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CCR9_MOUSE
ID   CCR9_MOUSE              Reviewed;         369 AA.
AC   Q9WUT7; A2RSM5; Q543I4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=C-C chemokine receptor type 9;
DE            Short=C-C CKR-9;
DE            Short=CC-CKR-9;
DE            Short=CCR-9;
DE   AltName: Full=Chemokine C-C receptor 10;
DE   AltName: CD_antigen=CDw199;
GN   Name=Ccr9; Synonyms=Cmkbr10;
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].
RC   TISSUE=Thymus;
RX   PubMed=10229797;
RA   Zaballos A., Gutierrez J., Varona R., Ardavin C., Marquez G.;
RT   "Identification of the orphan chemokine receptor GPR-9-6 as CCR9, the
RT   receptor for the chemokine TECK.";
RL   J. Immunol. 162:5671-5675(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10602049;
RX   DOI=10.1002/1521-4141(200001)30:1<262::aid-immu262>3.0.co;2-0;
RA   Wurbel M.A., Philippe J.-M., Nguyen C., Victorero G., Freeman T.,
RA   Wooding P., Miazek A., Mattei M.-G., Malissen M., Jordan B.R., Malissen B.,
RA   Carrier A., Naquet P.;
RT   "The chemokine TECK is expressed by thymic and intestinal epithelial cells
RT   and attracts double- and single-positive thymocytes expressing the TECK
RT   receptor CCR9.";
RL   Eur. J. Immunol. 30:262-271(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Skin, and Thymus;
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 MRNA].
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).
CC   -!- FUNCTION: Receptor for chemokine SCYA25/TECK. Subsequently transduces a
CC       signal by increasing the intracellular calcium ions level.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P51686};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P51686}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the thymus and low in lymph
CC       nodes and spleen.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AJ132336; CAB43480.1; -; mRNA.
DR   EMBL; AJ131357; CAB66136.2; -; mRNA.
DR   EMBL; AK019478; BAB31747.1; -; mRNA.
DR   EMBL; AK050615; BAC34344.1; -; mRNA.
DR   EMBL; AK153975; BAE32291.1; -; mRNA.
DR   EMBL; BC132166; AAI32167.1; -; mRNA.
DR   EMBL; BC132466; AAI32467.1; -; mRNA.
DR   CCDS; CCDS23662.1; -.
DR   RefSeq; NP_001160097.1; NM_001166625.1.
DR   RefSeq; NP_034043.1; NM_009913.6.
DR   AlphaFoldDB; Q9WUT7; -.
DR   SMR; Q9WUT7; -.
DR   BioGRID; 198769; 1.
DR   DIP; DIP-5886N; -.
DR   STRING; 10090.ENSMUSP00000127024; -.
DR   GlyGen; Q9WUT7; 1 site.
DR   iPTMnet; Q9WUT7; -.
DR   PhosphoSitePlus; Q9WUT7; -.
DR   jPOST; Q9WUT7; -.
DR   PaxDb; Q9WUT7; -.
DR   PRIDE; Q9WUT7; -.
DR   ProteomicsDB; 281130; -.
DR   Antibodypedia; 3479; 639 antibodies from 36 providers.
DR   DNASU; 12769; -.
DR   Ensembl; ENSMUST00000163559; ENSMUSP00000131782; ENSMUSG00000029530.
DR   Ensembl; ENSMUST00000166236; ENSMUSP00000127024; ENSMUSG00000029530.
DR   Ensembl; ENSMUST00000168910; ENSMUSP00000126758; ENSMUSG00000029530.
DR   Ensembl; ENSMUST00000180093; ENSMUSP00000137144; ENSMUSG00000029530.
DR   GeneID; 12769; -.
DR   KEGG; mmu:12769; -.
DR   UCSC; uc009sgl.2; mouse.
DR   CTD; 10803; -.
DR   MGI; MGI:1341902; Ccr9.
DR   VEuPathDB; HostDB:ENSMUSG00000029530; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01030000234667; -.
DR   InParanoid; Q9WUT7; -.
DR   OMA; TICTMVY; -.
DR   OrthoDB; 800663at2759; -.
DR   PhylomeDB; Q9WUT7; -.
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; 12769; 1 hit in 72 CRISPR screens.
DR   ChiTaRS; Ccr9; mouse.
DR   PRO; PR:Q9WUT7; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q9WUT7; protein.
DR   Bgee; ENSMUSG00000029530; Expressed in thymus and 88 other tissues.
DR   ExpressionAtlas; Q9WUT7; baseline and differential.
DR   Genevisible; Q9WUT7; MM.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR   GO; GO:0002305; P:CD8-positive, gamma-delta intraepithelial T cell differentiation; IMP:MGI.
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; IBA:GO_Central.
DR   InterPro; IPR004069; Chemokine_CCR9.
DR   InterPro; IPR000355; Chemokine_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00657; CCCHEMOKINER.
DR   PRINTS; PR01531; CHEMOKINER9.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..369
FT                   /note="C-C chemokine receptor type 9"
FT                   /id="PRO_0000069292"
FT   TOPO_DOM        1..48
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P51686"
FT   TRANSMEM        49..74
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:P51686"
FT   TOPO_DOM        75..85
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P51686"
FT   TRANSMEM        86..109
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:P51686"
FT   TOPO_DOM        110..120
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P51686"
FT   TRANSMEM        121..150
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P51686"
FT   TOPO_DOM        151..159
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P51686"
FT   TRANSMEM        160..185
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P51686"
FT   TOPO_DOM        186..208
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P51686"
FT   TRANSMEM        209..243
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:P51686"
FT   TOPO_DOM        244..248
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P51686"
FT   TRANSMEM        249..283
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:P51686"
FT   TOPO_DOM        284..290
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P51686"
FT   TRANSMEM        291..321
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250|UniProtKB:P51686"
FT   TOPO_DOM        322..369
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P51686"
FT   CARBOHYD        32
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        38..289
FT                   /evidence="ECO:0000250|UniProtKB:P51686"
FT   DISULFID        119..198
FT                   /evidence="ECO:0000250|UniProtKB:P51686,
FT                   ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   369 AA;  41913 MW;  6971F76F0A24B4AE CRC64;
     MMPTELTSLI PGMFDDFSYD STASTDDYMN LNFSSFFCKK NNVRQFASHF LPPLYWLVFI
     VGTLGNSLVI LVYWYCTRVK TMTDMFLLNL AIADLLFLAT LPFWAIAAAG QWMFQTFMCK
     VVNSMYKMNF YSCVLLIMCI SVDRYIAIVQ AMKAQVWRQK RLLYSKMVCI TIWVMAAVLC
     TPEILYSQVS GESGIATCTM VYPKDKNAKL KSAVLILKVT LGFFLPFMVM AFCYTIIIHT
     LVQAKKSSKH KALKVTITVL TVFIMSQFPY NSILVVQAVD AYAMFISNCT ISTNIDICFQ
     VTQTIAFFHS CLNPVLYVFV GERFRRDLVK TLKNLGCISQ AQWVSFTRRE GSLKLSSMLL
     ETTSGALSL
 
 
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