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CCR10_MOUSE
ID   CCR10_MOUSE             Reviewed;         362 AA.
AC   Q9JL21; Q542A4; Q9JIP1; Q9JL20;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=C-C chemokine receptor type 10;
DE            Short=C-C CKR-10;
DE            Short=CC-CKR-10;
DE            Short=CCR-10;
DE   AltName: Full=Chemokine C-C receptor 9;
DE   AltName: Full=G-protein coupled receptor 2;
GN   Name=Ccr10; Synonyms=Cmkbr9, Gpr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   STRAIN=BALB/cJ; TISSUE=Peyer patch;
RX   PubMed=10725696; DOI=10.4049/jimmunol.164.7.3460;
RA   Jarmin D.I., Rits M., Bota D., Gerard N.P., Graham G.J., Clark-Lewis I.,
RA   Gerard C.;
RT   "Identification of the orphan receptor G-protein-coupled receptor 2 as
RT   CCR10, a specific receptor for the chemokine ESkine.";
RL   J. Immunol. 164:3460-3464(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND LIGAND-BINDING.
RC   TISSUE=Thymocyte;
RX   PubMed=10781587; DOI=10.1074/jbc.m001461200;
RA   Wang W., Soto H., Oldham E.R., Buchanan M.E., Homey B., Catron D.,
RA   Jenkins N., Copeland N.G., Gilbert D.J., Nguyen N., Abrams J.,
RA   Kershenovich D., Smith K., McClanahan T., Vicari A.P., Zlotnik A.;
RT   "Identification of a novel chemokine (CCL28), which binds CCR10 (GPR2).";
RL   J. Biol. Chem. 275:22313-22323(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymocyte;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
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).
CC   -!- FUNCTION: Receptor for chemokines SCYA27 and SCYA28. Subsequently
CC       transduces a signal by increasing the intracellular calcium ions level.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in small intestine, colon,
CC       lymph nodes, Peyer patches and at lower levels in thymus, lung and
CC       spleen. {ECO:0000269|PubMed:10781587}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AF215982; AAF63710.1; -; mRNA.
DR   EMBL; AF215983; AAF63711.1; -; mRNA.
DR   EMBL; AF208238; AAF72872.1; -; mRNA.
DR   EMBL; AK090044; BAC41062.1; -; mRNA.
DR   EMBL; AL590969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466677; EDL03895.1; -; Genomic_DNA.
DR   EMBL; BC117043; AAI17044.1; -; mRNA.
DR   EMBL; BC120542; AAI20543.1; -; mRNA.
DR   CCDS; CCDS25454.1; -.
DR   RefSeq; NP_031747.2; NM_007721.4.
DR   AlphaFoldDB; Q9JL21; -.
DR   SMR; Q9JL21; -.
DR   STRING; 10090.ENSMUSP00000062588; -.
DR   BindingDB; Q9JL21; -.
DR   ChEMBL; CHEMBL3879821; -.
DR   GuidetoPHARMACOLOGY; 67; -.
DR   iPTMnet; Q9JL21; -.
DR   PhosphoSitePlus; Q9JL21; -.
DR   PaxDb; Q9JL21; -.
DR   PRIDE; Q9JL21; -.
DR   ProteomicsDB; 281429; -.
DR   Antibodypedia; 3185; 429 antibodies from 37 providers.
DR   DNASU; 12777; -.
DR   Ensembl; ENSMUST00000062759; ENSMUSP00000062588; ENSMUSG00000044052.
DR   GeneID; 12777; -.
DR   KEGG; mmu:12777; -.
DR   UCSC; uc007lns.1; mouse.
DR   CTD; 2826; -.
DR   MGI; MGI:1096320; Ccr10.
DR   VEuPathDB; HostDB:ENSMUSG00000044052; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01030000234667; -.
DR   HOGENOM; CLU_009579_8_3_1; -.
DR   InParanoid; Q9JL21; -.
DR   OMA; MLPELCE; -.
DR   OrthoDB; 1082304at2759; -.
DR   PhylomeDB; Q9JL21; -.
DR   TreeFam; TF330966; -.
DR   Reactome; R-MMU-380108; Chemokine receptors bind chemokines.
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   BioGRID-ORCS; 12777; 1 hit in 71 CRISPR screens.
DR   PRO; PR:Q9JL21; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q9JL21; protein.
DR   Bgee; ENSMUSG00000044052; Expressed in small intestine Peyer's patch and 25 other tissues.
DR   Genevisible; Q9JL21; MM.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
DR   GO; GO:0019957; F:C-C chemokine binding; IBA:GO_Central.
DR   GO; GO:0016493; F:C-C chemokine receptor activity; IDA:MGI.
DR   GO; GO:0004950; F:chemokine receptor activity; IDA:MGI.
DR   GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR   GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR   GO; GO:0006935; P:chemotaxis; IDA:MGI.
DR   GO; GO:0006955; P:immune response; IBA:GO_Central.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:MGI.
DR   InterPro; IPR005382; Chemokine_CCR10.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR10489:SF773; PTHR10489:SF773; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01557; CHEMOKINER10.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Membrane;
KW   Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..362
FT                   /note="C-C chemokine receptor type 10"
FT                   /id="PRO_0000069294"
FT   TOPO_DOM        1..48
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        49..69
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        70..80
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        102..115
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        137..159
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        181..208
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        230..247
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        248..268
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        269..291
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        292..312
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        313..362
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DISULFID        113..191
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        135
FT                   /note="S -> N (in Ref. 1; AAF63710/AAF63711)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   362 AA;  38900 MW;  13C4292859C376CE CRC64;
     MGTKPTEQVS WGLYSGYDEE AYSVGPLPEL CYKADVQAFS RAFQPSVSLM VAVLGLAGNG
     LVLATHLAAR RTTRSPTSVH LLQLALADLL LALTLPFAAA GALQGWNLGS TTCRAISGLY
     SASFHAGFLF LACISADRYV AIARALPAGQ RPSTPSRAHL VSVFVWLLSL FLALPALLFS
     RDGPREGQRR CRLIFPESLT QTVKGASAVA QVVLGFALPL GVMAACYALL GRTLLAARGP
     ERRRALRVVV ALVVAFVVLQ LPYSLALLLD TADLLAARER SCSSSKRKDL ALLVTGGLTL
     VRCSLNPVLY AFLGLRFRRD LRRLLQGGGC SPKPNPRGRC PRRLRLSSCS APTETHSLSW
     DN
 
 
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