CCR5_THEGE
ID CCR5_THEGE Reviewed; 352 AA.
AC Q95NC1;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 Theropithecus gelada (Gelada baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Theropithecus.
OX NCBI_TaxID=9565;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10486970; DOI=10.1093/oxfordjournals.molbev.a026205;
RA Zhang Y.-W., Ryder O.A., Zhang Y.-P.;
RT "Sequence evolution of the CCR5 chemokine receptor gene in primates.";
RL Mol. Biol. Evol. 16:1145-1154(1999).
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; AF177891; AAK43374.1; -; Genomic_DNA.
DR AlphaFoldDB; Q95NC1; -.
DR SMR; Q95NC1; -.
DR Ensembl; ENSTGET00000017298; ENSTGEP00000014437; ENSTGEG00000011733.
DR Proteomes; UP000694411; Chromosome 2.
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:0016493; F:C-C chemokine receptor activity; ISS:UniProtKB.
DR GO; GO:0071791; F:chemokine (C-C motif) ligand 5 binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:Ensembl.
DR GO; GO:0007267; P:cell-cell signaling; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IEA:InterPro.
DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
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 3: Inferred from homology;
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_0000069282"
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:0000250|UniProtKB:P51681"
FT DISULFID 20..269
FT /evidence="ECO:0000250|UniProtKB:P51681"
FT DISULFID 101..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 352 AA; 40475 MW; 4D3643B6C13E90D5 CRC64;
MDYQVSSPTY DIDYYTSEPC QKINVKQIAG RLLPPLYSLV FIFGFVGNIL VVLILINCKR
LKSMTDIYLL NLAISDLLFL LTVPFWAHYA AAQWDFGNTM CQLLTGLYFI GFFSGIFFII
LLTIDRYLAI VHAVFALKAR TVTFGVVTSV ITWVVAVFAS LPGIIFTRSQ REGLHYTCSS
HFPYSQYQFW KNFQTLKIVI LGLVLPLLVM VICYSGILKT LLRCRNEKKR HRAVRLIFTI
MIVYFLFWAP YNIVLLLNTF QEFFGLNNCS SSNRLDQAMQ VTETLGMTHC CINPIIYAFV
GEKFRNYLLV FFQKHIAKRF CKCCSIFQQE APERASSVYT RSTGEQEISV GL
