Linked Life Data

CPATH-1548

Source:http://cbio.mskcc.org/cpath#CPATH-1548

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
http://www.biopax.org/relea...
http://www.biopax.org/relea...
C-C chemokine receptor type 5
http://www.biopax.org/relea...
CCR5_HUMAN
http://www.biopax.org/relea...
http://www.biopax.org/relea...
C-C CKR-5, CC-CKR-5, CCR-5, CCR5, CD195, CHEMR13, HIV-1 fusion coreceptor
http://www.biopax.org/relea...
FUNCTION: 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. SUBUNIT: Interacts with PRAF2. Interacts with HIV-1 surface protein gp120. Efficient ligand binding to CCL3/MIP-1alpha and CCL4/MIP-1beta requires sulfation, O-glycosylation and sialic acid modifications. Glycosylation on Ser-6 is required for efficient binding of CCL4. Interacts with ADRBK1. Interacts with ARRB1 and ARRB2. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Highly expressed in spleen, thymus, in the myeloid cell line THP-1, in the promyeloblastic cell line KG-1A and on CD4+ and CD8+ T-cells. Medium levels in peripheral blood leukocytes and in small intestine. Low levels in ovary and lung. 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. PTM: O-glycosylated, but not N-glycosylated. Ser-6 appears to be the major site. 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. PTM: Palmitoylation in the C-terminal is important for cell surface expression, and to a lesser extent, for HIV entry. PTM: Phosphorylation on serine residues in the C-terminal is stimulated by binding CC chemokines especially by APO-RANTES. POLYMORPHISM: Variations in CCR5 are associated with resistance or susceptibility to immunodeficiency virus type 1 (resistance or susceptibility to HIV-1) [MIM:609423]. Variations in CCR5 gene also influence the rate of progression to AIDS after infection. POLYMORPHISM: Ser-60 variant, a naturally occurring mutation in a conserved residue in the first intracellular domain of CCR5, results in reduced amounts of the protein in the membrane and consequently may be associated with reduced susceptibility to infection by microbes that depend on these molecules as their receptors. POLYMORPHISM: Variations in CCR5 are associated with susceptibility to West Nile virus (WNV) infection [MIM:610379]. DISEASE: Genetic variation in CCR5 is associated with suseptibility to diabetes mellitus insulin-dependent type 22 (IDDM22) [MIM:612522]. A multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical fetaures 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. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. WEB RESOURCE: Name=Wikipedia; Note=CC chemokine receptors entry; URL="http://en.wikipedia.org/wiki/CC_chemokine_receptors"; WEB RESOURCE: Name=Wikipedia; Note=CCR5 receptor entry; URL="http://en.wikipedia.org/wiki/CCR5"; GENE SYNONYMS: CMKBR5. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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