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CCR2_RAT
ID   CCR2_RAT                Reviewed;         373 AA.
AC   O55193;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=C-C chemokine receptor type 2;
DE            Short=C-C CKR-2;
DE            Short=CC-CKR-2;
DE            Short=CCR-2;
DE            Short=CCR2;
DE   AltName: CD_antigen=CD192;
GN   Name=Ccr2; Synonyms=Cmkbr2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley;
RX   PubMed=9655467; DOI=10.1016/s0165-5728(98)00005-8;
RA   Jiang Y., Salafranca M.N., Adhikari S., Xia Y., Feng L., Sonntag M.K.,
RA   deFiebre C.M., Pennell N.A., Streit W.J., Harrison J.K.;
RT   "Chemokine receptor expression in cultured glia and rat experimental
RT   allergic encephalomyelitis.";
RL   J. Neuroimmunol. 86:1-12(1998).
CC   -!- FUNCTION: Key functional receptor for CCL2 but can also bind CCL7 and
CC       CCL12 (By similarity). Its binding with CCL2 on monocytes and
CC       macrophages mediates chemotaxis and migration induction through the
CC       activation of the PI3K cascade, the small G protein Rac and
CC       lamellipodium protrusion (By similarity). Also acts as a receptor for
CC       the beta-defensin DEFB106A/DEFB106B (By similarity). Regulates the
CC       expression of T-cell inflammatory cytokines and T-cell differentiation,
CC       promoting the differentiation of T-cells into T-helper 17 cells (Th17)
CC       during inflammation (By similarity). Facilitates the export of mature
CC       thymocytes by enhancing directional movement of thymocytes to
CC       sphingosine-1-phosphate stimulation and up-regulation of S1P1R
CC       expression; signals through the JAK-STAT pathway to regulate FOXO1
CC       activity leading to an increased expression of S1P1R (By similarity).
CC       Plays an important role in mediating peripheral nerve injury-induced
CC       neuropathic pain (By similarity). Increases NMDA-mediated synaptic
CC       transmission in both dopamine D1 and D2 receptor-containing neurons,
CC       which may be caused by MAPK/ERK-dependent phosphorylation of
CC       GRIN2B/NMDAR2B (By similarity). Mediates the recruitment of macrophages
CC       and monocytes to the injury site following brain injury (By
CC       similarity). {ECO:0000250|UniProtKB:P41597,
CC       ECO:0000250|UniProtKB:P51683}.
CC   -!- SUBUNIT: Interacts with ARRB1 (By similarity). Interacts (via
CC       extracellular N-terminal region) with beta-defensin DEFB106A/DEFB106B;
CC       this interaction may preferentially require specific tyrosine sulfation
CC       on CCR2 (By similarity). Interacts with NUP85; the interaction is
CC       required for CCR2 clusters formation on the cell membrane and CCR2
CC       signaling (By similarity). {ECO:0000250|UniProtKB:P41597}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P41597};
CC       Multi-pass membrane protein {ECO:0000255}. Note=The chemoattractant
CC       receptors are distributed throughout the cell surface; after
CC       stimulation with a ligand, such as CCL2, they are rapidly recruited
CC       into microdomain clusters at the cell membrane.
CC       {ECO:0000250|UniProtKB:P41597}.
CC   -!- TISSUE SPECIFICITY: Expressed in lung, spleen, kidney, thymus and
CC       macrophages. {ECO:0000269|PubMed:9655467}.
CC   -!- INDUCTION: In animals in which experimental allergic encephalomyelitis
CC       (EAE) has been induced. {ECO:0000269|PubMed:9655467}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P41597}.
CC   -!- PTM: Sulfation increases the affinity for both monomeric and dimeric
CC       CCL2 with stronger binding to the monomeric form (By similarity).
CC       Binding of sulfated CCR2 to CCL2 promotes conversion of CCL2 from dimer
CC       to monomer (By similarity). {ECO:0000250|UniProtKB:P41597}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; U77349; AAC03242.1; -; Genomic_DNA.
DR   RefSeq; NP_068638.1; NM_021866.1.
DR   AlphaFoldDB; O55193; -.
DR   SMR; O55193; -.
DR   BindingDB; O55193; -.
DR   ChEMBL; CHEMBL1293204; -.
DR   PhosphoSitePlus; O55193; -.
DR   Ensembl; ENSRNOT00000100998; ENSRNOP00000095594; ENSRNOG00000063127.
DR   Ensembl; ENSRNOT00000114724; ENSRNOP00000081733; ENSRNOG00000063127.
DR   GeneID; 60463; -.
DR   KEGG; rno:60463; -.
DR   UCSC; RGD:620876; rat.
DR   CTD; 729230; -.
DR   RGD; 620876; Ccr2.
DR   GeneTree; ENSGT01020000230359; -.
DR   InParanoid; O55193; -.
DR   PhylomeDB; O55193; -.
DR   TreeFam; TF330966; -.
DR   PRO; PR:O55193; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0043204; C:perikaryon; IDA:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0150001; C:primary dendrite; IDA:RGD.
DR   GO; GO:0019957; F:C-C chemokine binding; IBA:GO_Central.
DR   GO; GO:0016493; F:C-C chemokine receptor activity; ISO:RGD.
DR   GO; GO:0031727; F:CCR2 chemokine receptor binding; ISO:RGD.
DR   GO; GO:0035716; F:chemokine (C-C motif) ligand 12 binding; ISO:RGD.
DR   GO; GO:0035715; F:chemokine (C-C motif) ligand 2 binding; ISO:RGD.
DR   GO; GO:0071791; F:chemokine (C-C motif) ligand 5 binding; IBA:GO_Central.
DR   GO; GO:0035717; F:chemokine (C-C motif) ligand 7 binding; ISO:RGD.
DR   GO; GO:0019955; F:cytokine binding; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
DR   GO; GO:0001974; P:blood vessel remodeling; IEP:RGD.
DR   GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR   GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:RGD.
DR   GO; GO:0006968; P:cellular defense response; ISO:RGD.
DR   GO; GO:0019725; P:cellular homeostasis; ISS:BHF-UCL.
DR   GO; GO:0070098; P:chemokine-mediated signaling pathway; IMP:RGD.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IMP:RGD.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:RGD.
DR   GO; GO:0030097; P:hemopoiesis; ISO:RGD.
DR   GO; GO:0048873; P:homeostasis of number of cells within a tissue; ISO:RGD.
DR   GO; GO:0006959; P:humoral immune response; ISO:RGD.
DR   GO; GO:0006955; P:immune response; ISO:RGD.
DR   GO; GO:0006954; P:inflammatory response; IDA:RGD.
DR   GO; GO:0002437; P:inflammatory response to antigenic stimulus; IEP:RGD.
DR   GO; GO:0090594; P:inflammatory response to wounding; ISS:UniProtKB.
DR   GO; GO:0061756; P:leukocyte adhesion to vascular endothelial cell; ISO:RGD.
DR   GO; GO:1905517; P:macrophage migration; ISS:UniProtKB.
DR   GO; GO:0002548; P:monocyte chemotaxis; ISO:RGD.
DR   GO; GO:0035696; P:monocyte extravasation; ISS:UniProtKB.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; ISS:BHF-UCL.
DR   GO; GO:0043310; P:negative regulation of eosinophil degranulation; ISS:BHF-UCL.
DR   GO; GO:0002829; P:negative regulation of type 2 immune response; ISS:BHF-UCL.
DR   GO; GO:0097350; P:neutrophil clearance; ISO:RGD.
DR   GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; ISS:BHF-UCL.
DR   GO; GO:2000464; P:positive regulation of astrocyte chemotaxis; ISS:BHF-UCL.
DR   GO; GO:2000451; P:positive regulation of CD8-positive, alpha-beta T cell extravasation; ISS:BHF-UCL.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR   GO; GO:2000473; P:positive regulation of hematopoietic stem cell migration; ISS:BHF-UCL.
DR   GO; GO:0090265; P:positive regulation of immune complex clearance by monocytes and macrophages; ISS:BHF-UCL.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; ISS:BHF-UCL.
DR   GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:BHF-UCL.
DR   GO; GO:0032743; P:positive regulation of interleukin-2 production; ISS:BHF-UCL.
DR   GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; ISO:RGD.
DR   GO; GO:0090026; P:positive regulation of monocyte chemotaxis; ISS:UniProtKB.
DR   GO; GO:2000439; P:positive regulation of monocyte extravasation; ISS:BHF-UCL.
DR   GO; GO:1904783; P:positive regulation of NMDA glutamate receptor activity; IGI:ARUK-UCL.
DR   GO; GO:1900745; P:positive regulation of p38MAPK cascade; IDA:RGD.
DR   GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISS:UniProtKB.
DR   GO; GO:0050870; P:positive regulation of T cell activation; ISS:BHF-UCL.
DR   GO; GO:0010820; P:positive regulation of T cell chemotaxis; ISS:BHF-UCL.
DR   GO; GO:0002827; P:positive regulation of T-helper 1 type immune response; ISS:BHF-UCL.
DR   GO; GO:2000412; P:positive regulation of thymocyte migration; ISS:UniProtKB.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:RGD.
DR   GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
DR   GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR   GO; GO:1905521; P:regulation of macrophage migration; IEA:Ensembl.
DR   GO; GO:0002724; P:regulation of T cell cytokine production; ISS:UniProtKB.
DR   GO; GO:0045580; P:regulation of T cell differentiation; ISS:UniProtKB.
DR   GO; GO:0010574; P:regulation of vascular endothelial growth factor production; ISS:BHF-UCL.
DR   GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
DR   GO; GO:0035705; P:T-helper 17 cell chemotaxis; ISS:BHF-UCL.
DR   InterPro; IPR002237; Chemokine_CCR2.
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; PR01107; CHEMOKINER2.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
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   Inflammatory response; Membrane; Phosphoprotein; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..373
FT                   /note="C-C chemokine receptor type 2"
FT                   /id="PRO_0000069235"
FT   TOPO_DOM        1..60
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        82..91
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        113..128
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        150..170
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        192..220
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..241
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        242..256
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        278..301
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        302..322
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        323..373
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         152
FT                   /note="Phosphotyrosine; by JAK2"
FT                   /evidence="ECO:0000250|UniProtKB:P41597"
FT   DISULFID        126..203
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   373 AA;  42763 MW;  2E7BB012F5D6FD09 CRC64;
     MEDSNMLPQF IHGILSTSHS LFPRSIQELD EGATTPYDYD DGEPCHKTSV KQIGAWILPP
     LYSLVFIFGF VGNMLVIIIL ISCKKLKSMT DIYLFNLAIS DLLFLLTLPF WAHYAANEWV
     FGNIMCKLFT GLYHIGYFGG IFFIILLTID RYLAIVHAVF ALKARTVTFG VITSVVTWVV
     AVFASLPGII FTKSEQEDDQ HTCGPYFPTI WKNFQTIMRN ILSLILPLLV MVICYSGILH
     TLFRCRNEKK RHRAVRLIFA IMIVYFLFWT PYNIVLFLTT FQEFLGMSNC VVDMHLDQAM
     QVTETLGMTH CCVNPIIYAF VGEKFRRYLS IFFRKHIAKN LCKQCPVFYR ETADRVSSTF
     TPSTGEQEVS VGL
 
 
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