Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00881
Entry Name
UniProt Accession
Theoretical PI
9.21
Molecular Weight
40524.05
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
C-C chemokine receptor type 5
Protein Synonyms/Alias
C-C CKR-5; CC-CKR-5; CCR-5; CCR5; CHEMR13; HIV-1 fusion coreceptor; CD195;
Gene Name
CCR5
Gene Synonyms/Alias
CMKBR5;
Created Date
01-OCT-1996
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
321
Canonical
KHIAKRFCKCCSIFQ
[1]
S-Palmitoylation
323
Canonical
IAKRFCKCCSIFQQE
[1]
S-Palmitoylation
324
Canonical
AKRFCKCCSIFQQEA
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Blanpain C, Wittamer V, Vanderwinden JM, Boom A, Renneboog B, Lee B, Le PoulE, El Asmar L, Govaerts C, Vassart G, Doms RW, Parmentier M. Palmitoylation ofCCR5 is critical for receptor trafficking and efficient activation ofintracellular signaling pathways. J Biol Chem. 2001 Jun 29;276(26):23795-804.Epub 2001 Apr 25.[PMID:11323418]
Functional Description
Receptor for a number of inflammatory CC-chemokines including MIP-1-alpha, 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. Acts as a coreceptor (CD4 being the primary receptor) for HIV-1 R5 isolates.
Sequence Annotation
Topological domain: 1 30 Extracellular.
Transmembrane: 31 58 Helical; Name=1.
Topological domain: 59 68 Cytoplasmic.
Transmembrane: 69 89 Helical; Name=2.
Topological domain: 90 102 Extracellular.
Transmembrane: 103 124 Helical; Name=3.
Topological domain: 125 141 Cytoplasmic.
Transmembrane: 142 166 Helical; Name=4.
Topological domain: 167 198 Extracellular.
Transmembrane: 199 218 Helical; Name=5.
Topological domain: 219 235 Cytoplasmic.
Transmembrane: 236 260 Helical; Name=6.
Topological domain: 261 277 Extracellular.
Transmembrane: 278 301 Helical; Name=7.
Topological domain: 302 352 Cytoplasmic.
Modified residue: 3 3 Sulfotyrosine.
Modified residue: 10 10 Sulfotyrosine.
Modified residue: 14 14 Sulfotyrosine.
Modified residue: 15 15 Sulfotyrosine.
Modified residue: 336 336 Phosphoserine; by BARK1.
Modified residue: 337 337 Phosphoserine; by BARK1.
Modified residue: 342 342 Phosphoserine; by BARK1.
Modified residue: 349 349 Phosphoserine; by BARK1.
Protein Length
352 AA.
Protein Sequence
(Canonical)
MDYQVSSPIY DINYYTSEPC QKINVKQIAA RLLPPLYSLV FIFGFVGNML VILILINCKR  60
LKSMTDIYLL NLAISDLFFL LTVPFWAHYA AAQWDFGNTM CQLLTGLYFI GFFSGIFFII  120
LLTIDRYLAV VHAVFALKAR TVTFGVVTSV ITWVVAVFAS LPGIIFTRSQ KEGLHYTCSS  180
HFPYSQYQFW KNFQTLKIVI LGLVLPLLVM VICYSGILKT LLRCRNEKKR HRAVRLIFTI  240
MIVYFLFWAP YNIVLLLNTF QEFFGLNNCS SSNRLDQAMQ VTETLGMTHC CINPIIYAFV  300
GEKFRNYLLV FFQKHIAKRF CKCCSIFQQE APERASSVYT RSTGEQEISV GL          352
FASTA
(Canonical)
>LipidDB-9606-00881|P51681
MDYQVSSPIYDINYYTSEPCQKINVKQIAARLLPPLYSLVFIFGFVGNMLVILILINCKR
LKSMTDIYLLNLAISDLFFLLTVPFWAHYAAAQWDFGNTMCQLLTGLYFIGFFSGIFFII
LLTIDRYLAVVHAVFALKARTVTFGVVTSVITWVVAVFASLPGIIFTRSQKEGLHYTCSS
HFPYSQYQFWKNFQTLKIVILGLVLPLLVMVICYSGILKTLLRCRNEKKRHRAVRLIFTI
MIVYFLFWAPYNIVLLLNTFQEFFGLNNCSSSNRLDQAMQVTETLGMTHCCINPIIYAFV
GEKFRNYLLVFFQKHIAKRFCKCCSIFQQEAPERASSVYTRSTGEQEISVGL
Gene Ontology
GO:0009986; C:cell surface; IDA:UniProtKB
GO:0005737; C:cytoplasm; TAS:ProtInc
GO:0005768; C:endosome; IDA:UniProtKB
GO:0009897; C:external side of plasma membrane; IDA:UniProtKB
GO:0005887; C:integral component of plasma membrane; TAS:ProtInc
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0003779; F:actin binding; IDA:UniProtKB
GO:0019957; F:C-C chemokine binding; IPI:UniProtKB
GO:0016493; F:C-C chemokine receptor activity; NAS:UniProtKB
GO:0071791; F:chemokine (C-C motif) ligand 5 binding; IPI:UniProtKB
GO:0004950; F:chemokine receptor activity; TAS:ProtInc
GO:0015026; F:coreceptor activity; TAS:ProtInc
GO:0004435; F:phosphatidylinositol phospholipase C activity; TAS:ProtInc
GO:0006816; P:calcium ion transport; IDA:UniProtKB
GO:0019722; P:calcium-mediated signaling; IDA:UniProtKB
GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc
GO:0007267; P:cell-cell signaling; IDA:UniProtKB
GO:0006968; P:cellular defense response; TAS:ProtInc
GO:0071222; P:cellular response to lipopolysaccharide; IEP:UniProtKB
GO:0070098; P:chemokine-mediated signaling pathway; IDA:GOC
GO:0006935; P:chemotaxis; TAS:ProtInc
GO:0002407; P:dendritic cell chemotaxis; TAS:BHF-UCL
GO:0030260; P:entry into host cell; TAS:Reactome
GO:0007186; P:G-protein coupled receptor signaling pathway; IMP:UniProtKB
GO:0006955; P:immune response; TAS:ProtInc
GO:0006954; P:inflammatory response; TAS:ProtInc
GO:0000165; P:MAPK cascade; IEP:UniProtKB
GO:0007204; P:positive regulation of cytosolic calcium ion concentration; TAS:ProtInc
GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IDA:UniProtKB
GO:0070723; P:response to cholesterol; IMP:UniProtKB
GO:0023052; P:signaling; IEP:UniProtKB
GO:0016032; P:viral process; TAS:Reactome
Interpro
InterPro; IPR002240; Chemokine_CCR5
InterPro; IPR000355; Chemokine_rcpt
InterPro; IPR000276; GPCR_Rhodpsn
InterPro; IPR017452; GPCR_Rhodpsn_7TM
Pfam
Pfam; PF00001; 7tm_1;
SMART
PROSITE
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1;
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2;
PRINTS
PRINTS; PR00657; CCCHEMOKINER;
PRINTS; PR01110; CHEMOKINER5;
PRINTS; PR00237; GPCRRHODOPSN;