OX2G_PONAB
ID OX2G_PONAB Reviewed; 269 AA.
AC Q5RAL8;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=OX-2 membrane glycoprotein;
DE AltName: CD_antigen=CD200;
DE Flags: Precursor;
GN Name=CD200;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Costimulates T-cell proliferation. May regulate myeloid cell
CC activity in a variety of tissues (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: CD200 and CD200R1 interact via their respective N-terminal Ig-
CC like domains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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DR EMBL; CR858997; CAH91192.1; -; mRNA.
DR RefSeq; NP_001125699.1; NM_001132227.1.
DR AlphaFoldDB; Q5RAL8; -.
DR SMR; Q5RAL8; -.
DR STRING; 9601.ENSPPYP00000015150; -.
DR GeneID; 100172623; -.
DR KEGG; pon:100172623; -.
DR CTD; 4345; -.
DR eggNOG; ENOG502S5DU; Eukaryota.
DR InParanoid; Q5RAL8; -.
DR OrthoDB; 1161268at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043031; P:negative regulation of macrophage activation; IEA:InterPro.
DR GO; GO:0050776; P:regulation of immune response; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR033321; CD200.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR013151; Immunoglobulin.
DR PANTHER; PTHR46841:SF3; PTHR46841:SF3; 1.
DR Pfam; PF00047; ig; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..269
FT /note="OX-2 membrane glycoprotein"
FT /id="PRO_0000250714"
FT TOPO_DOM 31..236
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..141
FT /note="Ig-like V-type"
FT DOMAIN 142..232
FT /note="Ig-like C2-type"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 118..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 160..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 269 AA; 30265 MW; 49B0860A070191AC CRC64;
MERLVIRMPF CHLSTYSLVW VMAAVVLCTA QVQVVTQDER EQLYTPASLK CSLQNAQEAL
IVTWQKKKAV SPENMVTFSE NHGVVIQPAY KDKINIAQLG LQNSTITFWN ITLEDEGCYM
CLFNTFGFGK ISGTACLTVY VQPIVSLHYK FSEDHLNTTC SATARPAPMV FWKVPRSGIE
NSTVTLSHPN GTTSVTSILH IKDPKNQVGK EAICQVLHLG TVTDFKQTVN KGYWFSVPLL
LSIVSLVTLL VLISILLYWK RHRNQDREP
