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CCR3_CAVPO
ID   CCR3_CAVPO              Reviewed;         358 AA.
AC   Q9Z2I3;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=C-C chemokine receptor type 3;
DE            Short=C-C CKR-3;
DE            Short=CC-CKR-3;
DE            Short=CCR-3;
DE            Short=CCR3;
DE            Short=CKR3;
DE   AltName: CD_antigen=CD193;
GN   Name=CCR3; Synonyms=CMKBR3;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9834099;
RA   Sabroe I., Conroy D.M., Gerard N.P., Li Y., Collins P.D., Post T.W.,
RA   Jose P.J., Williams T.J., Gerard C.J., Ponath P.D.;
RT   "Cloning and characterization of the guinea pig eosinophil eotaxin
RT   receptor, C-C chemokine receptor-3: blockade using a monoclonal antibody in
RT   vivo.";
RL   J. Immunol. 161:6139-6147(1998).
CC   -!- FUNCTION: Receptor for C-C type chemokine. Binds and responds to a
CC       variety of chemokines, including CCL11, CCL26, CCL7, CCL13,
CC       RANTES(CCL5) and CCL15. Subsequently transduces a signal by increasing
CC       the intracellular calcium ions level. In addition acts as a possible
CC       functional receptor for NARS1. {ECO:0000250|UniProtKB:P51677}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AF060698; AAC80428.1; -; Genomic_DNA.
DR   RefSeq; XP_013015509.1; XM_013160055.1.
DR   RefSeq; XP_013015510.1; XM_013160056.1.
DR   RefSeq; XP_013015511.1; XM_013160057.1.
DR   AlphaFoldDB; Q9Z2I3; -.
DR   SMR; Q9Z2I3; -.
DR   STRING; 10141.ENSCPOP00000016457; -.
DR   Ensembl; ENSCPOT00000012621; ENSCPOP00000016457; ENSCPOG00000012502.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01020000230359; -.
DR   HOGENOM; CLU_009579_8_3_1; -.
DR   InParanoid; Q9Z2I3; -.
DR   OMA; DMGLLCE; -.
DR   OrthoDB; 900867at2759; -.
DR   TreeFam; TF330966; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000012502; Expressed in pituitary gland and 2 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019957; F:C-C chemokine binding; IEA:Ensembl.
DR   GO; GO:0016493; F:C-C chemokine receptor activity; IEA:Ensembl.
DR   GO; GO:0006935; P:chemotaxis; IEA:Ensembl.
DR   GO; GO:0006954; P:inflammatory response; IEA:InterPro.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
DR   InterPro; IPR002238; Chemokine_CCR3.
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; PR01108; CHEMOKINER3.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; G-protein coupled receptor; Membrane; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..358
FT                   /note="C-C chemokine receptor type 3"
FT                   /id="PRO_0000069237"
FT   TOPO_DOM        1..43
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..64
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        65..74
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        75..95
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        96..112
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        134..154
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        176..206
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        228..243
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        244..264
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        265..287
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        288..308
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        309..358
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   358 AA;  41623 MW;  7B73FAB7A3BC3670 CRC64;
     MATYPEEAEL ETEFPGTTFY DYEFAQPCFK VSITDLGAQF LPSLFSLVFI VGLLGNITVI
     VVLTKYQKLK IMTNIYLLNL AISDLLFLFT LPFWTYYVHW NKWVFGHFMC KIISGLYYVG
     LFSEIFFIIL LTIDRYLAIV HAVFALRTRT VTFGIITSVI TWVLAVLAAL PEFMFYGTQG
     HFEVLFCGPS YPEKKEHHWK RFQALRMNIF GLALPLLIMI ICYTGIIKTL LRCPSKKKYK
     AIRLIFVIMV VFFVFWTPYN LLLLFSAFDL SFLDDCERSK QLDMAKHVTE VIAHTHCCIN
     PIIYAFVGER FQKYLRHFLH RNVTMHLSKY IPFFTSEKLE RSSSISPSSG DPELSVVF
 
 
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