ID   OBCAM_CHICK             Reviewed;         337 AA.
AC   Q98892;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Opioid-binding protein/cell adhesion molecule homolog;
DE   AltName: Full=Neurite inhibitor GP55-A;
DE   AltName: Full=OBCAM protein gamma isoform;
DE   Flags: Precursor;
GN   Name=OPCML;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Lodge A.P., Kim D.-S., Howard M.R., McNamee C.J., Smith N., Moss D.J.;
RT   "Cloning of CEPU-s, a secreted isoform of CEPU-1, and OBCAM cDNAs from
RT   chick: structural diversity of IgLON family proteins.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 64-337, AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Brain;
RX   PubMed=9004047; DOI=10.1242/jcs.109.13.3129;
RA   Wilson D.J.A., Kim D.-S., Clarke G.A., Marshall-Clarke S., Moss D.J.;
RT   "A family of glycoproteins (GP55), which inhibit neurite outgrowth, are
RT   members of the Ig superfamily and are related to OBCAM, neurotrimin, LAMP
RT   and CEPU-1.";
RL   J. Cell Sci. 109:3129-3138(1996).
CC   -!- FUNCTION: Inhibits neurite outgrowth.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC   -!- TISSUE SPECIFICITY: Restricted to the nervous system.
CC   -!- DEVELOPMENTAL STAGE: Increases during development from very low levels
CC       at embryonic day 10 and is most abundant after hatching.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. IgLON family.
CC       {ECO:0000305}.
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DR   EMBL; Y08170; CAB41420.1; -; mRNA.
DR   AlphaFoldDB; Q98892; -.
DR   SMR; Q98892; -.
DR   STRING; 9031.ENSGALP00000033890; -.
DR   VEuPathDB; HostDB:geneid_395422; -.
DR   eggNOG; KOG3510; Eukaryota.
DR   InParanoid; Q98892; -.
DR   PhylomeDB; Q98892; -.
DR   Proteomes; UP000000539; 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   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..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..314
FT                   /note="Opioid-binding protein/cell adhesion molecule
FT                   homolog"
FT                   /id="PRO_0000015063"
FT   PROPEP          315..337
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000015064"
FT   DOMAIN          32..119
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          129..211
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          215..302
FT                   /note="Ig-like C2-type 3"
FT   LIPID           314
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        277
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        298
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..108
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        150..194
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        236..288
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   337 AA;  36887 MW;  BAE717551856651E CRC64;
     MYHPACWIVF TATTALLFIP GVPVRSGDAT FPKAMDNVTV RQGESATLRC TVDDRVRRVA
     WLNRSTILYA GNDKWSIDNR VVILSNTKTQ YSIKIHNVDV YDEGPYTCSV QTDNHPKTSR
     VHLIVQVPPQ IVNISSDITV NEGSSVTLMC LAFGRPEPTV TWRHLSGKGQ GFVSEDEYLE
     ITGITREQSG EYECSAVNDV AVPDVRKVKV TVNYPPYISN AKNTGASVGQ KGILQCEASA
     VPVAEFQWFK EDTRLANGLE GVRIESKGRL STLTFFNVSE KDYGNYTCVA TNKLGNTNAS
     IILYGPGAVH DSGNAASRAA AGLCLWATLL ARLLLDF