[1]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
TISSUE=Kidney;
DOI=10.1038/358239a0; PubMed=1321346 [NCBI, ExPASy, EBI, Israel, Japan]
Attree O.,
Olivos I.M.,
Okabe I.,
Bailey L.C.,
Nelson D.L.,
Lewis R.A.,
McInnes R.R.,
Nussbaum R.L.;
"The Lowe's oculocerebrorenal syndrome gene encodes a protein highly homologous to inositol polyphosphate-5-phosphatase.";
Nature 358:239-242(1992).
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[2]
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SEQUENCE REVISION TO 585.
Attree O.,
Olivos I.M.,
Okabe I.,
Bailey L.C.,
Nelson D.L.,
Lewis R.A.,
McInnes R.R.,
Nussbaum R.L.;
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
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[3]
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NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
TISSUE=Brain;
DOI=10.1007/s004390050329; PubMed=9048911 [NCBI, ExPASy, EBI, Israel, Japan]
Nussbaum R.L.,
Orrison B.M.,
Janne P.A.,
Charnas L.R.,
Chinault A.C.;
"Physical mapping and genomic structure of the Lowe syndrome gene OCRL1.";
Hum. Genet. 99:145-150(1997).
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[4]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03440; PubMed=15772651 [NCBI, ExPASy, EBI, Israel, Japan]
Ross M.T.,
Grafham D.V.,
Coffey A.J.,
Scherer S.,
McLay K.,
Muzny D.,
Platzer M.,
Howell G.R.,
Burrows C.,
Bird C.P.,
Frankish A.,
Lovell F.L.,
Howe K.L.,
Ashurst J.L.,
Fulton R.S.,
Sudbrak R.,
Wen G.,
Jones M.C.,
Hurles M.E., ![]()
Andrews T.D.,
Scott C.E.,
Searle S.,
Ramser J.,
Whittaker A.,
Deadman R.,
Carter N.P.,
Hunt S.E.,
Chen R.,
Cree A.,
Gunaratne P.,
Havlak P.,
Hodgson A.,
Metzker M.L.,
Richards S.,
Scott G.,
Steffen D.,
Sodergren E.,
Wheeler D.A.,
Worley K.C.,
Ainscough R.,
Ambrose K.D.,
Ansari-Lari M.A.,
Aradhya S.,
Ashwell R.I.,
Babbage A.K.,
Bagguley C.L.,
Ballabio A.,
Banerjee R.,
Barker G.E.,
Barlow K.F.,
Barrett I.P.,
Bates K.N.,
Beare D.M.,
Beasley H.,
Beasley O.,
Beck A.,
Bethel G.,
Blechschmidt K.,
Brady N.,
Bray-Allen S.,
Bridgeman A.M.,
Brown A.J.,
Brown M.J.,
Bonnin D.,
Bruford E.A.,
Buhay C.,
Burch P.,
Burford D.,
Burgess J.,
Burrill W.,
Burton J.,
Bye J.M.,
Carder C.,
Carrel L.,
Chako J.,
Chapman J.C.,
Chavez D.,
Chen E.,
Chen G.,
Chen Y.,
Chen Z.,
Chinault C.,
Ciccodicola A.,
Clark S.Y.,
Clarke G.,
Clee C.M.,
Clegg S.,
Clerc-Blankenburg K.,
Clifford K.,
Cobley V.,
Cole C.G.,
Conquer J.S.,
Corby N.,
Connor R.E.,
David R.,
Davies J.,
Davis C.,
Davis J.,
Delgado O.,
Deshazo D.,
Dhami P.,
Ding Y.,
Dinh H.,
Dodsworth S.,
Draper H.,
Dugan-Rocha S.,
Dunham A.,
Dunn M.,
Durbin K.J.,
Dutta I.,
Eades T.,
Ellwood M.,
Emery-Cohen A.,
Errington H.,
Evans K.L.,
Faulkner L.,
Francis F.,
Frankland J.,
Fraser A.E.,
Galgoczy P.,
Gilbert J.,
Gill R.,
Gloeckner G.,
Gregory S.G.,
Gribble S.,
Griffiths C.,
Grocock R.,
Gu Y.,
Gwilliam R.,
Hamilton C.,
Hart E.A.,
Hawes A.,
Heath P.D.,
Heitmann K.,
Hennig S.,
Hernandez J.,
Hinzmann B.,
Ho S.,
Hoffs M.,
Howden P.J.,
Huckle E.J.,
Hume J.,
Hunt P.J.,
Hunt A.R.,
Isherwood J.,
Jacob L.,
Johnson D.,
Jones S.,
de Jong P.J.,
Joseph S.S.,
Keenan S.,
Kelly S.,
Kershaw J.K.,
Khan Z.,
Kioschis P.,
Klages S.,
Knights A.J.,
Kosiura A.,
Kovar-Smith C.,
Laird G.K.,
Langford C.,
Lawlor S.,
Leversha M.,
Lewis L.,
Liu W.,
Lloyd C.,
Lloyd D.M.,
Loulseged H.,
Loveland J.E.,
Lovell J.D.,
Lozado R.,
Lu J.,
Lyne R.,
Ma J.,
Maheshwari M.,
Matthews L.H.,
McDowall J.,
McLaren S.,
McMurray A.,
Meidl P.,
Meitinger T.,
Milne S.,
Miner G.,
Mistry S.L.,
Morgan M.,
Morris S.,
Mueller I.,
Mullikin J.C.,
Nguyen N.,
Nordsiek G.,
Nyakatura G.,
O'dell C.N.,
Okwuonu G.,
Palmer S.,
Pandian R.,
Parker D.,
Parrish J.,
Pasternak S.,
Patel D.,
Pearce A.V.,
Pearson D.M.,
Pelan S.E.,
Perez L.,
Porter K.M.,
Ramsey Y.,
Reichwald K.,
Rhodes S.,
Ridler K.A.,
Schlessinger D.,
Schueler M.G.,
Sehra H.K.,
Shaw-Smith C.,
Shen H.,
Sheridan E.M.,
Shownkeen R.,
Skuce C.D.,
Smith M.L.,
Sotheran E.C.,
Steingruber H.E.,
Steward C.A.,
Storey R.,
Swann R.M.,
Swarbreck D.,
Tabor P.E.,
Taudien S.,
Taylor T.,
Teague B.,
Thomas K.,
Thorpe A.,
Timms K.,
Tracey A.,
Trevanion S.,
Tromans A.C.,
d'Urso M.,
Verduzco D.,
Villasana D.,
Waldron L.,
Wall M.,
Wang Q.,
Warren J.,
Warry G.L.,
Wei X.,
West A.,
Whitehead S.L.,
Whiteley M.N.,
Wilkinson J.E.,
Willey D.L.,
Williams G.,
Williams L.,
Williamson A.,
Williamson H.,
Wilming L.,
Woodmansey R.L.,
Wray P.W.,
Yen J.,
Zhang J.,
Zhou J.,
Zoghbi H.,
Zorilla S.,
Buck D.,
Reinhardt R.,
Poustka A.,
Rosenthal A.,
Lehrach H.,
Meindl A.,
Minx P.J.,
Hillier L.W.,
Willard H.F.,
Wilson R.K.,
Waterston R.H.,
Rice C.M.,
Vaudin M.,
Coulson A.,
Nelson D.L.,
Weinstock G.,
Sulston J.E.,
Durbin R.M.,
Hubbard T.,
Gibbs R.A.,
Beck S.,
Rogers J.,
Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
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[5]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J.,
Istrail S.,
Sutton G.G.,
Florea L.,
Halpern A.L.,
Mobarry C.M.,
Lippert R.,
Walenz B.,
Shatkay H.,
Dew I.,
Miller J.R.,
Flanigan M.J.,
Edwards N.J.,
Bolanos R.,
Fasulo D.,
Halldorsson B.V.,
Hannenhalli S.,
Turner R.,
Yooseph S., ![]()
Lu F.,
Nusskern D.R.,
Shue B.C.,
Zheng X.H.,
Zhong F.,
Delcher A.L.,
Huson D.H.,
Kravitz S.A.,
Mouchard L.,
Reinert K.,
Remington K.A.,
Clark A.G.,
Waterman M.S.,
Eichler E.E.,
Adams M.D.,
Hunkapiller M.W.,
Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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[6]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[7]
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NUCLEOTIDE SEQUENCE [MRNA] OF 814-843.
DOI=10.1093/hmg/2.4.461; PubMed=8504307 [NCBI, ExPASy, EBI, Israel, Japan]
Leahey A.-M.,
Charnas L.R.,
Nussbaum R.L.;
"Nonsense mutations in the OCRL-1 gene in patients with the oculocerebrorenal syndrome of Lowe.";
Hum. Mol. Genet. 2:461-463(1993).
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[8]
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CHARACTERIZATION.
DOI=10.1073/pnas.92.11.4853; PubMed=7761412 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang X.,
Jefferson A.B.,
Auethavekiat V.,
Majerus P.W.;
"The protein deficient in Lowe syndrome is a phosphatidylinositol-4,5-bisphosphate 5-phosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 92:4853-4856(1995).
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[9]
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CHARACTERIZATION.
DOI=10.1074/jbc.273.3.1574; PubMed=9430698 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang X.,
Hartz P.A.,
Philip E.,
Racusen L.C.,
Majerus P.W.;
"Cell lines from kidney proximal tubules of a patient with Lowe syndrome lack OCRL inositol polyphosphate 5-phosphatase and accumulate phosphatidylinositol 4,5-bisphosphate.";
J. Biol. Chem. 273:1574-1582(1998).
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[10]
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IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J.,
Superti-Furga G.,
Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
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[11]
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VARIANTS LOWE SYNDROME THR-367 DEL; GLY-451; SER-463 AND ARG-524.
PubMed=9199559 [NCBI, ExPASy, EBI, Israel, Japan]
Lin T.,
Orrison B.M.,
Leahey A.-M.,
Suchy S.F.,
Bernard D.J.,
Lewis R.A.,
Nussbaum R.L.;
"Spectrum of mutations in the OCRL1 gene in the Lowe oculocerebrorenal syndrome.";
Am. J. Hum. Genet. 60:1384-1388(1997).
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[12]
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VARIANTS LOWE SYNDROME TYR-375; GLN-500; ASP-508 AND CYS-513.
DOI=10.1006/mgme.1998.2687; PubMed=9682219 [NCBI, ExPASy, EBI, Israel, Japan]
Lin T.,
Orrison B.M.,
Suchy S.F.,
Lewis R.A.,
Nussbaum R.L.;
"Mutations are not uniformly distributed throughout the OCRL1 gene in Lowe syndrome patients.";
Mol. Genet. Metab. 64:58-61(1998).
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[13]
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VARIANTS LOWE SYNDROME GLN-500 AND GLN-524.
DOI=10.1002/(SICI)1096-8628(19980605)77:5<348::AID-AJMG2>3.3.CO;2-H; PubMed=9632163 [NCBI, ExPASy, EBI, Israel, Japan]
Kawano T.,
Indo Y.,
Nakazato H.,
Shimadzu M.,
Matsuda I.;
"Oculocerebrorenal syndrome of Lowe: three mutations in the OCRL1 gene derived from three patients with different phenotypes.";
Am. J. Med. Genet. 77:348-355(1998).
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[14]
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VARIANT LOWE SYNDROME ARG-522.
PubMed=9788721 [NCBI, ExPASy, EBI, Israel, Japan]
Kubota T.,
Sakurai A.,
Arakawa K.,
Shimazu M.,
Wakui K.,
Furihata K.,
Fukushima Y.;
"Identification of two novel mutations in the OCRL1 gene in Japanese families with Lowe syndrome.";
Clin. Genet. 54:199-202(1998).
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[15]
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VARIANTS LOWE SYNDROME GLU-357; GLU-421; ASP-424 AND TYR-498.
DOI=10.1002/1098-1004(200008)16:2<157::AID-HUMU8>3.0.CO;2-9; PubMed=10923037 [NCBI, ExPASy, EBI, Israel, Japan]
Monnier N.,
Satre V.,
Lerouge E.,
Berthoin F.,
Lunardi J.;
"OCRL1 mutation analysis in French Lowe syndrome patients: implications for molecular diagnosis strategy and genetic counseling.";
Hum. Mutat. 16:157-165(2000).
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[16]
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VARIANTS LOWE SYNDROME LYS-478-479-TYR DEL; GLN-500 AND LEU-526.
DOI=10.1006/mgme.1999.2955; PubMed=10767176 [NCBI, ExPASy, EBI, Israel, Japan]
Roeschinger W.,
Muntau A.C.,
Rudolph G.,
Roscher A.A.,
Kammerer S.;
"Carrier assessment in families with Lowe oculocerebrorenal syndrome: novel mutations in the OCRL1 gene and correlation of direct DNA diagnosis with ocular examination.";
Mol. Genet. Metab. 69:213-222(2000).
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[17]
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VARIANTS DD2 CYS-318 AND CYS-479.
DOI=10.1086/427887; PubMed=15627218 [NCBI, ExPASy, EBI, Israel, Japan]
Hoopes R.R. Jr.,
Shrimpton A.E.,
Knohl S.J.,
Hueber P.,
Hoppe B.,
Matyus J.,
Simckes A.,
Tasic V.,
Toenshoff B.,
Suchy S.F.,
Nussbaum R.L.,
Scheinman S.J.;
"Dent disease with mutations in OCRL1.";
Am. J. Hum. Genet. 76:260-267(2005).
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- FUNCTION: Converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-phosphate. Also converts inositol 1,4,5-trisphosphate to inositol 1,4-bisphosphate and inositol 1,3,4,5-tetrakisphosphate to inositol 1,3,4-trisphosphate. May function in lysosomal membrane trafficking by regulating the specific pool of phosphatidylinositol 4,5-bisphosphate that is associated with lysosomes.
- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate.
- ALTERNATIVE PRODUCTS:
2 named isoforms [FASTA] produced by alternative splicing.
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| Name | B |
| Isoform ID | Q01968-2 |
| Features which should be applied to build the isoform sequence: VSP_002681. |
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- TISSUE SPECIFICITY: Brain, skeletal muscle, heart, kidney, lung, placenta and fibroblasts.
- DISEASE: Defects in OCRL are the cause of Lowe syndrome [MIM:309000]; also known as Lowe oculocerebrorenal syndrome. The Lowe syndrome is an X-linked multisystem disorder affecting eyes, nervous system, and kidney. It is characterized by hydrophthalmia, cataract, mental retardation, vitamin D-resistant rickets, aminoaciduria, and reduced ammonia production by the kidney. Ocular abnormalities include cataract, glaucoma, microphthalmos, and decreased visual acuity. Developmental delay, hypotonia, behavior abnormalities, and areflexia are also present. Renal tubular involvement is characterized by impaired reabsorption of bicarbonate, amino acids, and phosphate. Musculoskeletal abnormalities such as joint hypermobility, dislocated hips, and fractures may develop as consequences of renal tubular acidosis and hypophosphatemia. Cataract is the only significant manifestation in carriers and is detected by slit-lamp examination.
- DISEASE: Defects in OCRL are the cause of Dent disease type 2 (DD2) [MIM:300555]. DD2 is a renal disease belonging to the 'Dent disease complex', a group of disorders characterized by proximal renal tubular defect, hypercalciuria, nephrocalcinosis, and renal insufficiency. The spectrum of phenotypic features is remarkably similar in the various disorders, except for differences in the severity of bone deformities and renal impairment. Characteristic abnormalities include low-molecular-weight proteinuria and other features of Fanconi syndrome, such as glycosuria, aminoaciduria, and phosphaturia, but typically do not include proximal renal tubular acidosis. Progressive renal failure is common, as are nephrocalcinosis and kidney stones.
- SIMILARITY: Belongs to the inositol-1,4,5-trisphosphate 5-phosphatase type II family.
- SIMILARITY: Contains 1 Rho-GAP domain.
- CAUTION: It is uncertain whether Met-1, Met-18 or Met-20 is the initiator.
- WEB RESOURCE: Name=Lowe Syndrome mutation database; URL="http://research.nhgri.nih.gov/lowe/";.
- WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=OCRL";.
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