Reviewed, UniProtKB/Swiss-Prot Q01968 (OCRL_HUMAN)

Names and origin

Protein names

Recommended name:
    Inositol polyphosphate 5-phosphatase OCRL-1
    EC=3.1.3.36
Alternative name(s):
    Lowe oculocerebrorenal syndrome protein

Gene names

Name:	OCRL
Synonyms:	INPP5F, OCRL1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	901 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

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.
Tissue specificity	Brain, skeletal muscle, heart, kidney, lung, placenta and fibroblasts.
Involvement in 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. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 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. Ref.17
Sequence similarities	Belongs to the inositol-1,4,5-trisphosphate 5-phosphatase type II family. Contains 1 Rho-GAP domain.
Caution	It is uncertain whether Met-1, Met-18 or Met-20 is the initiator.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Disease	Cataract Disease mutation
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	lipid metabolic process Ref.1 Ref.8 Traceable author statement. Source: ProtInc signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi stack Traceable author statement. Source: ProtInc Golgi-associated vesicle Traceable author statement. Source: ProtInc
Molecular function	phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Ref.8 Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: Q01968-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform B (identifier: Q01968-2)

The sequence of this isoform differs from the canonical sequence as follows:
     707-714: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 901

901

Inositol polyphosphate 5-phosphatase OCRL-1

PRO_0000209721

Regions

Domain

721 – 901

181

Rho-GAP

Natural variations

Alternative sequence

707 – 714

8

Missing in isoform B.

VSP_002681

Natural variant

318

1

R → C in DD2. Ref.17

VAR_022698

Natural variant

337

1

R → P in Lowe syndrome.

VAR_010169

Natural variant

357

1

G → E in Lowe syndrome; could be a rare polymorphism.

VAR_010170

Natural variant

367

1

Missing in Lowe syndrome.

VAR_010171

Natural variant

372

1

V → G in Lowe syndrome.

VAR_010172

Natural variant

375

1

H → Y in Lowe syndrome.

VAR_010173

Natural variant

421

1

G → E in Lowe syndrome.

VAR_010174

Natural variant

424

1

N → D in Lowe syndrome.

VAR_010175

Natural variant

451

1

D → G in Lowe syndrome.

VAR_010176

Natural variant

463

1

F → S in Lowe syndrome.

VAR_010177

Natural variant

478 – 479

2

Missing in Lowe syndrome.

VAR_023957

Natural variant

479

1

Y → C in DD2. Ref.17

VAR_022699

Natural variant

498

1

C → Y in Lowe syndrome.

VAR_010178

Natural variant

500

1

R → G in Lowe syndrome.

VAR_010179

Natural variant

500

1

R → Q in Lowe syndrome.

VAR_010180

Natural variant

508

1

V → D in Lowe syndrome.

VAR_010181

Natural variant

513

1

Y → C in Lowe syndrome.

VAR_010182

Natural variant

522

1

S → R in Lowe syndrome.

VAR_010183

Natural variant

524

1

H → Q in Lowe syndrome.

VAR_010184

Natural variant

524

1

H → R in Lowe syndrome.

VAR_010185

Natural variant

526

1

P → L in Lowe syndrome.

VAR_023958

Natural variant

533

1

I → S in Lowe syndrome.

VAR_010187

Natural variant

768

1

I → N in Lowe syndrome; could be a rare polymorphism.

VAR_010188

Natural variant

797

1

A → P in Lowe syndrome; could be a rare polymorphism.

VAR_010189

Secondary structure

1

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901

Helix Strand Turn

Details...

Beta strand

571 – 577

7

Turn

607 – 609

3

Beta strand

615 – 619

5

Beta strand

633 – 636

4

Turn

640 – 642

3

Helix

643 – 648

6

Beta strand

649 – 651

3

Beta strand

655 – 657

3

Beta strand

669 – 675

7

Helix

684 – 687

4

Helix

700 – 702

3

Beta strand

732 – 734

3

Helix

736 – 748

13

Turn

753 – 757

5

Helix

762 – 774

13

Helix

784 – 797

14

Helix

805 – 807

3

Helix

808 – 814

7

Helix

818 – 826

9

Helix

830 – 847

18

Helix

850 – 853

4

Helix

857 – 868

12

Helix

873 – 875

3

Helix

881 – 896

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified June 7, 2005. Version 3. Checksum: 476BFCCC3655C1FE	FASTA	901	104,205
	10 20 30 40 50 60 MEPPLPVGAQ PLATVEGMEM KGPLREPCAL TLAQRNGQYE LIIQLHEKEQ HVQDIIPINS 70 80 90 100 110 120 HFRCVQEAEE TLLIDIASNS GCKIRVQGDW IRERRFEIPD EEHCLKFLSA VLAAQKAQSQ 130 140 150 160 170 180 LLVPEQKDSS SWYQKLDTKD KPSVFSGLLG FEDNFSSMNL DKKINSQNQP TGIHREPPPP 190 200 210 220 230 240 PFSVNKMLPR EKEASNKEQP KVTNTMRKLF VPNTQSGQRE GLIKHILAKR EKEYVNIQTF 250 260 270 280 290 300 RFFVGTWNVN GQSPDSGLEP WLNCDPNPPD IYCIGFQELD LSTEAFFYFE SVKEQEWSMA 310 320 330 340 350 360 VERGLHSKAK YKKVQLVRLV GMMLLIFARK DQCRYIRDIA TETVGTGIMG KMGNKGGVAV 370 380 390 400 410 420 RFVFHNTTFC IVNSHLAAHV EDFERRNQDY KDICARMSFV VPNQTLPQLN IMKHEVVIWL 430 440 450 460 470 480 GDLNYRLCMP DANEVKSLIN KKDLQRLLKF DQLNIQRTQK KAFVDFNEGE IKFIPTYKYD 490 500 510 520 530 540 SKTDRWDSSG KCRVPAWCDR ILWRGTNVNQ LNYRSHMELK TSDHKPVSAL FHIGVKVVDE 550 560 570 580 590 600 RRYRKVFEDS VRIMDRMEND FLPSLELSRR EFVFENVKFR QLQKEKFQIS NNGQVPCHFS 610 620 630 640 650 660 FIPKLNDSQY CKPWLRAEPF EGYLEPNETV DISLDVYVSK DSVTILNSGE DKIEDILVLH 670 680 690 700 710 720 LDRGKDYFLT ISGNYLPSCF GTSLEALCRM KRPIREVPVT KLIDLEEDSF LEKEKSLLQM 730 740 750 760 770 780 VPLDEGASER PLQVPKEIWL LVDHLFKYAC HQEDLFQTPG MQEELQQIID CLDTSIPETI 790 800 810 820 830 840 PGSNHSVAEA LLIFLEALPE PVICYELYQR CLDSAYDPRI CRQVISQLPR CHRNVFRYLM 850 860 870 880 890 900 AFLRELLKFS EYNSVNANMI ATLFTSLLLR PPPNLMARQT PSDRQRAIQF LLGFLLGSEE D
	Isoform B. Checksum: E61E59C6AD0AC650	FASTA	893	103,227
	10 20 30 40 50 60 MEPPLPVGAQ PLATVEGMEM KGPLREPCAL TLAQRNGQYE LIIQLHEKEQ HVQDIIPINS 70 80 90 100 110 120 HFRCVQEAEE TLLIDIASNS GCKIRVQGDW IRERRFEIPD EEHCLKFLSA VLAAQKAQSQ 130 140 150 160 170 180 LLVPEQKDSS SWYQKLDTKD KPSVFSGLLG FEDNFSSMNL DKKINSQNQP TGIHREPPPP 190 200 210 220 230 240 PFSVNKMLPR EKEASNKEQP KVTNTMRKLF VPNTQSGQRE GLIKHILAKR EKEYVNIQTF 250 260 270 280 290 300 RFFVGTWNVN GQSPDSGLEP WLNCDPNPPD IYCIGFQELD LSTEAFFYFE SVKEQEWSMA 310 320 330 340 350 360 VERGLHSKAK YKKVQLVRLV GMMLLIFARK DQCRYIRDIA TETVGTGIMG KMGNKGGVAV 370 380 390 400 410 420 RFVFHNTTFC IVNSHLAAHV EDFERRNQDY KDICARMSFV VPNQTLPQLN IMKHEVVIWL 430 440 450 460 470 480 GDLNYRLCMP DANEVKSLIN KKDLQRLLKF DQLNIQRTQK KAFVDFNEGE IKFIPTYKYD 490 500 510 520 530 540 SKTDRWDSSG KCRVPAWCDR ILWRGTNVNQ LNYRSHMELK TSDHKPVSAL FHIGVKVVDE 550 560 570 580 590 600 RRYRKVFEDS VRIMDRMEND FLPSLELSRR EFVFENVKFR QLQKEKFQIS NNGQVPCHFS 610 620 630 640 650 660 FIPKLNDSQY CKPWLRAEPF EGYLEPNETV DISLDVYVSK DSVTILNSGE DKIEDILVLH 670 680 690 700 710 720 LDRGKDYFLT ISGNYLPSCF GTSLEALCRM KRPIREVPVT KLIDLEKSLL QMVPLDEGAS 730 740 750 760 770 780 ERPLQVPKEI WLLVDHLFKY ACHQEDLFQT PGMQEELQQI IDCLDTSIPE TIPGSNHSVA 790 800 810 820 830 840 EALLIFLEAL PEPVICYELY QRCLDSAYDP RICRQVISQL PRCHRNVFRY LMAFLRELLK 850 860 870 880 890 FSEYNSVNAN MIATLFTSLL LRPPPNLMAR QTPSDRQRAI QFLLGFLLGS EED

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Lowe's oculocerebrorenal syndrome gene encodes a protein highly homologous to inositol polyphosphate-5-phosphatase." Attree O., Olivos I.M., Okabe I., Bailey L.C., Nelson D.L., Lewis R.A., McInnes R.R., Nussbaum R.L. Nature 358:239-242(1992) [PubMed: 1321346] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B). Tissue: Kidney.
[2]	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 Cited for: SEQUENCE REVISION TO 585.
[3]	"Physical mapping and genomic structure of the Lowe syndrome gene OCRL1." Nussbaum R.L., Orrison B.M., Janne P.A., Charnas L.R., Chinault A.C. Hum. Genet. 99:145-150(1997) [PubMed: 9048911] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING. Tissue: Brain.
[4]	"The DNA sequence of the human X chromosome." 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. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
[7]	"Nonsense mutations in the OCRL-1 gene in patients with the oculocerebrorenal syndrome of Lowe." Leahey A.-M., Charnas L.R., Nussbaum R.L. Hum. Mol. Genet. 2:461-463(1993) [PubMed: 8504307] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 814-843.
[8]	"The protein deficient in Lowe syndrome is a phosphatidylinositol-4,5-bisphosphate 5-phosphatase." Zhang X., Jefferson A.B., Auethavekiat V., Majerus P.W. Proc. Natl. Acad. Sci. U.S.A. 92:4853-4856(1995) [PubMed: 7761412] [Abstract] Cited for: CHARACTERIZATION.
[9]	"Cell lines from kidney proximal tubules of a patient with Lowe syndrome lack OCRL inositol polyphosphate 5-phosphatase and accumulate phosphatidylinositol 4,5-bisphosphate." Zhang X., Hartz P.A., Philip E., Racusen L.C., Majerus P.W. J. Biol. Chem. 273:1574-1582(1998) [PubMed: 9430698] [Abstract] Cited for: CHARACTERIZATION.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]	"Spectrum of mutations in the OCRL1 gene in the Lowe oculocerebrorenal syndrome." Lin T., Orrison B.M., Leahey A.-M., Suchy S.F., Bernard D.J., Lewis R.A., Nussbaum R.L. Am. J. Hum. Genet. 60:1384-1388(1997) [PubMed: 9199559] [Abstract] Cited for: VARIANTS LOWE SYNDROME THR-367 DEL; GLY-451; SER-463 AND ARG-524.
[12]	"Mutations are not uniformly distributed throughout the OCRL1 gene in Lowe syndrome patients." Lin T., Orrison B.M., Suchy S.F., Lewis R.A., Nussbaum R.L. Mol. Genet. Metab. 64:58-61(1998) [PubMed: 9682219] [Abstract] Cited for: VARIANTS LOWE SYNDROME TYR-375; GLN-500; ASP-508 AND CYS-513.
[13]	"Oculocerebrorenal syndrome of Lowe: three mutations in the OCRL1 gene derived from three patients with different phenotypes." Kawano T., Indo Y., Nakazato H., Shimadzu M., Matsuda I. Am. J. Med. Genet. 77:348-355(1998) [PubMed: 9632163] [Abstract] Cited for: VARIANTS LOWE SYNDROME GLN-500 AND GLN-524.
[14]	"Identification of two novel mutations in the OCRL1 gene in Japanese families with Lowe syndrome." Kubota T., Sakurai A., Arakawa K., Shimazu M., Wakui K., Furihata K., Fukushima Y. Clin. Genet. 54:199-202(1998) [PubMed: 9788721] [Abstract] Cited for: VARIANT LOWE SYNDROME ARG-522.
[15]	"OCRL1 mutation analysis in French Lowe syndrome patients: implications for molecular diagnosis strategy and genetic counseling." Monnier N., Satre V., Lerouge E., Berthoin F., Lunardi J. Hum. Mutat. 16:157-165(2000) [PubMed: 10923037] [Abstract] Cited for: VARIANTS LOWE SYNDROME GLU-357; GLU-421; ASP-424 AND TYR-498.
[16]	"Carrier assessment in families with Lowe oculocerebrorenal syndrome: novel mutations in the OCRL1 gene and correlation of direct DNA diagnosis with ocular examination." Roeschinger W., Muntau A.C., Rudolph G., Roscher A.A., Kammerer S. Mol. Genet. Metab. 69:213-222(2000) [PubMed: 10767176] [Abstract] Cited for: VARIANTS LOWE SYNDROME LYS-478-479-TYR DEL; GLN-500 AND LEU-526.
[17]	"Dent disease with mutations in OCRL1." 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. Am. J. Hum. Genet. 76:260-267(2005) [PubMed: 15627218] [Abstract] Cited for: VARIANTS DD2 CYS-318 AND CYS-479.
+	Additional computationally mapped references.

Web resources

Lowe Syndrome mutation database

GeneReviews

Cross-references

Sequence databases

EMBLGenBankDDBJ

M88162 mRNA. Translation: AAA59964.2. Different initiation.
U57627 mRNA. Translation: AAB03839.2.
AL022162, AL138745, AL662877 Genomic DNA. Translation: CAI95696.1.
AL138745, AL022162, AL662877 Genomic DNA. Translation: CAI42615.1.
AL138745, AL022162, AL662877 Genomic DNA. Translation: CAI42616.1.
AL662877, AL022162, AL138745 Genomic DNA. Translation: CAI41087.1.
AL662877, AL022162, AL138745 Genomic DNA. Translation: CAI41088.1.
Z73496 Genomic DNA. No translation available.
CH471107 Genomic DNA. Translation: EAX11831.1.
BC130612 mRNA. Translation: AAI30613.1.
S62085 mRNA. Translation: AAB26926.1.

IPI

IPI00480049.
IPI00873093.

PIR

S29069.

RefSeq

NP_000267.2.
NP_001578.2.

UniGene

Hs.126357

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2QV2	X-ray	2.40	A	564-901	[»]

ModBase

Search...

PTM databases

PhosphoSite

Q01968.

Proteomic databases

PRIDE

Q01968.

Genome annotation databases

Ensembl

ENSG00000122126. Homo sapiens. [Contig view]

GeneID

4952.

KEGG

hsa:4952.

UCSC

uc004euq.1. human.
uc004eur.1. human.

Organism-specific databases

GeneCards

GC0XP128501.

H-InvDB

HIX0056225.

HGNC

HGNC:8108. OCRL.

HPA

HPA012495.

MIM

300535. gene.
300555. phenotype.
309000. phenotype.

Orphanet

1652. Dent syndrome.
534. Lowe syndrome.

PharmGKB

PA31896.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q01968.

OMA

Q01968. TGIHREP.

Enzyme and pathway databases

BRENDA

3.1.3.36. 247.

Reactome

REACT_11044. Signaling by Rho GTPases.

Gene expression databases

ArrayExpress

Q01968.

Bgee

Q01968.

CleanEx

HS_INPP5F.

GermOnline

ENSG00000122126. Homo sapiens.

Family and domain databases

InterPro

IPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
IPR000198. RhoGAP.
[Graphical view]

Pfam

PF03372. Exo_endo_phos. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]

SMART

SM00128. IPPc. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]

PROSITE

PS50238. RHOGAP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

19074.

SOURCE

Search...

Entry information

Entry name

OCRL_HUMAN

Accession

Primary (citable) accession number: Q01968
Secondary accession number(s): A6NKI1 , O60800, Q15684, Q15774, Q4VY09, Q5JQF1, Q5JQF2, Q9UJG5, Q9UMA5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	June 7, 2005
Last modified:	July 7, 2009
This is version 105 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)