CCR5
entrez
1234
canonical
uniprot
P51681
canonical
ensembl
ENSG00000160791
resolver
ensp
ENSP00000292303
resolver
ensp
ENSP00000404881
resolver
enst
ENST00000292303
resolver
enst
ENST00000445772
resolver
genesymbol
CCR5
resolver
genesymbol_syn
CMKBR5
resolver
hgnc
HGNC:1606
resolver
uniprot
O14692
resolver
uniprot
O14693
resolver
uniprot
O14695
resolver
uniprot
O14696
resolver
uniprot
O14697
resolver
uniprot
O14698
resolver
uniprot
O14699
resolver
uniprot
O14700
resolver
uniprot
O14701
resolver
uniprot
O14702
resolver
uniprot
O14703
resolver
uniprot
O14704
resolver
uniprot
O14705
resolver
uniprot
O14706
resolver
uniprot
O14707
resolver
uniprot
O14708
resolver
uniprot
O15538
resolver
uniprot
Q38L21
resolver
uniprot
Q9UPA4
resolver
uniprot_entry
CCR5_HUMAN
resolver
uniprot_entry
Q38L21_HUMAN
resolver
uniprot_sec
O14692
resolver
uniprot_sec
O14693
resolver
uniprot_sec
O14695
resolver
uniprot_sec
O14696
resolver
uniprot_sec
O14697
resolver
uniprot_sec
O14698
resolver
uniprot_sec
O14699
resolver
uniprot_sec
O14700
resolver
uniprot_sec
O14701
resolver
uniprot_sec
O14702
resolver
uniprot_sec
O14703
resolver
uniprot_sec
O14704
resolver
uniprot_sec
O14705
resolver
uniprot_sec
O14706
resolver
uniprot_sec
O14707
resolver
uniprot_sec
O14708
resolver
uniprot_sec
O15538
resolver
uniprot_sec
Q9UPA4
resolver
amino_acid_sequence
MDYQVSSPIYDINYYTSEPCQKINVKQIAARLLPPLYSLVFIFGFVGNMLVILILINCKRLKSMTDIYLLNLAISDLFFLLTVPFWAHYAAAQWDFGNTMCQLLTGLYFIGFFSGIFFIILLTIDRYLAVVHAVFALKARTVTFGVVTSVITWVVAVFASLPGIIFTRSQKEGLHYTCSSHFPYSQYQFWKNFQTLKIVILGLVLPLLVMVICYSGILKTLLRCRNEKKRHRAVRLIFTIMIVYFLFWAPYNIVLLLNTFQEFFGLNNCSSSNRLDQAMQVTETLGMTHCCINPIIYAFVGEKFRNYLLVFFQKHIAKRFCKCCSIFQQEAPERASSVYTRSTGEQEISVGL
uniprot
proteins
disease_involvement
DISEASE: Type 1 diabetes mellitus 22 (T1D22) [MIM:612522]: A multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical features are polydipsia, polyphagia and polyuria which result from hyperglycemia-induced osmotic diuresis and secondary thirst. These derangements result in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:19073967}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Receptor for a number of inflammatory CC-chemokines including CCL3/MIP-1-alpha, CCL4/MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. May play a role in the control of granulocytic lineage proliferation or differentiation. Participates in T-lymphocyte migration to the infection site by acting as a chemotactic receptor (PubMed:30713770). {ECO:0000269|PubMed:10383387, ECO:0000269|PubMed:11323418, ECO:0000269|PubMed:30713770, ECO:0000269|PubMed:8639485, ECO:0000269|PubMed:8663314, ECO:0000269|PubMed:8699119}.; FUNCTION: (Microbial infection) Acts as a coreceptor (CD4 being the primary receptor) of human immunodeficiency virus-1/HIV-1. {ECO:0000269|PubMed:10383387, ECO:0000269|PubMed:21763489, ECO:0000269|PubMed:8649511, ECO:0000269|PubMed:8649512, ECO:0000269|PubMed:9632396}.
uniprot
proteins
mass_dalton
40524
uniprot
proteins
mutagenesis
MUTAGEN 3; /note="Y->D: No sulfation and strongly decreases binding with CCL4 and CCL5; when associated with D-10; D-14 and D-15. Restores most CCL4 binding; when associated with D-10 and D-15."; /evidence="ECO:0000269|PubMed:10089882, ECO:0000269|PubMed:11733580"; MUTAGEN 3; /note="Y->F: No sulfation and strongly decreases binding with CCL4 and CCL5; when associated with F-10; F-14 and F-15."; /evidence="ECO:0000269|PubMed:10089882, ECO:0000269|PubMed:11733580"; MUTAGEN 6..7; /note="SS->AA: Loss of molecular mass of 2 kDa compared to wild type when treated with O-glycosidase. Dramatically reduces binding with CCL4. Loss of molecular mass of about 2 kDa as compared to wild type, dramatically reduces binding by CCL4; when associated with A-16-17-A."; /evidence="ECO:0000269|PubMed:11733580"; MUTAGEN 6; /note="S->A: Strongly decreases CCL4 binding. No change in glycosylation status."; /evidence="ECO:0000269|PubMed:11733580"; MUTAGEN 7; /note="S->A: No change in glycosylation status and binds CCL4 as efficiently as wild type."; /evidence="ECO:0000269|PubMed:11733580"; MUTAGEN 10; /note="Y->F: No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-3; F-14 and F-15. Small loss of sulfation; when associated with F-14 and F-15."; /evidence="ECO:0000269|PubMed:10089882, ECO:0000269|PubMed:11733580"; MUTAGEN 14; /note="Y->D: No sulfation and greatly decreased binding of CCL4 and CCL5; when associated with D-3; D-10 and D-14. No restoration of CCL4 binding; when associated with D-10 and D-15."; /evidence="ECO:0000269|PubMed:10089882, ECO:0000269|PubMed:11733580"; MUTAGEN 14; /note="Y->F: No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-3; F-10; and F-15. Small loss of sulfation; when associated with F-10 and F-15."; /evidence="ECO:0000269|PubMed:10089882, ECO:0000269|PubMed:11733580"; MUTAGEN 15; /note="Y->D: No sulfation and greatly decreased binding of CCL4 and CCL5; when associated with D-3; D-10 and D-14. Restored most CCL4 binding; when associated with D-3 and D-10."; /evidence="ECO:0000269|PubMed:10089882, ECO:0000269|PubMed:11733580"; MUTAGEN 15; /note="Y->F: No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-3; F-10 and F-14. Small loss of sulfation; when associated with F-10 and F-14."; /evidence="ECO:0000269|PubMed:10089882, ECO:0000269|PubMed:11733580"; MUTAGEN 16..17; /note="TS->AA: Similar decrease in molecular mass when treated with O-glycosidase as for wild type. Loss of molecular mass of about 2 kDa as compared to wild type, dramatically reduces binding by CCL4; when associated with A-6-7-A."; /evidence="ECO:0000269|PubMed:11733580"; MUTAGEN 20; /note="C->A: Decreases to 40% surface expression. No effect on conformational integrity. Disrupts binding of CCL4. Decreases cell HIV infection."; /evidence="ECO:0000269|PubMed:10383387"; MUTAGEN 101; /note="C->A: Decreases to 40% surface expression. Disrupts conformational integrity. Disrupts binding of CCL4. Decreases HIV cell infection."; /evidence="ECO:0000269|PubMed:10383387"; MUTAGEN 178; /note="C->A: Decreases to 40% surface expression. Disrupts conformational integrity. Disrupts binding of CCL4. Decreases HIV cell infection."; /evidence="ECO:0000269|PubMed:10383387"; MUTAGEN 269; /note="C->A: Decreases to 40% surface expression. No effect on conformational integrity. Disrupts binding of CCL4. Decreases cell HIV infection."; /evidence="ECO:0000269|PubMed:10383387"; MUTAGEN 321; /note="C->A: Small reduction in palmitoylation. Cell surface expression reduced by 50%. Greatly reduced palmitoylation. Cell surface expression greatly reduced; when associated with A-323 or A-324. No palmitoylation. Cell surface expression greatly reduced. HIV entry reduced by 50%; when associated with A-323 and A-324."; /evidence="ECO:0000269|PubMed:11323418"; MUTAGEN 323; /note="C->A: Small reduction in palmitoylation. Cell surface expression reduced by 50%. Greatly reduced palmitoylation. Cell surface expression greatly reduced; when associated with A-321 or A-324. No palmitoylation. Cell surface expression greatly reduced. HIV entry reduced by 50%; when associated with A-321 and A-324."; /evidence="ECO:0000269|PubMed:11323418"; MUTAGEN 324; /note="C->A: Small reduction in palmitoylation. Cell surface expression reduced by 50%. Greatly reduced palmitoylation. Cell surface expression greatly reduced; when associated with A-321 or A-323. No palmitoylation. Cell surface expression greatly reduced. HIV entry reduced by 50%; when associated with A-321 and A-323."; /evidence="ECO:0000269|PubMed:11323418"; MUTAGEN 336; /note="S->A: APO-RANTES-stimulated phosphorylation reduced by 15%; APO-RANTES-stimulated phosphorylation reduced by 30-50%; when associated with A-337 or A-342 or A-349; APO-RANTES-stimulated phosphorylation reduced by 80%; when associated with A-337 and A-342 or A-349; No APO-RANTES-stimulated phosphorylation; when associated with A-337; A-342 and A349; abolishes interaction with ARRB2; when associated with S-337; S-342 and S-349."; /evidence="ECO:0000269|PubMed:10085131, ECO:0000269|PubMed:11448957"; MUTAGEN 337; /note="S->A: APO-RANTES-stimulated phosphorylation reduced by 18%; APO-RANTES-stimulated phosphorylation reduced by 30-50% on APO-RANTES stimulation; when associated with A-336 or A-342 or A-349; APO-RANTES-stimulated phosphorylation reduced by 80%; when associated with A-336 and A-342 or A-349; No APO-RANTES-stimulated phosphorylation; when associated with A-336; A-342 and A349; abolishes interaction with ARRB2; when associated with S-336; S-342 and S-349."; /evidence="ECO:0000269|PubMed:10085131, ECO:0000269|PubMed:11448957"; MUTAGEN 342; /note="S->A: APO-RANTES-stimulated phosphorylation reduced by 42%. Phosphorylation reduced by 50% on APO-RANTES stimulation; when associated with A-336 or A-337 or A-349; APO-RANTES-stimulated phosphorylation reduced by 80% when associated with A-336 and A-337 or A-349; No APO-RANTES-stimulated phosphorylation; when associated with A-336; A-337 and A349; abolishes interaction with ARRB2; when associated with S-336; S-337 and S-349."; /evidence="ECO:0000269|PubMed:10085131, ECO:0000269|PubMed:11448957"; MUTAGEN 349; /note="S->A: APO-RANTES-stimulated phosphorylation reduced by 43%; APO-RANTES-stimulated phosphorylation reduced by 30-50%; when associated with A-336 or A-337 or A-342; APO-RANTES-stimulated phosphorylation reduced by 80%; when associated with A-336 and A-337 or A-342; No APO-RANTES-stimulated phosphorylation stimulation; when associated with A-336; A-337 and A347; abolishes interaction with ARRB2; when associated with S-336; S-337 and S-342."; /evidence="ECO:0000269|PubMed:10085131, ECO:0000269|PubMed:11448957
uniprot
proteins
post_translational_modification
PTM: Sulfated on at least 2 of the N-terminal tyrosines. Sulfation contributes to the efficiency of HIV-1 entry and is required for efficient binding of the chemokines, CCL3 and CCL4. {ECO:0000269|PubMed:10089882, ECO:0000269|PubMed:11733580, ECO:0000269|PubMed:21763489}.; PTM: O-glycosylated, but not N-glycosylated. Ser-6 appears to be the major site even if Ser-7 may be also O-glycosylated. Also sialylated glycans present which contribute to chemokine binding. Thr-16 and Ser-17 may also be glycosylated and, if so, with small moieties such as a T-antigen. {ECO:0000269|PubMed:10089882, ECO:0000269|PubMed:11733580}.; PTM: Palmitoylation in the C-terminal is important for cell surface expression, and to a lesser extent, for HIV entry. {ECO:0000269|PubMed:11323418}.; PTM: Phosphorylation on serine residues in the C-terminal is stimulated by binding CC chemokines especially by APO-RANTES. {ECO:0000269|PubMed:10085131}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
10085131
uniprot
proteins
pubmed
10089882
uniprot
proteins
pubmed
10383387
uniprot
proteins
pubmed
10917742
uniprot
proteins
pubmed
11323418
uniprot
proteins
pubmed
11369664
uniprot
proteins
pubmed
11448957
uniprot
proteins
pubmed
11733580
uniprot
proteins
pubmed
12496074
uniprot
proteins
pubmed
14517611
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15757671
uniprot
proteins
pubmed
16144840
uniprot
proteins
pubmed
16418398
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
17092330
uniprot
proteins
pubmed
19073967
uniprot
proteins
pubmed
21763489
uniprot
proteins
pubmed
22496149
uniprot
proteins
pubmed
24030490
uniprot
proteins
pubmed
24405750
uniprot
proteins
pubmed
30713770
uniprot
proteins
pubmed
8639485
uniprot
proteins
pubmed
8649511
uniprot
proteins
pubmed
8649512
uniprot
proteins
pubmed
8663314
uniprot
proteins
pubmed
8699119
uniprot
proteins
pubmed
8751444
uniprot
proteins
pubmed
8756719
uniprot
proteins
pubmed
9207783
uniprot
proteins
pubmed
9287217
uniprot
proteins
pubmed
9343222
uniprot
proteins
pubmed
9359654
uniprot
proteins
pubmed
9388201
uniprot
proteins
pubmed
9399903
uniprot
proteins
pubmed
9632396
uniprot
proteins
sequence_length
352
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10383387, ECO:0000269|PubMed:11323418}; Multi-pass membrane protein {ECO:0000269|PubMed:11323418}.
uniprot
proteins
transmembrane_region
TRANSMEM 31..58; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 69..89; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 103..124; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 142..166; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 199..218; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 236..260; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 278..301; /note="Helical; Name=7"; /evidence="ECO:0000255
uniprot
proteins