CCR5_MACMU
ID CCR5_MACMU Reviewed; 352 AA.
AC P61813; O02746; P79436;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
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 Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9032394; DOI=10.1128/jvi.71.3.2522-2527.1997;
RA Marcon L., Choe H., Martin K.A., Farzan M., Ponath P.D., Wu L., Newman W.,
RA Gerard N., Gerard C., Sodroski J.;
RT "Utilization of C-C chemokine receptor 5 by the envelope glycoproteins of a
RT pathogenic simian immunodeficiency virus, SIVmac239.";
RL J. Virol. 71:2522-2527(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Indian macaque;
RX PubMed=9060623; DOI=10.1128/jvi.71.4.2705-2714.1997;
RA Chen Z., Zhou P., Ho D.D., Landau N.R., Marx P.A.;
RT "Genetically divergent strains of simian immunodeficiency virus use CCR5 as
RT a coreceptor for entry.";
RL J. Virol. 71:2705-2714(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11461684; DOI=10.1089/088922201750290104;
RA Margulies B.J., Hauer D.A., Clements J.E.;
RT "Identification and comparison of eleven rhesus macaque chemokine
RT receptors.";
RL AIDS Res. Hum. Retroviruses 17:981-986(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9108095; DOI=10.1073/pnas.94.8.4005;
RA Edinger A.L., Amedee A., Miller K., Doranz B.J., Endres M., Sharron M.,
RA Samson M., Lu Z.-H., Clements J.E., Murphey-Corb M., Peiper S.C.,
RA Parmentier M., Broder C.C., Doms R.W.;
RT "Differential utilization of CCR5 by macrophage and T cell tropic simian
RT immunodeficiency virus strains.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:4005-4010(1997).
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. Participates in T-lymphocyte migration to the
CC infection site by acting as a chemotactic receptor.
CC {ECO:0000250|UniProtKB:P51681}.
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: 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 -!- PTM: O-glycosylated, but not N-glycosylated. Ser-6 appears to be the
CC major site even if Ser-7 may be also O-glycosylated. Also sialylated
CC glycans present which contribute to chemokine binding. Thr-16 and Ser-
CC 17 may also be glycosylated and, if so, with small moieties such as a
CC T-antigen. {ECO:0000250|UniProtKB:P51681}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U77672; AAC51109.1; -; Genomic_DNA.
DR EMBL; U73739; AAC51158.1; -; mRNA.
DR EMBL; U96762; AAC34132.1; -; mRNA.
DR EMBL; AF005662; AAB62556.1; -; Genomic_DNA.
DR RefSeq; NP_001036238.2; NM_001042773.3.
DR RefSeq; NP_001296331.1; NM_001309402.1.
DR AlphaFoldDB; P61813; -.
DR SMR; P61813; -.
DR ChEMBL; CHEMBL3217397; -.
DR DrugCentral; P61813; -.
DR GeneID; 735311; -.
DR KEGG; mcc:735311; -.
DR CTD; 1234; -.
DR InParanoid; P61813; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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: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:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
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_0000069264"
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 15
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 7
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000305"
FT CARBOHYD 16
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 17
FT /note="O-linked (GalNAc...) serine"
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 241
FT /note="M -> I (in Ref. 3; AAC34132)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="I -> M (in Ref. 3; AAC34132)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 40507 MW; 58B96C85909FACB2 CRC64;
MDYQVSSPTY DIDYYTSEPC QKINVKQIAA RLLPPLYSLV FIFGFVGNIL VVLILINCKR
LKSMTDIYLL NLAISDLLFL LTVPFWAHYA AAQWDFGNTM CQLLTGLYFI GFFSGIFFII
LLTIDRYLAI VHAVFALKAR TVTFGVVTSV ITWVVAVFAS LPGIIFTRSQ REGLHYTCSS
HFPYSQYQFW KNFQTLKMVI LGLVLPLLVM VICYSGILKT LLRCRNEKKR HRAVRLIFTI
MIVYFLFWAP YNIVLLLNTF QEFFGLNNCS SSNRLDQAMQ VTETLGMTHC CINPIIYAFV
GEKFRNYLLV FFQKHIAKRF CKCCSIFQQE APERASSVYT RSTGEQEISV GL
