CCR5_CANLF
ID CCR5_CANLF Reviewed; 352 AA.
AC Q5ECR9; Q5KSV8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=C-C chemokine receptor type 5;
DE Short=C-C CKR-5;
DE Short=CC-CKR-5;
DE Short=CCR-5;
DE Short=CCR5;
DE AltName: CD_antigen=CD195;
GN Name=CCR5; Synonyms=CMKBR5;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tsukui T., Maeda S., Koyanagi M., Hashimoto R., Masuda K., Ohno K.,
RA Sakaguchi M., Tsujimoto H., Iwabuchi S.;
RT "Expression analysis of CCR5 gene in canine atopic dermatitis.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=16806494; DOI=10.1016/j.vetimm.2006.05.009;
RA Mosley M., Pullen S., Botham A., Gray A., Napier C., Mansfield R.,
RA Holbrook M.;
RT "The molecular cloning and functional expression of the dog CCR5.";
RL Vet. Immunol. Immunopathol. 113:415-420(2006).
CC -!- FUNCTION: Receptor for a number of inflammatory CC-chemokines including
CC CCL3/MIP-1-alpha, CCL4/MIP-1-beta and RANTES and subsequently
CC transduces a signal by increasing the intracellular calcium ion level.
CC May play a role in the control of granulocytic lineage proliferation or
CC differentiation (PubMed:16806494). Participates in T-lymphocyte
CC migration to the infection site by acting as a chemotactic receptor (By
CC similarity) (PubMed:16806494). {ECO:0000250|UniProtKB:P51681,
CC ECO:0000269|PubMed:16806494}.
CC -!- SUBUNIT: Interacts with PRAF2. Efficient ligand binding to CCL3/MIP-
CC 1alpha and CCL4/MIP-1beta requires sulfation, O-glycosylation and
CC sialic acid modifications. Glycosylation on Ser-6 is required for
CC efficient binding of CCL4. Interacts with GRK2. Interacts with ARRB1
CC and ARRB2. Interacts with CNIH4. Interacts with S100A4; this
CC interaction stimulates T-lymphocyte chemotaxis.
CC {ECO:0000250|UniProtKB:P51681}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9XT76};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9XT76}.
CC -!- PTM: Sulfated on at least 2 of the N-terminal tyrosines. Sulfation is
CC required for efficient binding of the chemokines, CCL3 and CCL4 (By
CC similarity). {ECO:0000250|UniProtKB:P51681}.
CC -!- PTM: O-glycosylated, but not N-glycosylated. Ser-6 appears to be the
CC major site. Also sialylated glycans present which contribute to
CC chemokine binding. Thr-16 and Ser-17 may also be glycosylated and, if
CC so, with small moieties such as a T-antigen.
CC {ECO:0000250|UniProtKB:P51681}.
CC -!- PTM: Palmitoylation in the C-terminal is important for cell surface
CC expression. {ECO:0000250|UniProtKB:P51681}.
CC -!- PTM: Phosphorylation on serine residues in the C-terminal is stimulated
CC by binding CC chemokines especially by APO-RANTES.
CC {ECO:0000250|UniProtKB:P51681}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB183192; BAD83840.1; -; mRNA.
DR EMBL; AY904725; AAW83502.1; -; mRNA.
DR RefSeq; NP_001012342.2; NM_001012342.3.
DR RefSeq; XP_005632385.1; XM_005632328.2.
DR RefSeq; XP_013977216.1; XM_014121741.1.
DR AlphaFoldDB; Q5ECR9; -.
DR SMR; Q5ECR9; -.
DR STRING; 9615.ENSCAFP00000020323; -.
DR PaxDb; Q5ECR9; -.
DR Ensembl; ENSCAFT00030046693; ENSCAFP00030040815; ENSCAFG00030025292.
DR Ensembl; ENSCAFT00040033273; ENSCAFP00040028958; ENSCAFG00040018022.
DR Ensembl; ENSCAFT00845021544; ENSCAFP00845016932; ENSCAFG00845012125.
DR Ensembl; ENSCAFT00845021561; ENSCAFP00845016943; ENSCAFG00845012125.
DR GeneID; 484789; -.
DR KEGG; cfa:484789; -.
DR CTD; 1234; -.
DR VEuPathDB; HostDB:ENSCAFG00845012125; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230359; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; Q5ECR9; -.
DR OMA; HYTCSPH; -.
DR OrthoDB; 937138at2759; -.
DR TreeFam; TF330966; -.
DR Reactome; R-CFA-418594; G alpha (i) signalling events.
DR Proteomes; UP000002254; Chromosome 20.
DR Bgee; ENSCAFG00000013783; Expressed in cartilage tissue and 43 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IEA:Ensembl.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:Ensembl.
DR GO; GO:0019957; F:C-C chemokine binding; IBA:GO_Central.
DR GO; GO:0016493; F:C-C chemokine receptor activity; ISS:UniProtKB.
DR GO; GO:0071791; F:chemokine (C-C motif) ligand 5 binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0070723; P:response to cholesterol; IEA:Ensembl.
DR InterPro; IPR002240; Chemokine_CCR5.
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; PR01110; CHEMOKINER5.
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 Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Sulfation; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..352
FT /note="C-C chemokine receptor type 5"
FT /id="PRO_0000069250"
FT TOPO_DOM 1..30
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..58
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..102
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..124
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..166
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..198
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..218
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..260
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..301
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 3
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P51681"
FT MOD_RES 10
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 14
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 336
FT /note="Phosphoserine; by BARK1"
FT /evidence="ECO:0000250|UniProtKB:P51681"
FT MOD_RES 337
FT /note="Phosphoserine; by BARK1"
FT /evidence="ECO:0000250|UniProtKB:P51681"
FT MOD_RES 342
FT /note="Phosphoserine; by BARK1"
FT /evidence="ECO:0000250|UniProtKB:P51681"
FT MOD_RES 349
FT /note="Phosphoserine; by BARK1"
FT /evidence="ECO:0000250|UniProtKB:P51681"
FT LIPID 321
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P51681"
FT LIPID 323
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P51681"
FT LIPID 324
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P51681"
FT CARBOHYD 6
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250|UniProtKB:P51681"
FT CARBOHYD 16
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT DISULFID 20..269
FT /evidence="ECO:0000250|UniProtKB:P51681"
FT DISULFID 101..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 116
FT /note="N -> S (in Ref. 1; BAD83840)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="G -> E (in Ref. 1; BAD83840)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="P -> R (in Ref. 1; BAD83840)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 40437 MW; F945BEA8BD77BF2E CRC64;
MNYQTSTPYY DIDYGTSEPC QKVNVRQIAA RLLPPLYSLV FIFGFVGNVL VVLILIDCKK
LKSMTDIYLL NLAISDLLFL LTIPFWAHYA ADQWTFGNKM CQLLTGLYYI GFFTGNFFII
LLTMDRYLAI VHAVSASKAR TVTFGVVTSG IAWVVAVLAS FPRIIFTRSQ KEGSRFTCSP
HFPPSQHHFW KNFQALKMSV LGLILPLLVM IIGYSAILKT LLRCRNEKKR HKAERLIFVI
MIVYFLFWAP YNIVLLLSTF QEFFGLNNCN SSNRLDQAMQ ITETLGMTHC CINPIIYAFV
GEKFRRYLSL FFRKHIARRF CKCCPIFQGE LPDRVSSVYT RSTGEQEISV AL
