OCRL

OCRL
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4CMN, 2KIE, 2QV2, 3QBT, 3QIS
Identifiers
Aliases	OCRL, LOCR, NPHL2, OCRL-1, OCRL1, oculocerebrorenal syndrome of Lowe, inositol polyphosphate-5-phosphatase, OCRL inositol polyphosphate-5-phosphatase, INPP5F, Dent-2, DENT2
External IDs	OMIM: 300535 MGI: 109589 HomoloGene: 233 GeneCards: OCRL
Gene location (Human) Chr. X chromosome (human) Band Xq26.1 Start 129,539,849 bp End 129,592,561 bp
Gene location (Mouse) Chr. X chromosome (mouse) Band X|X A5 Start 47,912,387 bp End 47,965,868 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Brodmann area 10 gastric mucosa frontal pole islet of Langerhans anterior pituitary left adrenal gland middle frontal gyrus left uterine tube ganglionic eminence rectum Top expressed in otolith organ utricle superior frontal gyrus ventromedial nucleus adrenal gland hand secondary oocyte cerebellar cortex arcuate nucleus ventral tegmental area More reference expression data BioGPS n/a
Gene ontology Molecular function phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity protein binding hydrolase activity GTPase activator activity inositol-1,4,5-trisphosphate 5-phosphatase activity inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity phosphatidylinositol phosphate 4-phosphatase activity phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity inositol phosphate phosphatase activity Cellular component cytoplasm cytosol endosome phagocytic vesicle membrane Golgi apparatus cell projection early endosome membrane membrane plasma membrane cilium Golgi-associated vesicle trans-Golgi network early endosome Golgi stack clathrin-coated pit cytoplasmic vesicle nucleus clathrin-coated vesicle photoreceptor outer segment Biological process lipid metabolism regulation of GTPase activity in utero embryonic development inositol phosphate metabolic process cell projection organization phosphatidylinositol dephosphorylation phosphatidylinositol biosynthetic process regulation of small GTPase mediated signal transduction signal transduction positive regulation of GTPase activity phosphatidylinositol-3-phosphate biosynthetic process cilium assembly membrane organization inositol phosphate dephosphorylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4952 320634 Ensembl ENSG00000122126 ENSMUSG00000001173 UniProt Q01968 Q6NVF0 RefSeq (mRNA) NM_000276 NM_001587 NM_001318784 NM_177215 RefSeq (protein) NP_000267 NP_001305713 NP_001578 NP_796189 Location (UCSC) Chr X: 129.54 – 129.59 Mb Chr X: 47.91 – 47.97 Mb PubMed search
Wikidata
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Inositol polyphosphate 5-phosphatase OCRL-1, also known as Lowe oculocerebrorenal syndrome protein, is an enzyme encoded by the OCRL gene located on the X chromosome in humans.

This gene encodes an inositol polyphosphate 5-phosphatase. The responsible gene locus is at Xq26.1. This phosphatase enzyme is in part responsible for regulating membrane trafficking actin polymerization, and is located in several subcellular parts of the trans-Golgi network.

Deficiencies in OCRL-1 may cause with oculocerebrorenal syndrome and also have been linked to Dent's disease.

Further reading

• Ross MT, Grafham DV, Coffey AJ, et al. (2005). "The DNA sequence of the human X chromosome". Nature. 434 (7031): 325–37. Bibcode:2005Natur.434..325R. doi:10.1038/nature03440. PMC 2665286. PMID 15772651.
• Erdmann KS, Mao Y, McCrea HJ, et al. (2007). "A role of the Lowe syndrome protein OCRL in early steps of the endocytic pathway". Dev. Cell. 13 (3): 377–90. doi:10.1016/j.devcel.2007.08.004. PMC 2025683. PMID 17765681.
• Hyvola N, Diao A, McKenzie E, et al. (2006). "Membrane targeting and activation of the Lowe syndrome protein OCRL1 by rab GTPases". EMBO J. 25 (16): 3750–61. doi:10.1038/sj.emboj.7601274. PMC 1553191. PMID 16902405.
• Mao Y, Balkin DM, Zoncu R, et al. (2009). "A PH domain within OCRL bridges clathrin-mediated membrane trafficking to phosphoinositide metabolism". EMBO J. 28 (13): 1831–42. doi:10.1038/emboj.2009.155. PMC 2711190. PMID 19536138.
• Suchy SF, Cronin JC, Nussbaum RL (2009). "Abnormal bradykinin signalling in fibroblasts deficient in the PIP(2) 5-phosphatase, ocrl1". J. Inherit. Metab. Dis. 32 (2): 280–8. doi:10.1007/s10545-009-1058-3. PMID 19172411. S2CID 31583330.
• Wu F, Reed AA, Williams SE, et al. (2009). "Mutational analysis of CLC-5, cofilin and CLC-4 in patients with Dent's disease". Nephron Physiol. 112 (4): 53–62. doi:10.1159/000225944. PMID 19546591. S2CID 24946606.
• Coon BG, Mukherjee D, Hanna CB, et al. (2009). "Lowe syndrome patient fibroblasts display Ocrl1-specific cell migration defects that cannot be rescued by the homologous Inpp5b phosphatase". Hum. Mol. Genet. 18 (23): 4478–91. doi:10.1093/hmg/ddp407. PMC 7289333. PMID 19700499.
• Tosetto E, Addis M, Caridi G, et al. (2009). "Locus heterogeneity of Dent's disease: OCRL1 and TMEM27 genes in patients with no CLCN5 mutations". Pediatr. Nephrol. 24 (10): 1967–73. doi:10.1007/s00467-009-1228-4. PMID 19582483. S2CID 25741167.
• Faucherre A, Desbois P, Nagano F, et al. (2005). "Lowe syndrome protein Ocrl1 is translocated to membrane ruffles upon Rac GTPase activation: a new perspective on Lowe syndrome pathophysiology". Hum. Mol. Genet. 14 (11): 1441–8. doi:10.1093/hmg/ddi153. PMID 15829501.
• Shrimpton AE, Hoopes RR, Knohl SJ, et al. (2009). "OCRL1 mutations in Dent 2 patients suggest a mechanism for phenotypic variability". Nephron Physiol. 112 (2): 27–36. doi:10.1159/000213506. PMID 19390221. S2CID 21834343.
• Sekine T, Nozu K, Iyengar R, et al. (2007). "OCRL1 mutations in patients with Dent disease phenotype in Japan". Pediatr. Nephrol. 22 (7): 975–80. doi:10.1007/s00467-007-0454-x. PMID 17384968. S2CID 20047399.
• Chabaâ L, Monnier N, Dahri S, et al. (2006). "[Oculo-cerebro-renal Lowe syndrome: clinical, biochemical and molecular studies in a Moroccan patient]". Ann. Biol. Clin. (Paris). 64 (1): 53–9. PMID 16420990.
• Choudhury R, Diao A, Zhang F, et al. (2005). "Lowe syndrome protein OCRL1 interacts with clathrin and regulates protein trafficking between endosomes and the trans-Golgi network". Mol. Biol. Cell. 16 (8): 3467–79. doi:10.1091/mbc.E05-02-0120. PMC 1182289. PMID 15917292.
• Sethi SK, Bagga A, Gulati A, et al. (2008). "Mutations in OCRL1 gene in Indian children with Lowe syndrome". Clin. Exp. Nephrol. 12 (5): 358–62. doi:10.1007/s10157-008-0059-0. PMID 18500547. S2CID 3458176.
• Cui S, Guerriero CJ, Szalinski CM, et al. (2010). "OCRL1 function in renal epithelial membrane traffic". Am. J. Physiol. Renal Physiol. 298 (2): F335-45. doi:10.1152/ajprenal.00453.2009. PMC 2822509. PMID 19940034.
• McCrea HJ, Paradise S, Tomasini L, et al. (2008). "All known patient mutations in the ASH-RhoGAP domains of OCRL affect targeting and APPL1 binding". Biochem. Biophys. Res. Commun. 369 (2): 493–9. doi:10.1016/j.bbrc.2008.02.067. PMC 2442618. PMID 18307981.
• Hoopes RR, Shrimpton AE, Knohl SJ, et al. (2005). "Dent Disease with mutations in OCRL1". Am. J. Hum. Genet. 76 (2): 260–7. doi:10.1086/427887. PMC 1196371. PMID 15627218.
• Levtchenko EN, Monnens LA, Bökenkamp A, Knoers NV (2007). "[From gene to disease; Dent's disease caused by abnormalities in the CLCN5 and OCRL1 genes]". Ned Tijdschr Geneeskd. 151 (43): 2377–80. PMID 18019214.
• Choudhury R, Noakes CJ, McKenzie E, et al. (2009). "Differential clathrin binding and subcellular localization of OCRL1 splice isoforms". J. Biol. Chem. 284 (15): 9965–73. doi:10.1074/jbc.M807442200. PMC 2665120. PMID 19211563.
• Swan LE, Tomasini L, Pirruccello M, et al. (2010). "Two closely related endocytic proteins that share a common OCRL-binding motif with APPL1". Proc. Natl. Acad. Sci. U.S.A. 107 (8): 3511–6. Bibcode:2010PNAS..107.3511S. doi:10.1073/pnas.0914658107. PMC 2840420. PMID 20133602.

External links

• GeneReviews/NCBI/NIH/UW entry on Lowe Syndrome
• OCRL+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
• PDBe-KB provides an overview of all the structure information available in the PDB for Human Inositol polyphosphate 5-phosphatase OCRL-1