 11q25 is epigenetically inactivated and has tumor-suppressor
RT function in epithelial ovarian cancer.";
RL Nat. Genet. 34:337-343(2003).
CC -!- FUNCTION: Binds opioids in the presence of acidic lipids; probably
CC involved in cell contact.
CC -!- INTERACTION:
CC Q14982; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-6447201, EBI-10171774;
CC Q14982; Q701N4: KRTAP5-2; NbExp=3; IntAct=EBI-6447201, EBI-11958178;
CC Q14982; Q8N1F7: NUP93; NbExp=3; IntAct=EBI-6447201, EBI-1042703;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q14982-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14982-2; Sequence=VSP_043440;
CC Name=3;
CC IsoId=Q14982-3; Sequence=VSP_047730;
CC Name=4;
CC IsoId=Q14982-4; Sequence=VSP_054155;
CC -!- DISEASE: Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer
CC defines malignancies originating from ovarian tissue. Although many
CC histologic types of ovarian tumors have been described, epithelial
CC ovarian carcinoma is the most common form. Ovarian cancers are often
CC asymptomatic and the recognized signs and symptoms, even of late-stage
CC disease, are vague. Consequently, most patients are diagnosed with
CC advanced disease. {ECO:0000269|PubMed:12819783}. Note=Disease
CC susceptibility is associated with variants affecting the gene
CC represented in this entry.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. IgLON family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/OPCMLID44423ch11q25.html";
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DR EMBL; L34774; AAA36387.1; -; mRNA.
DR EMBL; EU562296; ACB56656.1; -; mRNA.
DR EMBL; EU562297; ACB56657.1; -; mRNA.
DR EMBL; EU562299; ACB56659.1; -; mRNA.
DR EMBL; AK299908; BAG61748.1; -; mRNA.
DR EMBL; AK316491; BAH14862.1; -; mRNA.
DR EMBL; BX537377; CAD97619.1; -; mRNA.
DR EMBL; AP000843; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP004606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP004782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP005122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP005133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP005638; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC074773; AAH74773.1; -; mRNA.
DR EMBL; BC117254; AAI17255.1; -; mRNA.
DR EMBL; BC126251; AAI26252.1; -; mRNA.
DR EMBL; BC143946; AAI43947.1; -; mRNA.
DR CCDS; CCDS31722.1; -. [Q14982-2]
DR CCDS; CCDS81649.1; -. [Q14982-3]
DR CCDS; CCDS8492.1; -. [Q14982-1]
DR PIR; JC4025; JC4025.
DR RefSeq; NP_001012393.1; NM_001012393.2. [Q14982-2]
DR RefSeq; NP_001306032.1; NM_001319103.1. [Q14982-4]
DR RefSeq; NP_001306033.1; NM_001319104.1.
DR RefSeq; NP_001306034.1; NM_001319105.1. [Q14982-3]
DR RefSeq; NP_001306035.1; NM_001319106.1.
DR RefSeq; NP_002536.1; NM_002545.4. [Q14982-1]
DR RefSeq; XP_011541158.1; XM_011542856.2. [Q14982-3]
DR PDB; 5UV6; X-ray; 2.65 A; A/B=36-316.
DR PDBsum; 5UV6; -.
DR AlphaFoldDB; Q14982; -.
DR SMR; Q14982; -.
DR BioGRID; 111026; 18.
DR IntAct; Q14982; 14.
DR STRING; 9606.ENSP00000330862; -.
DR GlyGen; Q14982; 6 sites.
DR iPTMnet; Q14982; -.
DR PhosphoSitePlus; Q14982; -.
DR BioMuta; OPCML; -.
DR DMDM; 2497326; -.
DR jPOST; Q14982; -.
DR MassIVE; Q14982; -.
DR MaxQB; Q14982; -.
DR PaxDb; Q14982; -.
DR PeptideAtlas; Q14982; -.
DR PRIDE; Q14982; -.
DR ProteomicsDB; 3410; -.
DR ProteomicsDB; 60274; -. [Q14982-1]
DR ProteomicsDB; 60275; -. [Q14982-2]
DR ProteomicsDB; 7231; -.
DR Antibodypedia; 53494; 218 antibodies from 29 providers.
DR DNASU; 4978; -.
DR Ensembl; ENST00000331898.11; ENSP00000330862.7; ENSG00000183715.14. [Q14982-1]
DR Ensembl; ENST00000374778.4; ENSP00000363910.4; ENSG00000183715.14. [Q14982-3]
DR Ensembl; ENST00000524381.6; ENSP00000434750.1; ENSG00000183715.14. [Q14982-2]
DR Ensembl; ENST00000541867.5; ENSP00000445496.1; ENSG00000183715.14. [Q14982-4]
DR Ensembl; ENST00000612177.4; ENSP00000482061.1; ENSG00000183715.14. [Q14982-1]
DR GeneID; 4978; -.
DR KEGG; hsa:4978; -.
DR MANE-Select; ENST00000524381.6; ENSP00000434750.1; NM_001012393.5; NP_001012393.1. [Q14982-2]
DR UCSC; uc001qgs.4; human. [Q14982-1]
DR CTD; 4978; -.
DR DisGeNET; 4978; -.
DR GeneCards; OPCML; -.
DR HGNC; HGNC:8143; OPCML.
DR HPA; ENSG00000183715; Group enriched (brain, parathyroid gland, retina).
DR MalaCards; OPCML; -.
DR MIM; 167000; phenotype.
DR MIM; 600632; gene.
DR neXtProt; NX_Q14982; -.
DR OpenTargets; ENSG00000183715; -.
DR PharmGKB; PA31930; -.
DR VEuPathDB; HostDB:ENSG00000183715; -.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000160304; -.
DR HOGENOM; CLU_027228_2_2_1; -.
DR InParanoid; Q14982; -.
DR OMA; FAGTEKW; -.
DR OrthoDB; 583722at2759; -.
DR PhylomeDB; Q14982; -.
DR TreeFam; TF325565; -.
DR PathwayCommons; Q14982; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR SignaLink; Q14982; -.
DR BioGRID-ORCS; 4978; 6 hits in 1069 CRISPR screens.
DR ChiTaRS; OPCML; human.
DR GeneWiki; OPCML; -.
DR GenomeRNAi; 4978; -.
DR Pharos; Q14982; Tbio.
DR PRO; PR:Q14982; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q14982; protein.
DR Bgee; ENSG00000183715; Expressed in Brodmann (1909) area 23 and 142 other tissues.
DR ExpressionAtlas; Q14982; baseline and differential.
DR Genevisible; Q14982; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0008038; P:neuron recognition; TAS:ProtInc.
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 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Disease variant; 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_0000015118"
FT PROPEP 323..345
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000015119"
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..41
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_047730"
FT VAR_SEQ 1..27
FT /note="MGVCGYLFLPWKCLVVVSLRLLFLVPT -> MYHPAYWVVFSATTALLFIP
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.2"
FT /id="VSP_043440"
FT VAR_SEQ 312
FT /note="Y -> YEISPSSAVA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054155"
FT VARIANT 95
FT /note="P -> R (in ovarian cancer; somatic mutation;
FT dbSNP:rs137852691)"
FT /evidence="ECO:0000269|PubMed:12819783"
FT /id="VAR_055421"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:5UV6"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:5UV6"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:5UV6"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:5UV6"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:5UV6"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:5UV6"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:5UV6"
FT STRAND 111..121
FT /evidence="ECO:0007829|PDB:5UV6"
FT STRAND 127..141
FT /evidence="ECO:0007829|PDB:5UV6"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:5UV6"
FT STRAND 153..163
FT /evidence="ECO:0007829|PDB:5UV6"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:5UV6"
FT STRAND 180..191
FT /evidence="ECO:0007829|PDB:5UV6"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:5UV6"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:5UV6"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:5UV6"
FT STRAND 212..228
FT /evidence="ECO:0007829|PDB:5UV6"
FT STRAND 240..250
FT /evidence="ECO:0007829|PDB:5UV6"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:5UV6"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:5UV6"
FT STRAND 276..285
FT /evidence="ECO:0007829|PDB:5UV6"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:5UV6"
FT STRAND 292..300
FT /evidence="ECO:0007829|PDB:5UV6"
FT STRAND 303..312
FT /evidence="ECO:0007829|PDB:5UV6"
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
