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Inositol polyphosphate 5-phosphatase OCRL-1 (EC 3.1.3.36) (Lowe oculocerebrorenal syndrome protein)

 OCRL_HUMAN              Reviewed;         901 AA.
Q01968; A6NKI1; A8KAP2; B7ZLX2; O60800; Q15684; Q15774; Q4VY09;
Q4VY10; Q5JQF1; Q5JQF2; Q9UJG5; Q9UMA5;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 3.
18-JUL-2018, entry version 198.
RecName: Full=Inositol polyphosphate 5-phosphatase OCRL-1;
EC=3.1.3.36;
AltName: Full=Lowe oculocerebrorenal syndrome protein;
Name=OCRL; Synonyms=INPP5F, OCRL1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
TISSUE=Kidney;
PubMed=1321346; DOI=10.1038/358239a0;
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).
[2]
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.
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
TISSUE=Brain;
PubMed=9048911; DOI=10.1007/s004390050329;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
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).
[6]
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 814-843.
PubMed=8504307; DOI=10.1093/hmg/2.4.461;
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).
[9]
CHARACTERIZATION.
PubMed=7761412; DOI=10.1073/pnas.92.11.4853;
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).
[10]
CHARACTERIZATION.
PubMed=9430698; DOI=10.1074/jbc.273.3.1574;
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).
[11]
INTERACTION WITH APPL1; CLATHRIN; FAM109A AND FAM109B, SUBCELLULAR
LOCATION, AND VARIANTS OCRL ASN-768 AND PRO-797.
PubMed=20133602; DOI=10.1073/pnas.0914658107;
Swan L.E., Tomasini L., Pirruccello M., Lunardi J., De Camilli P.;
"Two closely related endocytic proteins that share a common OCRL-
binding motif with APPL1.";
Proc. Natl. Acad. Sci. U.S.A. 107:3511-3516(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
INTERACTION WITH APPL1; FAM109A AND FAM109B, VARIANT OCRL ASN-768, AND
CHARACTERIZATION OF VARIANT OCRL ASN-768.
PubMed=21233288; DOI=10.1091/mbc.E10-08-0730;
Noakes C.J., Lee G., Lowe M.;
"The PH domain proteins IPIP27A and B link OCRL1 to receptor recycling
in the endocytic pathway.";
Mol. Biol. Cell 22:606-623(2011).
[14]
FUNCTION IN CILIA ASSEMBLY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
INTERACTION WITH RAB8A, AND MUTAGENESIS OF ASP-422; ASP-499 AND
PHE-668.
PubMed=22543976; DOI=10.1093/hmg/dds163;
Luo N., West C.C., Murga-Zamalloa C.A., Sun L., Anderson R.M.,
Wells C.D., Weinreb R.N., Travers J.B., Khanna H., Sun Y.;
"OCRL localizes to the primary cilium: a new role for cilia in Lowe
syndrome.";
Hum. Mol. Genet. 21:3333-3344(2012).
[15]
FUNCTION IN CILIOGENESIS.
PubMed=22228094; DOI=10.1093/hmg/ddr615;
Coon B.G., Hernandez V., Madhivanan K., Mukherjee D., Hanna C.B.,
Barinaga-Rementeria Ramirez I., Lowe M., Beales P.L., Aguilar R.C.;
"The Lowe syndrome protein OCRL1 is involved in primary cilia
assembly.";
Hum. Mol. Genet. 21:1835-1847(2012).
[16]
REVIEW.
PubMed=22381590; DOI=10.1016/j.tibs.2012.01.002;
Pirruccello M., De Camilli P.;
"Inositol 5-phosphatases: insights from the Lowe syndrome protein
OCRL.";
Trends Biochem. Sci. 37:134-143(2012).
[17]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH INPP5F AND RAB5A.
PubMed=25869668; DOI=10.1083/jcb.201409064;
Nakatsu F., Messa M., Nandez R., Czapla H., Zou Y., Strittmatter S.M.,
De Camilli P.;
"Sac2/INPP5F is an inositol 4-phosphatase that functions in the
endocytic pathway.";
J. Cell Biol. 209:85-95(2015).
[18]
STRUCTURE BY NMR OF 1-119, DOMAIN PH, INTERACTION WITH CLATHRIN, AND
SUBCELLULAR LOCATION.
PubMed=19536138; DOI=10.1038/emboj.2009.155;
Mao Y., Balkin D.M., Zoncu R., Erdmann K.S., Tomasini L., Hu F.,
Jin M.M., Hodsdon M.E., De Camilli P.;
"A PH domain within OCRL bridges clathrin-mediated membrane
trafficking to phosphoinositide metabolism.";
EMBO J. 28:1831-1842(2009).
[19]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 540-678 IN COMPLEX WITH
RAB8A.
PubMed=21378754; DOI=10.1038/emboj.2011.60;
Hou X., Hagemann N., Schoebel S., Blankenfeldt W., Goody R.S.,
Erdmann K.S., Itzen A.;
"A structural basis for Lowe syndrome caused by mutations in the Rab-
binding domain of OCRL1.";
EMBO J. 30:1659-1670(2011).
[20]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 564-901, SUBCELLULAR
LOCATION, AND INTERACTION WITH APPL1.
PubMed=17765681; DOI=10.1016/j.devcel.2007.08.004;
Erdmann K.S., Mao Y., McCrea H.J., Zoncu R., Lee S., Paradise S.,
Modregger J., Biemesderfer D., Toomre D., De Camilli P.;
"A role of the Lowe syndrome protein OCRL in early steps of the
endocytic pathway.";
Dev. Cell 13:377-390(2007).
[21]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 536-901 IN COMPLEX WITH
FAM109A.
PubMed=21666675; DOI=10.1038/nsmb.2071;
Pirruccello M., Swan L.E., Folta-Stogniew E., De Camilli P.;
"Recognition of the F&H motif by the Lowe syndrome protein OCRL.";
Nat. Struct. Mol. Biol. 18:789-795(2011).
[22]
VARIANTS OCRL THR-367 DEL; GLY-451; SER-463 AND ARG-524.
PubMed=9199559; DOI=10.1086/515471;
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).
[23]
VARIANTS OCRL TYR-375; GLN-500; ASP-508 AND CYS-513.
PubMed=9682219; DOI=10.1006/mgme.1998.2687;
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).
[24]
VARIANTS OCRL GLN-500 AND GLN-524.
PubMed=9632163;
DOI=10.1002/(SICI)1096-8628(19980605)77:5<348::AID-AJMG2>3.0.CO;2-J;
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).
[25]
VARIANT OCRL ARG-522.
PubMed=9788721;
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).
[26]
VARIANTS OCRL GLU-357; GLU-421; ASP-424 AND TYR-498.
PubMed=10923037;
DOI=10.1002/1098-1004(200008)16:2<157::AID-HUMU8>3.0.CO;2-9;
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).
[27]
VARIANTS OCRL LYS-478-479-TYR DEL; GLN-500 AND LEU-526.
PubMed=10767176; DOI=10.1006/mgme.1999.2955;
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).
[28]
VARIANTS DD2 CYS-318 AND CYS-479.
PubMed=15627218; DOI=10.1086/427887;
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).
[29]
VARIANTS DD2 CYS-318 AND TRP-493.
PubMed=17384968; DOI=10.1007/s00467-007-0454-x;
Sekine T., Nozu K., Iyengar R., Fu X.J., Matsuo M., Tanaka R.,
Iijima K., Matsui E., Harita Y., Inatomi J., Igarashi T.;
"OCRL1 mutations in patients with Dent disease phenotype in Japan.";
Pediatr. Nephrol. 22:975-980(2007).
[30]
VARIANT OCRL LYS-591.
PubMed=19168822; DOI=10.1177/0883073808321047;
Yuksel A., Karaca E., Albayram M.S.;
"Magnetic resonance imaging, magnetic resonance spectroscopy, and
facial dysmorphism in a case of Lowe syndrome with novel OCRL1 gene
mutation.";
J. Child Neurol. 24:93-96(2009).
[31]
VARIANTS OCRL SER-242; THR-274; ARG-277; CYS-318; CYS-337; ILE-361;
GLY-372; TYR-373; PHE-374; ARG-414; ASN-451; GLY-457; LYS-468;
GLY-468; LEU-495; HIS-499; ARG-503; LYS-591; VAL-742 DEL; PRO-797;
LEU-801 AND ARG-891, AND VARIANTS DD2 HIS-354 AND LEU-799.
PubMed=21031565; DOI=10.1002/humu.21391;
Hichri H., Rendu J., Monnier N., Coutton C., Dorseuil O.,
Poussou R.V., Baujat G., Blanchard A., Nobili F., Ranchin B.,
Remesy M., Salomon R., Satre V., Lunardi J.;
"From Lowe syndrome to Dent disease: correlations between mutations of
the OCRL1 gene and clinical and biochemical phenotypes.";
Hum. Mutat. 32:379-388(2011).
-!- 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
(PubMed:25869668, PubMed:7761412, PubMed:9430698). May function in
lysosomal membrane trafficking by regulating the specific pool of
phosphatidylinositol 4,5-bisphosphate that is associated with
lysosomes. Involved in primary cilia assembly (PubMed:22228094,
PubMed:22543976). {ECO:0000269|PubMed:22228094,
ECO:0000269|PubMed:22543976, ECO:0000269|PubMed:25869668,
ECO:0000269|PubMed:7761412, ECO:0000269|PubMed:9430698}.
-!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-
bisphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 4-phosphate
+ phosphate.
-!- SUBUNIT: Interacts with APPL1, FAM109A/SES1 and FAM109B/SES2;
APPL1-binding and FAM109A-binding are mutually exclusive.
Interacts with clathrin heavy chain. Interacts with several Rab
GTPases, at least RAB1B, RAB5A, RAB6A, RAB8A and RAB31; these
interactions may play a dual role in targeting OCRL to the
specific membranes and stimulating the phosphatase activity.
Interaction with RAB8A modulates OCRL recruitment to cilia.
Interacts with INPP5F (PubMed:25869668).
{ECO:0000269|PubMed:17765681, ECO:0000269|PubMed:19536138,
ECO:0000269|PubMed:20133602, ECO:0000269|PubMed:21233288,
ECO:0000269|PubMed:21378754, ECO:0000269|PubMed:21666675,
ECO:0000269|PubMed:22543976, ECO:0000269|PubMed:25869668}.
-!- INTERACTION:
O95782:AP2A1; NbExp=3; IntAct=EBI-6148898, EBI-353552;
Q96CW1:AP2M1; NbExp=3; IntAct=EBI-6148898, EBI-297683;
P09496:CLTA; NbExp=3; IntAct=EBI-6148898, EBI-1171169;
P09497:CLTB; NbExp=3; IntAct=EBI-6148898, EBI-726598;
Q00610:CLTC; NbExp=10; IntAct=EBI-6148898, EBI-354967;
P11442:Cltc (xeno); NbExp=5; IntAct=EBI-6148898, EBI-397997;
Q68FD5:Cltc (xeno); NbExp=2; IntAct=EBI-6148898, EBI-769168;
Q6ICB4:FAM109B; NbExp=4; IntAct=EBI-11749425, EBI-11081747;
P61106:RAB14; NbExp=3; IntAct=EBI-6148898, EBI-1056404;
P62820:RAB1A; NbExp=8; IntAct=EBI-6148898, EBI-716845;
Q9H0U4:RAB1B; NbExp=3; IntAct=EBI-6148898, EBI-1045214;
P20339:RAB5A; NbExp=11; IntAct=EBI-6148898, EBI-399437;
P20340:RAB6A; NbExp=13; IntAct=EBI-6148898, EBI-1052826;
P61006:RAB8A; NbExp=13; IntAct=EBI-6148898, EBI-722293;
P63000:RAC1; NbExp=3; IntAct=EBI-6148898, EBI-413628;
Q9Y5X1:SNX9; NbExp=6; IntAct=EBI-6148898, EBI-77848;
Q91VH2:Snx9 (xeno); NbExp=2; IntAct=EBI-6148898, EBI-8429356;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane
{ECO:0000250|UniProtKB:D3ZGS3}. Early endosome membrane
{ECO:0000269|PubMed:25869668}. Membrane, clathrin-coated pit
{ECO:0000269|PubMed:25869668}. Cell projection, cilium,
photoreceptor outer segment {ECO:0000269|PubMed:22543976}. Cell
projection, cilium {ECO:0000269|PubMed:22543976}. Cytoplasmic
vesicle {ECO:0000250|UniProtKB:D3ZGS3}. Endosome
{ECO:0000269|PubMed:25869668}. Golgi apparatus, trans-Golgi
network {ECO:0000250|UniProtKB:D3ZGS3}. Note=Also found on
macropinosomes. {ECO:0000269|PubMed:25869668}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A;
IsoId=Q01968-1; Sequence=Displayed;
Name=B;
IsoId=Q01968-2; Sequence=VSP_002681;
-!- TISSUE SPECIFICITY: Brain, skeletal muscle, heart, kidney, lung,
placenta and fibroblasts. Expressed in the retina and the retinal
pigment epithelium. {ECO:0000269|PubMed:22543976}.
-!- DOMAIN: The ASH (ASPM-SPD2-Hydin) and RhoGAP (Rho GTPase
activating) domains form a single folding module. The ASH domain
has an immunoglobulin-like fold, the Rho-GAP domain lacks the
catalytic arginine and is catalytically inactive. The ASH-RhoGAP
module regulates the majority of the protein-protein interactions
currently described. The ASH domain mediates association with
membrane-targeting Rab GTPases. The Rho-GAP domain interacts with
the endocytic adapter APPL1, which is then displaced by FAM109A
and FAM109B as endosomes mature. {ECO:0000269|PubMed:19536138}.
-!- DISEASE: Lowe oculocerebrorenal syndrome (OCRL) [MIM:309000]: 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. {ECO:0000269|PubMed:10767176,
ECO:0000269|PubMed:10923037, ECO:0000269|PubMed:19168822,
ECO:0000269|PubMed:20133602, ECO:0000269|PubMed:21031565,
ECO:0000269|PubMed:21233288, ECO:0000269|PubMed:9199559,
ECO:0000269|PubMed:9632163, ECO:0000269|PubMed:9682219,
ECO:0000269|PubMed:9788721}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Dent disease 2 (DD2) [MIM:300555]: 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. {ECO:0000269|PubMed:15627218,
ECO:0000269|PubMed:17384968, ECO:0000269|PubMed:21031565}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-
phosphatase type II family. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1, Met-18 or Met-20 is the
initiator. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA59964.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Lowe Syndrome mutation database;
URL="http://research.nhgri.nih.gov/lowe/";
-----------------------------------------------------------------------
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EMBL; M88162; AAA59964.2; ALT_INIT; mRNA.
EMBL; U57627; AAB03839.2; -; mRNA.
EMBL; AK293107; BAF85796.1; -; mRNA.
EMBL; AL022162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL138745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL662877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z73496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471107; EAX11831.1; -; Genomic_DNA.
EMBL; CH471107; EAX11832.1; -; Genomic_DNA.
EMBL; BC130612; AAI30613.1; -; mRNA.
EMBL; BC144106; AAI44107.1; -; mRNA.
EMBL; S62085; AAB26926.1; -; mRNA.
CCDS; CCDS35393.1; -. [Q01968-1]
CCDS; CCDS35394.1; -. [Q01968-2]
PIR; S29069; S29069.
RefSeq; NP_000267.2; NM_000276.3. [Q01968-1]
RefSeq; NP_001578.2; NM_001587.3. [Q01968-2]
UniGene; Hs.126357; -.
PDB; 2KIE; NMR; -; A=1-119.
PDB; 2QV2; X-ray; 2.40 A; A=564-901.
PDB; 3QBT; X-ray; 2.00 A; B/D/F/H=540-678.
PDB; 3QIS; X-ray; 2.30 A; A=536-901.
PDB; 4CMN; X-ray; 3.13 A; A=215-560.
PDBsum; 2KIE; -.
PDBsum; 2QV2; -.
PDBsum; 3QBT; -.
PDBsum; 3QIS; -.
PDBsum; 4CMN; -.
ProteinModelPortal; Q01968; -.
SMR; Q01968; -.
BioGrid; 111006; 53.
DIP; DIP-45092N; -.
IntAct; Q01968; 176.
MINT; Q01968; -.
STRING; 9606.ENSP00000360154; -.
SwissLipids; SLP:000001182; -.
DEPOD; Q01968; -.
iPTMnet; Q01968; -.
PhosphoSitePlus; Q01968; -.
BioMuta; OCRL; -.
DMDM; 67477390; -.
EPD; Q01968; -.
MaxQB; Q01968; -.
PaxDb; Q01968; -.
PeptideAtlas; Q01968; -.
PRIDE; Q01968; -.
ProteomicsDB; 58022; -.
ProteomicsDB; 58023; -. [Q01968-2]
TopDownProteomics; Q01968-2; -. [Q01968-2]
Ensembl; ENST00000357121; ENSP00000349635; ENSG00000122126. [Q01968-2]
Ensembl; ENST00000371113; ENSP00000360154; ENSG00000122126. [Q01968-1]
GeneID; 4952; -.
KEGG; hsa:4952; -.
UCSC; uc004euq.4; human. [Q01968-1]
CTD; 4952; -.
DisGeNET; 4952; -.
EuPathDB; HostDB:ENSG00000122126.15; -.
GeneCards; OCRL; -.
GeneReviews; OCRL; -.
HGNC; HGNC:8108; OCRL.
HPA; HPA012495; -.
MalaCards; OCRL; -.
MIM; 300535; gene.
MIM; 300555; phenotype.
MIM; 309000; phenotype.
neXtProt; NX_Q01968; -.
OpenTargets; ENSG00000122126; -.
Orphanet; 93623; Dent disease type 2.
Orphanet; 534; Oculocerebrorenal syndrome.
PharmGKB; PA31896; -.
eggNOG; KOG0565; Eukaryota.
eggNOG; COG5411; LUCA.
GeneTree; ENSGT00760000119075; -.
HOGENOM; HOG000008071; -.
HOVERGEN; HBG000070; -.
InParanoid; Q01968; -.
KO; K01099; -.
OMA; ASNSGCK; -.
OrthoDB; EOG091G02KE; -.
PhylomeDB; Q01968; -.
TreeFam; TF317034; -.
BioCyc; MetaCyc:HS04546-MONOMER; -.
BRENDA; 3.1.3.36; 2681.
Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-HSA-1660514; Synthesis of PIPs at the Golgi membrane.
Reactome; R-HSA-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
Reactome; R-HSA-1855204; Synthesis of IP3 and IP4 in the cytosol.
Reactome; R-HSA-194840; Rho GTPase cycle.
Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
SignaLink; Q01968; -.
EvolutionaryTrace; Q01968; -.
GeneWiki; OCRL; -.
GenomeRNAi; 4952; -.
PRO; PR:Q01968; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000122126; -.
CleanEx; HS_INPP5F; -.
Genevisible; Q01968; HS.
GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005795; C:Golgi stack; TAS:ProtInc.
GO; GO:0005798; C:Golgi-associated vesicle; TAS:ProtInc.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
GO; GO:0005802; C:trans-Golgi network; IDA:FlyBase.
GO; GO:0005096; F:GTPase activator activity; IDA:FlyBase.
GO; GO:0052745; F:inositol phosphate phosphatase activity; IDA:UniProtKB.
GO; GO:0052659; F:inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity; TAS:Reactome.
GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; TAS:Reactome.
GO; GO:0034596; F:phosphatidylinositol phosphate 4-phosphatase activity; TAS:Reactome.
GO; GO:0043813; F:phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity; TAS:Reactome.
GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; TAS:Reactome.
GO; GO:0048365; F:Rac GTPase binding; IPI:FlyBase.
GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:Ensembl.
GO; GO:0043087; P:regulation of GTPase activity; IDA:FlyBase.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
CDD; cd09093; INPP5c_INPP5B; 1.
CDD; cd13382; PH_OCRL1; 1.
Gene3D; 1.10.555.10; -; 1.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.60.10.10; -; 1.
InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
InterPro; IPR005135; Endo/exonuclease/phosphatase.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR000300; IPPc.
InterPro; IPR037793; OCRL1/INPP5B_INPP5c.
InterPro; IPR037787; OCRL1_PH.
InterPro; IPR031995; OCRL_clath-bd.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR000198; RhoGAP_dom.
Pfam; PF03372; Exo_endo_phos; 1.
Pfam; PF16726; OCRL_clath_bd; 1.
Pfam; PF00620; RhoGAP; 1.
SMART; SM00128; IPPc; 1.
SMART; SM00324; RhoGAP; 1.
SUPFAM; SSF48350; SSF48350; 2.
SUPFAM; SSF56219; SSF56219; 1.
PROSITE; PS50238; RHOGAP; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cataract; Cell projection;
Ciliopathy; Cilium; Cilium biogenesis/degradation; Coated pit;
Complete proteome; Cytoplasmic vesicle; Disease mutation; Endosome;
Golgi apparatus; Hydrolase; Membrane; Reference proteome.
CHAIN 1 901 Inositol polyphosphate 5-phosphatase
OCRL-1.
/FTId=PRO_0000209721.
DOMAIN 1 119 PH.
DOMAIN 721 901 Rho-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00172}.
REGION 237 563 5-phosphatase.
REGION 564 678 ASH.
MOTIF 73 77 Clathrin box 1.
MOTIF 702 706 Clathrin box 2.
VAR_SEQ 707 714 Missing (in isoform B).
{ECO:0000303|PubMed:1321346,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_002681.
VARIANT 242 242 F -> S (in OCRL; dbSNP:rs137853828).
{ECO:0000269|PubMed:21031565}.
/FTId=VAR_064773.
VARIANT 274 274 I -> T (in OCRL; dbSNP:rs137853829).
{ECO:0000269|PubMed:21031565}.
/FTId=VAR_064774.
VARIANT 277 277 Q -> R (in OCRL; dbSNP:rs137853830).
{ECO:0000269|PubMed:21031565}.
/FTId=VAR_064775.
VARIANT 318 318 R -> C (in DD2 and OCRL;
dbSNP:rs137853263).
{ECO:0000269|PubMed:15627218,
ECO:0000269|PubMed:17384968,
ECO:0000269|PubMed:21031565}.
/FTId=VAR_022698.
VARIANT 337 337 R -> C (in OCRL; associated with I-361;
dbSNP:rs137853831).
{ECO:0000269|PubMed:21031565}.
/FTId=VAR_064776.
VARIANT 337 337 R -> P (in OCRL).
/FTId=VAR_010169.
VARIANT 354 354 N -> H (in DD2; dbSNP:rs137853833).
{ECO:0000269|PubMed:21031565}.
/FTId=VAR_064777.
VARIANT 357 357 G -> E (in OCRL; uncertain pathological
significance; dbSNP:rs137853854).
{ECO:0000269|PubMed:10923037}.
/FTId=VAR_010170.
VARIANT 361 361 R -> I (in OCRL; associated with C-337;
dbSNP:rs137853832).
{ECO:0000269|PubMed:21031565}.
/FTId=VAR_064778.
VARIANT 367 367 Missing (in OCRL).
{ECO:0000269|PubMed:9199559}.
/FTId=VAR_010171.
VARIANT 372 372 V -> G (in OCRL; dbSNP:rs137853834).
{ECO:0000269|PubMed:21031565}.
/FTId=VAR_010172.
VARIANT 373 373 N -> Y (in OCRL; dbSNP:rs137853835).
{ECO:0000269|PubMed:21031565}.
/FTId=VAR_064779.
VARIANT 374 374 S -> F (in OCRL; dbSNP:rs137853836).
{ECO:0000269|PubMed:21031565}.
/FTId=VAR_064780.
VARIANT 375 375 H -> Y (in OCRL; dbSNP:rs137853848).
{ECO:0000269|PubMed:9682219}.
/FTId=VAR_010173.
VARIANT 414 414 H -> R (in OCRL; dbSNP:rs137853837).
{ECO:0000269|PubMed:21031565}.
/FTId=VAR_064781.
VARIANT 421 421 G -> E (in OCRL; dbSNP:rs137853855).
{ECO:0000269|PubMed:10923037}.
/FTId=VAR_010174.
VARIANT 424 424 N -> D (in OCRL; dbSNP:rs137853856).
{ECO:0000269|PubMed:10923037}.
/FTId=VAR_010175.
VARIANT 451 451 D -> G (in OCRL; dbSNP:rs137853850).
{ECO:0000269|PubMed:9199559}.
/FTId=VAR_010176.
VARIANT 451 451 D -> N (in OCRL; dbSNP:rs137853838).
{ECO:0000269|PubMed:21031565}.
/FTId=VAR_064782.
VARIANT 457 457 R -> G (in OCRL; dbSNP:rs137853839).
{ECO:0000269|PubMed:21031565}.
/FTId=VAR_064783.
VARIANT 463 463 F -> S (in OCRL; dbSNP:rs137853851).
{ECO:0000269|PubMed:9199559}.
/FTId=VAR_010177.
VARIANT 468 468 E -> G (in OCRL; dbSNP:rs137853841).
{ECO:0000269|PubMed:21031565}.
/FTId=VAR_064784.
VARIANT 468 468 E -> K (in OCRL; dbSNP:rs137853840).
{ECO:0000269|PubMed:21031565}.
/FTId=VAR_064785.
VARIANT 478 479 Missing (in OCRL).
/FTId=VAR_023957.
VARIANT 479 479 Y -> C (in DD2; dbSNP:rs137853262).
{ECO:0000269|PubMed:15627218}.
/FTId=VAR_022699.
VARIANT 493 493 R -> W (in DD2; dbSNP:rs137853846).
{ECO:0000269|PubMed:17384968}.
/FTId=VAR_064786.
VARIANT 495 495 P -> L (in OCRL).
{ECO:0000269|PubMed:21031565}.
/FTId=VAR_064787.
VARIANT 498 498 C -> Y (in OCRL; dbSNP:rs137853857).
{ECO:0000269|PubMed:10923037}.
/FTId=VAR_010178.
VARIANT 499 499 D -> H (in OCRL; dbSNP:rs137853842).
{ECO:0000269|PubMed:21031565}.
/FTId=VAR_064788.
VARIANT 500 500 R -> G (in OCRL; dbSNP:rs398123287).
/FTId=VAR_010179.
VARIANT 500 500 R -> Q (in OCRL; dbSNP:rs137853260).
{ECO:0000269|PubMed:10767176,
ECO:0000269|PubMed:9632163,
ECO:0000269|PubMed:9682219}.
/FTId=VAR_010180.
VARIANT 503 503 W -> R (in OCRL; dbSNP:rs137853843).
{ECO:0000269|PubMed:21031565}.
/FTId=VAR_064789.
VARIANT 508 508 V -> D (in OCRL; dbSNP:rs137853849).
{ECO:0000269|PubMed:9682219}.
/FTId=VAR_010181.
VARIANT 513 513 Y -> C (in OCRL; dbSNP:rs137853847).
{ECO:0000269|PubMed:9682219}.
/FTId=VAR_010182.
VARIANT 522 522 S -> R (in OCRL; dbSNP:rs137853853).
{ECO:0000269|PubMed:9788721}.
/FTId=VAR_010183.
VARIANT 524 524 H -> Q (in OCRL; dbSNP:rs137853261).
{ECO:0000269|PubMed:9632163}.
/FTId=VAR_010184.
VARIANT 524 524 H -> R (in OCRL; dbSNP:rs137853852).
{ECO:0000269|PubMed:9199559}.
/FTId=VAR_010185.
VARIANT 526 526 P -> L (in OCRL; dbSNP:rs137853858).
{ECO:0000269|PubMed:10767176}.
/FTId=VAR_023958.
VARIANT 533 533 I -> S (in OCRL).
/FTId=VAR_010187.
VARIANT 591 591 N -> K (in OCRL; dbSNP:rs137853844).
{ECO:0000269|PubMed:19168822,
ECO:0000269|PubMed:21031565}.
/FTId=VAR_064790.
VARIANT 742 742 Missing (in OCRL).
{ECO:0000269|PubMed:21031565}.
/FTId=VAR_064791.
VARIANT 768 768 I -> N (in OCRL; uncertain pathological
significance; abolishes FAM109A-,
FAM109B- and APPL1-binding).
{ECO:0000269|PubMed:20133602,
ECO:0000269|PubMed:21233288}.
/FTId=VAR_010188.
VARIANT 797 797 A -> P (in OCRL; uncertain pathological
significance).
{ECO:0000269|PubMed:20133602,
ECO:0000269|PubMed:21031565}.
/FTId=VAR_010189.
VARIANT 799 799 P -> L (in DD2).
{ECO:0000269|PubMed:21031565}.
/FTId=VAR_064792.
VARIANT 801 801 P -> L (in OCRL).
{ECO:0000269|PubMed:21031565}.
/FTId=VAR_064793.
VARIANT 891 891 L -> R (in OCRL; dbSNP:rs137853845).
{ECO:0000269|PubMed:21031565}.
/FTId=VAR_064794.
MUTAGEN 422 422 D->A: Does not affect interaction with
RAB8A. {ECO:0000269|PubMed:22543976}.
MUTAGEN 499 499 D->A: Does not affect interaction with
RAB8A. {ECO:0000269|PubMed:22543976}.
MUTAGEN 668 668 F->V: Does not interact with RAB8A. Does
not localize to cilia.
{ECO:0000269|PubMed:22543976}.
CONFLICT 180 180 P -> L (in Ref. 4; BAF85796).
{ECO:0000305}.
CONFLICT 321 321 G -> E (in Ref. 7; AAI44107).
{ECO:0000305}.
STRAND 10 21 {ECO:0000244|PDB:2KIE}.
STRAND 24 35 {ECO:0000244|PDB:2KIE}.
STRAND 38 45 {ECO:0000244|PDB:2KIE}.
STRAND 52 57 {ECO:0000244|PDB:2KIE}.
STRAND 59 61 {ECO:0000244|PDB:2KIE}.
STRAND 63 70 {ECO:0000244|PDB:2KIE}.
HELIX 76 78 {ECO:0000244|PDB:2KIE}.
STRAND 80 90 {ECO:0000244|PDB:2KIE}.
STRAND 94 98 {ECO:0000244|PDB:2KIE}.
HELIX 101 118 {ECO:0000244|PDB:2KIE}.
HELIX 222 229 {ECO:0000244|PDB:4CMN}.
HELIX 231 234 {ECO:0000244|PDB:4CMN}.
STRAND 235 248 {ECO:0000244|PDB:4CMN}.
HELIX 259 262 {ECO:0000244|PDB:4CMN}.
STRAND 265 267 {ECO:0000244|PDB:4CMN}.
STRAND 270 277 {ECO:0000244|PDB:4CMN}.
HELIX 283 286 {ECO:0000244|PDB:4CMN}.
HELIX 292 304 {ECO:0000244|PDB:4CMN}.
STRAND 311 319 {ECO:0000244|PDB:4CMN}.
STRAND 322 329 {ECO:0000244|PDB:4CMN}.
HELIX 332 335 {ECO:0000244|PDB:4CMN}.
STRAND 336 345 {ECO:0000244|PDB:4CMN}.
HELIX 348 350 {ECO:0000244|PDB:4CMN}.
STRAND 355 364 {ECO:0000244|PDB:4CMN}.
STRAND 367 375 {ECO:0000244|PDB:4CMN}.
HELIX 383 396 {ECO:0000244|PDB:4CMN}.
HELIX 411 413 {ECO:0000244|PDB:4CMN}.
STRAND 414 422 {ECO:0000244|PDB:4CMN}.
HELIX 432 440 {ECO:0000244|PDB:4CMN}.
HELIX 444 448 {ECO:0000244|PDB:4CMN}.
HELIX 452 458 {ECO:0000244|PDB:4CMN}.
STRAND 461 463 {ECO:0000244|PDB:4CMN}.
STRAND 483 486 {ECO:0000244|PDB:4CMN}.
STRAND 489 491 {ECO:0000244|PDB:4CMN}.
STRAND 499 504 {ECO:0000244|PDB:4CMN}.
STRAND 506 510 {ECO:0000244|PDB:4CMN}.
STRAND 521 524 {ECO:0000244|PDB:4CMN}.
STRAND 527 538 {ECO:0000244|PDB:4CMN}.
HELIX 541 548 {ECO:0000244|PDB:3QBT}.
HELIX 553 560 {ECO:0000244|PDB:3QBT}.
STRAND 565 568 {ECO:0000244|PDB:3QBT}.
STRAND 571 577 {ECO:0000244|PDB:3QBT}.
STRAND 583 591 {ECO:0000244|PDB:3QBT}.
STRAND 593 595 {ECO:0000244|PDB:3QBT}.
STRAND 597 602 {ECO:0000244|PDB:3QBT}.
STRAND 608 611 {ECO:0000244|PDB:3QBT}.
STRAND 615 619 {ECO:0000244|PDB:3QBT}.
STRAND 621 624 {ECO:0000244|PDB:3QBT}.
STRAND 629 636 {ECO:0000244|PDB:3QBT}.
HELIX 640 648 {ECO:0000244|PDB:3QBT}.
STRAND 649 651 {ECO:0000244|PDB:3QBT}.
STRAND 655 661 {ECO:0000244|PDB:3QBT}.
STRAND 666 675 {ECO:0000244|PDB:3QBT}.
HELIX 684 689 {ECO:0000244|PDB:3QIS}.
HELIX 700 702 {ECO:0000244|PDB:2QV2}.
HELIX 736 748 {ECO:0000244|PDB:3QIS}.
TURN 753 757 {ECO:0000244|PDB:3QIS}.
HELIX 762 774 {ECO:0000244|PDB:3QIS}.
HELIX 784 797 {ECO:0000244|PDB:3QIS}.
HELIX 805 814 {ECO:0000244|PDB:3QIS}.
HELIX 818 826 {ECO:0000244|PDB:3QIS}.
HELIX 830 847 {ECO:0000244|PDB:3QIS}.
HELIX 850 853 {ECO:0000244|PDB:3QIS}.
HELIX 857 868 {ECO:0000244|PDB:3QIS}.
HELIX 873 875 {ECO:0000244|PDB:2QV2}.
HELIX 883 895 {ECO:0000244|PDB:3QIS}.
SEQUENCE 901 AA; 104205 MW; 476BFCCC3655C1FE CRC64;
MEPPLPVGAQ PLATVEGMEM KGPLREPCAL TLAQRNGQYE LIIQLHEKEQ HVQDIIPINS
HFRCVQEAEE TLLIDIASNS GCKIRVQGDW IRERRFEIPD EEHCLKFLSA VLAAQKAQSQ
LLVPEQKDSS SWYQKLDTKD KPSVFSGLLG FEDNFSSMNL DKKINSQNQP TGIHREPPPP
PFSVNKMLPR EKEASNKEQP KVTNTMRKLF VPNTQSGQRE GLIKHILAKR EKEYVNIQTF
RFFVGTWNVN GQSPDSGLEP WLNCDPNPPD IYCIGFQELD LSTEAFFYFE SVKEQEWSMA
VERGLHSKAK YKKVQLVRLV GMMLLIFARK DQCRYIRDIA TETVGTGIMG KMGNKGGVAV
RFVFHNTTFC IVNSHLAAHV EDFERRNQDY KDICARMSFV VPNQTLPQLN IMKHEVVIWL
GDLNYRLCMP DANEVKSLIN KKDLQRLLKF DQLNIQRTQK KAFVDFNEGE IKFIPTYKYD
SKTDRWDSSG KCRVPAWCDR ILWRGTNVNQ LNYRSHMELK TSDHKPVSAL FHIGVKVVDE
RRYRKVFEDS VRIMDRMEND FLPSLELSRR EFVFENVKFR QLQKEKFQIS NNGQVPCHFS
FIPKLNDSQY CKPWLRAEPF EGYLEPNETV DISLDVYVSK DSVTILNSGE DKIEDILVLH
LDRGKDYFLT ISGNYLPSCF GTSLEALCRM KRPIREVPVT KLIDLEEDSF LEKEKSLLQM
VPLDEGASER PLQVPKEIWL LVDHLFKYAC HQEDLFQTPG MQEELQQIID CLDTSIPETI
PGSNHSVAEA LLIFLEALPE PVICYELYQR CLDSAYDPRI CRQVISQLPR CHRNVFRYLM
AFLRELLKFS EYNSVNANMI ATLFTSLLLR PPPNLMARQT PSDRQRAIQF LLGFLLGSEE
D


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