OX2G_HUMAN
ID OX2G_HUMAN Reviewed; 278 AA.
AC P41217; B3KQI1; B4DLW9; D3DN65; Q6J2Q6; Q6PIQ4; Q8TB85; Q9H3J3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 4.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=OX-2 membrane glycoprotein;
DE AltName: CD_antigen=CD200;
DE Flags: Precursor;
GN Name=CD200; Synonyms=MOX1, MOX2; ORFNames=My033;
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 2), AND VARIANT CYS-11.
RA Hou Z.F., Gao S., Zheng Y.C., Hao B., Wang W.Z., Bu L.S., Yang S.J.,
RA Hou R.Z., Gao S.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain;
RA Mao Y.M., Xie Y., Zheng Z.H.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT CYS-11.
RC TISSUE=Brain;
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), AND VARIANT CYS-11.
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT CYS-11.
RC TISSUE=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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-278 (ISOFORM 1), AND VARIANT THR-46.
RC TISSUE=Blood;
RX PubMed=3032785; DOI=10.1007/bf00404426;
RA McCaughan G.W., Clark M.J., Barclay A.N.;
RT "Characterization of the human homolog of the rat MRC OX-2 membrane
RT glycoprotein.";
RL Immunogenetics 25:329-335(1987).
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 -!- INTERACTION:
CC P41217; Q8TD46: CD200R1; NbExp=2; IntAct=EBI-3910563, EBI-4314412;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P41217-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P41217-2; Sequence=VSP_002613;
CC Name=3;
CC IsoId=P41217-3; Sequence=VSP_040027, VSP_002613;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CD200ID44381ch3q13.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY603771; AAT37533.1; -; mRNA.
DR EMBL; AF063591; AAG43150.1; -; mRNA.
DR EMBL; AK297194; BAG59681.1; -; mRNA.
DR EMBL; AK074972; BAG52043.1; -; mRNA.
DR EMBL; AC112487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79672.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79676.1; -; Genomic_DNA.
DR EMBL; BC022522; AAH22522.1; -; mRNA.
DR EMBL; BC031103; AAH31103.1; -; mRNA.
DR EMBL; X05323; CAA28943.1; -; Genomic_DNA.
DR EMBL; X05324; CAA28943.1; JOINED; Genomic_DNA.
DR EMBL; X05325; CAA28943.1; JOINED; Genomic_DNA.
DR EMBL; X05326; CAA28943.1; JOINED; Genomic_DNA.
DR CCDS; CCDS2965.1; -. [P41217-2]
DR CCDS; CCDS33818.1; -. [P41217-3]
DR PIR; A47639; A47639.
DR RefSeq; NP_001004196.2; NM_001004196.3. [P41217-3]
DR RefSeq; NP_001305757.1; NM_001318828.1.
DR RefSeq; NP_005935.4; NM_005944.6. [P41217-2]
DR RefSeq; XP_005247539.1; XM_005247482.2.
DR AlphaFoldDB; P41217; -.
DR SMR; P41217; -.
DR BioGRID; 110486; 8.
DR IntAct; P41217; 2.
DR STRING; 9606.ENSP00000420298; -.
DR ChEMBL; CHEMBL3712870; -.
DR GlyGen; P41217; 7 sites.
DR iPTMnet; P41217; -.
DR PhosphoSitePlus; P41217; -.
DR BioMuta; CD200; -.
DR DMDM; 311033489; -.
DR EPD; P41217; -.
DR jPOST; P41217; -.
DR MassIVE; P41217; -.
DR MaxQB; P41217; -.
DR PaxDb; P41217; -.
DR PeptideAtlas; P41217; -.
DR PRIDE; P41217; -.
DR ProteomicsDB; 55419; -. [P41217-1]
DR ProteomicsDB; 55420; -. [P41217-2]
DR ProteomicsDB; 55421; -. [P41217-3]
DR TopDownProteomics; P41217-3; -. [P41217-3]
DR ABCD; P41217; 9 sequenced antibodies.
DR Antibodypedia; 16297; 979 antibodies from 41 providers.
DR DNASU; 4345; -.
DR Ensembl; ENST00000315711.12; ENSP00000312766.8; ENSG00000091972.18. [P41217-2]
DR Ensembl; ENST00000473539.5; ENSP00000420298.1; ENSG00000091972.18. [P41217-3]
DR GeneID; 4345; -.
DR KEGG; hsa:4345; -.
DR MANE-Select; ENST00000315711.12; ENSP00000312766.8; NM_005944.7; NP_005935.4. [P41217-2]
DR UCSC; uc003dyw.4; human. [P41217-1]
DR CTD; 4345; -.
DR DisGeNET; 4345; -.
DR GeneCards; CD200; -.
DR HGNC; HGNC:7203; CD200.
DR HPA; ENSG00000091972; Low tissue specificity.
DR MIM; 155970; gene.
DR neXtProt; NX_P41217; -.
DR OpenTargets; ENSG00000091972; -.
DR PharmGKB; PA30911; -.
DR VEuPathDB; HostDB:ENSG00000091972; -.
DR eggNOG; ENOG502S5DU; Eukaryota.
DR GeneTree; ENSGT00530000063970; -.
DR InParanoid; P41217; -.
DR OMA; MISWKVS; -.
DR OrthoDB; 1161268at2759; -.
DR PhylomeDB; P41217; -.
DR TreeFam; TF334493; -.
DR PathwayCommons; P41217; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; P41217; -.
DR BioGRID-ORCS; 4345; 4 hits in 1062 CRISPR screens.
DR ChiTaRS; CD200; human.
DR GeneWiki; CD200; -.
DR GenomeRNAi; 4345; -.
DR Pharos; P41217; Tbio.
DR PRO; PR:P41217; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P41217; protein.
DR Bgee; ENSG00000091972; Expressed in cortical plate and 181 other tissues.
DR ExpressionAtlas; P41217; baseline and differential.
DR Genevisible; P41217; HS.
DR GO; GO:0030424; C:axon; IDA:ARUK-UCL.
DR GO; GO:0044297; C:cell body; IDA:ARUK-UCL.
DR GO; GO:0009986; C:cell surface; IDA:ARUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; NAS:ARUK-UCL.
DR GO; GO:0043005; C:neuron projection; ISS:ARUK-UCL.
DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0140081; F:glycosylated region protein binding; TAS:ARUK-UCL.
DR GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; ISS:ARUK-UCL.
DR GO; GO:0098609; P:cell-cell adhesion; ISS: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; ISS:ARUK-UCL.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISS:ARUK-UCL.
DR GO; GO:0002695; P:negative regulation of leukocyte activation; TAS:ARUK-UCL.
DR GO; GO:0043031; P:negative regulation of macrophage activation; ISS:ARUK-UCL.
DR GO; GO:1905522; P:negative regulation of macrophage migration; ISS:ARUK-UCL.
DR GO; GO:1904465; P:negative regulation of matrix metallopeptidase secretion; IDA:ARUK-UCL.
DR GO; GO:0150079; P:negative regulation of neuroinflammatory response; ISS:ARUK-UCL.
DR GO; GO:1901215; P:negative regulation of neuron death; ISS:ARUK-UCL.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:ARUK-UCL.
DR GO; GO:2000405; P:negative regulation of T cell migration; ISS:ARUK-UCL.
DR GO; GO:0150072; P:positive regulation of arginase activity; IGI:ARUK-UCL.
DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; IDA:ARUK-UCL.
DR GO; GO:0150074; P:positive regulation of protein-glutamine gamma-glutamyltransferase activity; IGI:ARUK-UCL.
DR GO; GO:0071636; P:positive regulation of transforming growth factor beta production; IGI:ARUK-UCL.
DR GO; GO:0050776; P:regulation of immune response; IEA:InterPro.
DR GO; GO:0150077; P:regulation of neuroinflammatory response; ISS: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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..278
FT /note="OX-2 membrane glycoprotein"
FT /id="PRO_0000015124"
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"
FT VAR_SEQ 4
FT /note="L -> LTLTRTIGGPLLTATLLGKTTINDYQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040027"
FT VAR_SEQ 268..278
FT /note="GELSQGVQKMT -> EP (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16303743,
FT ECO:0000303|Ref.1, ECO:0000303|Ref.2"
FT /id="VSP_002613"
FT VARIANT 11
FT /note="S -> C (in dbSNP:rs1131199)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16303743,
FT ECO:0000269|Ref.1"
FT /id="VAR_027605"
FT VARIANT 46
FT /note="P -> T (in dbSNP:rs2272022)"
FT /evidence="ECO:0000269|PubMed:3032785"
FT /id="VAR_027606"
FT VARIANT 76
FT /note="V -> G (in dbSNP:rs35465733)"
FT /id="VAR_056110"
FT CONFLICT 181
FT /note="N -> D (in Ref. 1; AAT37533)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="F -> S (in Ref. 1; AAT37533)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 278 AA; 31264 MW; 38DF327B382CC970 CRC64;
MERLVIRMPF SHLSTYSLVW VMAAVVLCTA QVQVVTQDER EQLYTPASLK CSLQNAQEAL
IVTWQKKKAV SPENMVTFSE NHGVVIQPAY KDKINITQLG LQNSTITFWN ITLEDEGCYM
CLFNTFGFGK ISGTACLTVY VQPIVSLHYK FSEDHLNITC SATARPAPMV FWKVPRSGIE
NSTVTLSHPN GTTSVTSILH IKDPKNQVGK EVICQVLHLG TVTDFKQTVN KGYWFSVPLL
LSIVSLVILL VLISILLYWK RHRNQDRGEL SQGVQKMT
