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MO2R1_HUMAN
ID   MO2R1_HUMAN             Reviewed;         325 AA.
AC   Q8TD46; B3KWZ9; E9PCM9; Q52LJ7; Q6IS95; Q6UW94; Q6WHB8; Q8TD44; Q8TD45;
AC   Q8TD52;
DT   28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 3.
DT   03-AUG-2022, entry version 175.
DE   RecName: Full=Cell surface glycoprotein CD200 receptor 1;
DE   AltName: Full=CD200 cell surface glycoprotein receptor;
DE   AltName: Full=Cell surface glycoprotein OX2 receptor 1;
DE   Flags: Precursor;
GN   Name=CD200R1; Synonyms=CD200R, CRTR2, MOX2R, OX2R;
GN   ORFNames=UNQ2522/PRO6015;
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 4).
RX   PubMed=15274657; DOI=10.1111/j.1600-0897.2004.00192.x;
RA   Gorczynski R.M., Chen Z., Clark D.A., Kai Y., Lee L., Nachman J., Wong S.,
RA   Marsden P.;
RT   "Structural and functional heterogeneity in the CD200R family of
RT   immunoregulatory molecules and their expression at the feto-maternal
RT   interface.";
RL   Am. J. Reprod. Immunol. 52:147-163(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH HERPES VIRUS 8
RP   PROTEIN VOX2/K14 (MICROBIAL INFECTION).
RA   Wright G.J., Brown M.H., Barclay N.;
RT   "K14, the HHV-8 viral OX2 homolog interacts with the human OX2 receptor
RT   with identical affinity and kinetics as the host OX2 protein.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
RA   Suarez A., Vieites J.M., De la Torre R., Ortega M.A., Gil A.,
RA   Sanchez-Pozo A.;
RT   "Characterization of human CD200R gene.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANTS ARG-89;
RP   PRO_121; GLN-177 AND GLN-312.
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANTS
RP   ARG-89; PRO_121; GLN-177 AND GLN-312.
RC   TISSUE=Trachea, and Uterus;
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   [6]
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   [7]
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
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   [9]
RP   PROTEIN SEQUENCE OF N-TERMINUS.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally verified
RT   cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [10]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12960329; DOI=10.4049/jimmunol.171.6.3034;
RA   Wright G.J., Cherwinski H., Foster-Cuevas M., Brooke G., Puklavec M.J.,
RA   Bigler M., Song Y., Jenmalm M., Gorman D., McClanahan T., Liu M.-R.,
RA   Brown M.H., Sedgwick J.D., Phillips J.H., Barclay A.N.;
RT   "Characterization of the CD200 receptor family in mice and humans and their
RT   interactions with CD200.";
RL   J. Immunol. 171:3034-3046(2003).
RN   [11]
RP   REVIEW.
RX   PubMed=24388216; DOI=10.1016/b978-0-12-800100-4.00005-2;
RA   Vaine C.A., Soberman R.J.;
RT   "The CD200-CD200R1 inhibitory signaling pathway: immune regulation and
RT   host-pathogen interactions.";
RL   Adv. Immunol. 121:191-211(2014).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Inhibitory receptor for the CD200/OX2 cell surface
CC       glycoprotein. Limits inflammation by inhibiting the expression of pro-
CC       inflammatory molecules including TNF-alpha, interferons, and inducible
CC       nitric oxide synthase (iNOS) in response to selected stimuli. Also
CC       binds to HHV-8 K14 viral CD200 homolog with identical affinity and
CC       kinetics as the host CD200. {ECO:0000269|PubMed:12960329}.
CC   -!- SUBUNIT: CD200 and CD200R1 interact via their respective N-terminal Ig-
CC       like domains (By similarity). Interacts with Human herpesvirus 8 vOX2
CC       protein. {ECO:0000250}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with human herpesvirus 8/HHV-8
CC       protein vOX2/K14. {ECO:0000269|Ref.2}.
CC   -!- INTERACTION:
CC       Q8TD46; P41217: CD200; NbExp=2; IntAct=EBI-4314412, EBI-3910563;
CC       Q8TD46-4; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-12824513, EBI-10827839;
CC       Q8TD46-4; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-12824513, EBI-12256978;
CC       Q8TD46-4; Q7Z2K6: ERMP1; NbExp=3; IntAct=EBI-12824513, EBI-10976398;
CC       Q8TD46-4; Q8N3T1: GALNT15; NbExp=3; IntAct=EBI-12824513, EBI-3925203;
CC       Q8TD46-4; Q92982: NINJ1; NbExp=3; IntAct=EBI-12824513, EBI-2802124;
CC       Q8TD46-4; Q13635-3: PTCH1; NbExp=3; IntAct=EBI-12824513, EBI-14199621;
CC       Q8TD46-4; P11686: SFTPC; NbExp=3; IntAct=EBI-12824513, EBI-10197617;
CC       Q8TD46-4; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-12824513, EBI-744081;
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
CC       membrane protein.
CC   -!- SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane; Single-pass type I
CC       membrane protein.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
CC   -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8TD46-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8TD46-2; Sequence=VSP_002614, VSP_002615, VSP_002616;
CC       Name=3;
CC         IsoId=Q8TD46-3; Sequence=VSP_002615, VSP_002616;
CC       Name=4;
CC         IsoId=Q8TD46-4; Sequence=VSP_002614;
CC   -!- TISSUE SPECIFICITY: Expressed in granulocytes, monocytes, most T-cells,
CC       neutrophils, basophils and a subset of NK, NKT and B-cells (at protein
CC       level). Expressed in bone marrow, lymph nodes, spleen, lung, liver,
CC       spinal cord, kidney. Expressed in monocyte-derived dendritic and mast
CC       cells. {ECO:0000269|PubMed:12960329}.
CC   -!- PTM: The mature form of isoform 2 and/or isoform 4 starts at sequence
CC       position 27 of the corresponding isoform.
CC   -!- SIMILARITY: Belongs to the CD200R family. {ECO:0000305}.
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DR   EMBL; AY284975; AAQ19772.1; -; mRNA.
DR   EMBL; AF283760; AAN61171.1; -; mRNA.
DR   EMBL; AF497548; AAM16157.2; -; mRNA.
DR   EMBL; AF497549; AAM16158.2; -; mRNA.
DR   EMBL; AF497550; AAM16159.2; -; mRNA.
DR   EMBL; AF495380; AAM14622.2; -; mRNA.
DR   EMBL; AY358910; AAQ89269.2; -; mRNA.
DR   EMBL; AK126349; BAG54311.1; -; mRNA.
DR   EMBL; AK293071; BAF85760.1; -; mRNA.
DR   EMBL; AC074044; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471052; EAW79657.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW79658.1; -; Genomic_DNA.
DR   EMBL; BC069661; AAH69661.1; -; mRNA.
DR   EMBL; BC069721; AAH69721.1; -; mRNA.
DR   EMBL; BC069743; AAH69743.1; -; mRNA.
DR   EMBL; BC093890; AAH93890.1; -; mRNA.
DR   CCDS; CCDS2969.1; -. [Q8TD46-4]
DR   CCDS; CCDS2970.1; -. [Q8TD46-1]
DR   CCDS; CCDS46889.1; -. [Q8TD46-2]
DR   CCDS; CCDS54623.1; -. [Q8TD46-3]
DR   RefSeq; NP_620161.1; NM_138806.3. [Q8TD46-4]
DR   RefSeq; NP_620385.1; NM_138939.2. [Q8TD46-2]
DR   RefSeq; NP_620386.1; NM_138940.2. [Q8TD46-3]
DR   RefSeq; NP_740750.1; NM_170780.2. [Q8TD46-1]
DR   AlphaFoldDB; Q8TD46; -.
DR   SMR; Q8TD46; -.
DR   BioGRID; 126281; 23.
DR   IntAct; Q8TD46; 9.
DR   GlyGen; Q8TD46; 8 sites.
DR   iPTMnet; Q8TD46; -.
DR   PhosphoSitePlus; Q8TD46; -.
DR   SwissPalm; Q8TD46; -.
DR   BioMuta; CD200R1; -.
DR   DMDM; 26006823; -.
DR   jPOST; Q8TD46; -.
DR   MassIVE; Q8TD46; -.
DR   PeptideAtlas; Q8TD46; -.
DR   PRIDE; Q8TD46; -.
DR   ProteomicsDB; 74236; -. [Q8TD46-1]
DR   ProteomicsDB; 74237; -. [Q8TD46-2]
DR   ProteomicsDB; 74238; -. [Q8TD46-3]
DR   ProteomicsDB; 74239; -. [Q8TD46-4]
DR   ABCD; Q8TD46; 1 sequenced antibody.
DR   Antibodypedia; 16344; 676 antibodies from 33 providers.
DR   DNASU; 131450; -.
DR   Ensembl; ENST00000308611.8; ENSP00000311035.3; ENSG00000163606.11. [Q8TD46-4]
DR   Ensembl; ENST00000440122.6; ENSP00000405733.2; ENSG00000163606.11. [Q8TD46-2]
DR   Ensembl; ENST00000471858.5; ENSP00000418928.1; ENSG00000163606.11. [Q8TD46-1]
DR   Ensembl; ENST00000490004.1; ENSP00000418801.1; ENSG00000163606.11. [Q8TD46-3]
DR   GeneID; 131450; -.
DR   KEGG; hsa:131450; -.
DR   MANE-Select; ENST00000308611.8; ENSP00000311035.3; NM_138806.4; NP_620161.1. [Q8TD46-4]
DR   UCSC; uc003dzj.2; human. [Q8TD46-1]
DR   CTD; 131450; -.
DR   DisGeNET; 131450; -.
DR   GeneCards; CD200R1; -.
DR   HGNC; HGNC:24235; CD200R1.
DR   HPA; ENSG00000163606; Tissue enhanced (lymphoid).
DR   MIM; 607546; gene.
DR   neXtProt; NX_Q8TD46; -.
DR   OpenTargets; ENSG00000163606; -.
DR   PharmGKB; PA134922446; -.
DR   VEuPathDB; HostDB:ENSG00000163606; -.
DR   eggNOG; ENOG502S9IV; Eukaryota.
DR   GeneTree; ENSGT00390000014496; -.
DR   HOGENOM; CLU_069156_0_0_1; -.
DR   InParanoid; Q8TD46; -.
DR   OrthoDB; 993609at2759; -.
DR   PhylomeDB; Q8TD46; -.
DR   TreeFam; TF335960; -.
DR   PathwayCommons; Q8TD46; -.
DR   Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   SignaLink; Q8TD46; -.
DR   BioGRID-ORCS; 131450; 13 hits in 1069 CRISPR screens.
DR   ChiTaRS; CD200R1; human.
DR   GeneWiki; CD200R1; -.
DR   GenomeRNAi; 131450; -.
DR   Pharos; Q8TD46; Tbio.
DR   PRO; PR:Q8TD46; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q8TD46; protein.
DR   Bgee; ENSG00000163606; Expressed in epithelium of nasopharynx and 116 other tissues.
DR   ExpressionAtlas; Q8TD46; baseline and differential.
DR   Genevisible; Q8TD46; HS.
DR   GO; GO:0009986; C:cell surface; IDA:ARUK-UCL.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0043235; C:receptor complex; IDA:MGI.
DR   GO; GO:0140081; F:glycosylated region protein binding; TAS:ARUK-UCL.
DR   GO; GO:0019763; F:immunoglobulin receptor activity; TAS:ARUK-UCL.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0034113; P:heterotypic cell-cell adhesion; ISS:ARUK-UCL.
DR   GO; GO:0035556; P:intracellular signal transduction; TAS:ARUK-UCL.
DR   GO; GO:0032715; P:negative regulation of interleukin-6 production; ISS:ARUK-UCL.
DR   GO; GO:1905522; P:negative regulation of macrophage migration; ISS: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:2000405; P:negative regulation of T cell migration; ISS:ARUK-UCL.
DR   GO; GO:0150077; P:regulation of neuroinflammatory response; ISS:ARUK-UCL.
DR   GO; GO:0007165; P:signal transduction; TAS:ARUK-UCL.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR040012; CD200R.
DR   InterPro; IPR013162; CD80_C2-set.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR21462; PTHR21462; 1.
DR   Pfam; PF08205; C2-set_2; 1.
DR   SUPFAM; SSF48726; SSF48726; 2.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Host-virus interaction; Membrane; Receptor;
KW   Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..325
FT                   /note="Cell surface glycoprotein CD200 receptor 1"
FT                   /id="PRO_0000015128"
FT   TOPO_DOM        29..243
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        265..325
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          53..139
FT                   /note="Ig-like V-type"
FT   DOMAIN          140..228
FT                   /note="Ig-like C2-type"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        210
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        224
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        60..132
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        84..100
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        167..216
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        186..204
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         22
FT                   /note="A -> AEAEGAAQPNNSLMLQTSKENHAL (in isoform 2 and
FT                   isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:12975309,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15274657,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT                   /id="VSP_002614"
FT   VAR_SEQ         151..165
FT                   /note="VTPEVTLFQNRNRTA -> GKEHHILRYFTSPDL (in isoform 2 and
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_002615"
FT   VAR_SEQ         166..325
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_002616"
FT   VARIANT         89
FT                   /note="K -> R (in dbSNP:rs2171509)"
FT                   /evidence="ECO:0000269|PubMed:12975309,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|Ref.2"
FT                   /id="VAR_014352"
FT   VARIANT         121
FT                   /note="T -> P (in dbSNP:rs4596117)"
FT                   /evidence="ECO:0000269|PubMed:12975309,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|Ref.2"
FT                   /id="VAR_014353"
FT   VARIANT         177
FT                   /note="H -> Q (in dbSNP:rs9826308)"
FT                   /evidence="ECO:0000269|PubMed:12975309,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|Ref.2"
FT                   /id="VAR_014354"
FT   VARIANT         312
FT                   /note="E -> Q (in dbSNP:rs9865242)"
FT                   /evidence="ECO:0000269|PubMed:12975309,
FT                   ECO:0000269|PubMed:14702039"
FT                   /id="VAR_031022"
FT   CONFLICT        155
FT                   /note="V -> L (in Ref. 4; AAQ89269)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   325 AA;  36605 MW;  A7E761243FA346DC CRC64;
     MLCPWRTANL GLLLILTIFL VAASSSLCMD EKQITQNYSK VLAEVNTSWP VKMATNAVLC
     CPPIALRNLI IITWEIILRG QPSCTKAYKK ETNETKETNC TDERITWVSR PDQNSDLQIR
     TVAITHDGYY RCIMVTPDGN FHRGYHLQVL VTPEVTLFQN RNRTAVCKAV AGKPAAHISW
     IPEGDCATKQ EYWSNGTVTV KSTCHWEVHN VSTVTCHVSH LTGNKSLYIE LLPVPGAKKS
     AKLYIPYIIL TIIILTIVGF IWLLKVNGCR KYKLNKTEST PVVEEDEMQP YASYTEKNNP
     LYDTTNKVKA SEALQSEVDT DLHTL
 
 
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