OX2G_RAT
ID OX2G_RAT Reviewed; 278 AA.
AC P04218;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=OX-2 membrane glycoprotein;
DE AltName: Full=MRC OX-2 antigen;
DE AltName: CD_antigen=CD200;
DE Flags: Precursor;
GN Name=Cd200; Synonyms=Mox2;
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].
RX PubMed=2862025; DOI=10.1002/j.1460-2075.1985.tb02324.x;
RA Clark M.J., Gagnon J., Williams A.F., Barclay A.N.;
RT "MRC OX-2 antigen: a lymphoid/neuronal membrane glycoprotein with a
RT structure like a single immunoglobulin light chain.";
RL EMBO J. 4:113-118(1985).
CC -!- FUNCTION: Costimulates T-cell proliferation. May regulate myeloid cell
CC activity in a variety of tissues.
CC -!- SUBUNIT: CD200 and CD200R1 interact via their respective N-terminal Ig-
CC like domains.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Found on the surface of neurons, thymocytes, B-
CC cells and follicular dendritic cells.
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DR EMBL; X01785; CAA25925.1; -; mRNA.
DR PIR; A02114; TDRTOX.
DR AlphaFoldDB; P04218; -.
DR SMR; P04218; -.
DR IntAct; P04218; 2.
DR MINT; P04218; -.
DR STRING; 10116.ENSRNOP00000055253; -.
DR GlyGen; P04218; 6 sites.
DR PaxDb; P04218; -.
DR PRIDE; P04218; -.
DR UCSC; RGD:3104; rat.
DR RGD; 3104; Cd200.
DR eggNOG; ENOG502S5DU; Eukaryota.
DR InParanoid; P04218; -.
DR PhylomeDB; P04218; -.
DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR PRO; PR:P04218; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0009986; C:cell surface; IDA:ARUK-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IDA:ARUK-UCL.
DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; IPI:ARUK-UCL.
DR GO; GO:0098609; P:cell-cell adhesion; IGI:ARUK-UCL.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IGI:ARUK-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IGI:ARUK-UCL.
DR GO; GO:0043031; P:negative regulation of macrophage activation; ISO:RGD.
DR GO; GO:1905522; P:negative regulation of macrophage migration; IGI:ARUK-UCL.
DR GO; GO:1904465; P:negative regulation of matrix metallopeptidase secretion; ISO:RGD.
DR GO; GO:0150079; P:negative regulation of neuroinflammatory response; IGI:ARUK-UCL.
DR GO; GO:1901215; P:negative regulation of neuron death; IGI:ARUK-UCL.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR GO; GO:2000405; P:negative regulation of T cell migration; IGI:ARUK-UCL.
DR GO; GO:0150072; P:positive regulation of arginase activity; ISO:RGD.
DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; ISO:RGD.
DR GO; GO:0150074; P:positive regulation of protein-glutamine gamma-glutamyltransferase activity; ISO:RGD.
DR GO; GO:0071636; P:positive regulation of transforming growth factor beta production; ISO:RGD.
DR GO; GO:0050776; P:regulation of immune response; IEA:InterPro.
DR GO; GO:0150077; P:regulation of neuroinflammatory response; IGI:ARUK-UCL.
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; 2.
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..278
FT /note="OX-2 membrane glycoprotein"
FT /id="PRO_0000015126"
FT TOPO_DOM 31..232
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..278
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 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 278 AA; 31088 MW; B5A72DBE7B3116CD CRC64;
MGSPVFRRPF CHLSTYSLLW AIAAVALSTA QVEVVTQDER KLLHTTASLR CSLKTTQEPL
IVTWQKKKAV GPENMVTYSK AHGVVIQPTY KDRINITELG LLNTSITFWN TTLDDEGCYM
CLFNMFGSGK VSGTACLTLY VQPIVHLHYN YFEDHLNITC SATARPAPAI SWKGTGSGIE
NSTESHSHSN GTTSVTSILR VKDPKTQVGK EVICQVLYLG NVIDYKQSLD KGFWFSVPLL
LSIVSLVILL VLISILLYWK RHRNQERGES SQGMQRMK
