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CCR5_ALLLH
ID   CCR5_ALLLH              Reviewed;         352 AA.
AC   Q9XT76;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 82.
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   Allochrocebus lhoesti (L'Hoest's monkey) (Cercopithecus lhoesti).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Allochrocebus.
OX   NCBI_TaxID=100224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10408730; DOI=10.1089/088922299310647;
RA   Mueller-Trutwin M.-C., Corbet S., Hansen J., Georges-Courbot M.-C.,
RA   Diop O., Rigoulet J., Barre-Sinoussi F., Fomsgaard A.;
RT   "Mutations in CCR5-coding sequences are not associated with SIV carrier
RT   status in African nonhuman primates.";
RL   AIDS Res. Hum. Retroviruses 15:931-939(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; Multi-pass membrane protein.
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; AF081579; AAD45497.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9XT76; -.
DR   SMR; Q9XT76; -.
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_0000256649"
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   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   DISULFID        20..269
FT                   /evidence="ECO:0000250|UniProtKB:P51681"
FT   DISULFID        101..178
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   352 AA;  40409 MW;  2D354E5128C779E0 CRC64;
     MDYQVSSPTY DIDYYTSEPC QKINVKQIAA RLLPPLYSLV FIFGFVGNIL VVLILINCKR
     LKSMTDIYLL NLAISDLLFL LTIPFWAHYA AAQWDFGNTM CQLLTGLYLI GFFSGIFFII
     LLTIDRYLAI VHAVFALKAR TVTFGLVTSV ITWVVAVFAS LPGIIFTRSQ REGLHYTCSS
     HFPSSQYQFW KNFQTLKIVI LGLVLPLLVM VICYSGILKT LLRCRNEKKR HRAVRLIFTI
     MIVYFLFWAP YNIVLLLNTF QEFFGLNNCS SSNRLDQAMQ VTETLGMTHC CINPIIYAFV
     GEKFRNYLLV FFQKHLAKRF CKCCSIFQQE APERASSVYT RSTGEQETTV GL
 
 
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