CCR5_ATEGE
ID CCR5_ATEGE Reviewed; 352 AA.
AC Q95NC4;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 83.
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 Ateles geoffroyi (Black-handed spider monkey) (Geoffroy's spider monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Atelidae;
OC Atelinae; Ateles.
OX NCBI_TaxID=9509;
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. Ser-17 may also
CC be glycosylated and, if so, with small moieties such as a T-antigen.
CC {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; AF177885; AAK43368.1; -; Genomic_DNA.
DR AlphaFoldDB; Q95NC4; -.
DR SMR; Q95NC4; -.
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:0016493; F:C-C chemokine receptor activity; ISS:UniProtKB.
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 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; Sulfation;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..352
FT /note="C-C chemokine receptor type 5"
FT /id="PRO_0000069248"
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 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; 40441 MW; F0A686CB4FE3964B CRC64;
MDYQVSSPIY DIDYGASEPC RKTDVKQMGA HLLPPLYSMV FLFGFVGNML VVLILVNCKR
PKSMTDIYLL NLAISDLLFL FTVPFWAHYA AGQWDFGNTM CQFLTGLYFI GFFSGIFFII
LLTIDRYLAI VHAVFALKAR TVTFGVMTSV ITWVVAVFAS LPGIIFTRSQ KEGYHYTCSP
HFPFGQYQFW KNFETLKMVI LGLVLPLLVM VICYSGILKT LLRCRNEKKR HRAVRLIFTI
MIVYFLFWAP YNIVLLLNTY QEFFGLNNCS SSNRLDQAMQ VTETLGMTHC CVNPIIYAFV
GEKFRNYLLV FFQKHIAKCF CECCSIFQKE APERANSVYT RSTGEQEISV GL
