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Protein

Polyphosphoinositide phosphatase

Gene

SPAC1093.03

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).By similarity

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate.

Cofactori

Mg2+By similarity

GO - Molecular functioni

  1. phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity Source: PomBase

GO - Biological processi

  1. cell morphogenesis involved in conjugation with cellular fusion Source: PomBase
  2. phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
  3. phosphatidylinositol dephosphorylation Source: PomBase
  4. phosphatidylinositol-mediated signaling Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

ReactomeiREACT_272691. Synthesis of PIPs at the Golgi membrane.
REACT_281363. Synthesis of PIPs at the early endosome membrane.
REACT_306644. Synthesis of PIPs at the late endosome membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyphosphoinositide phosphatase (EC:3.1.3.-)
Alternative name(s):
Phosphatidylinositol 3,5-bisphosphate 5-phosphatase
Gene namesi
ORF Names:SPAC1093.03
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

PomBaseiSPAC1093.03.

Subcellular locationi

Cytoplasm 1 Publication. Vacuole membrane By similarity; Peripheral membrane protein By similarity

GO - Cellular componenti

  1. cytosol Source: PomBase
  2. extrinsic component of membrane Source: PomBase
  3. fungal-type vacuole membrane Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 832832Polyphosphoinositide phosphatasePRO_0000317231Add
BLAST

Proteomic databases

MaxQBiQ7Z9H9.

Interactioni

Subunit structurei

Component of the PI(3,5)P2 regulatory complex.By similarity

Protein-protein interaction databases

BioGridi280477. 38 interactions.
MINTiMINT-4700749.
STRINGi4896.SPAC1093.03-1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini145 – 491347SACPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 SAC domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5329.
HOGENOMiHOG000168063.
InParanoidiQ7Z9H9.
OMAiDIRDYSD.
OrthoDBiEOG7DRJBN.

Family and domain databases

InterProiIPR002013. SAC_dom.
[Graphical view]
PfamiPF02383. Syja_N. 1 hit.
[Graphical view]
PROSITEiPS50275. SAC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7Z9H9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPATNSDEPL VKFELYQLKK CYYIVSENAT ATIFRILKIT QSEDELSISI
60 70 80 90 100
EEAAKILFRQ KLQLYLEKLE NESADGKLIL VTKAYAILGL FRFTAGYYLY
110 120 130 140 150
LCTERKVVAV IGGHNVYHVD KTQFIELNPS RRHNTSVERK CMSSIEKVDL
160 170 180 190 200
ARTFYFSYSY DLSQTIQYGF THPIPQHQVR DMFVWNWNML RPILDSVGID
210 220 230 240 250
SPWCIPLIHG FVDQAKLSVY GKPIIVTLIA RRSRHFAGAR FLRRGIRDDG
260 270 280 290 300
YVANEVETEQ IVFDGSASSF PISSTTPGIP CYTSYVQHRG SIPLRWSQEF
310 320 330 340 350
SNITPKPPIG IDFHDPFYAS TALHFDRLFG HYGIPCIVLN LVKSSEKVKR
360 370 380 390 400
ESLLLDEFES AIQYLNQFLK DSQKIQYIAW DMSAASKKKV PVTKTLEQMA
410 420 430 440 450
SDIVKKTGFF CTADRFFPGT FQTGVVRTNC VDCLDRTNAA QFVIGKCVLA
460 470 480 490 500
AQLRALGVLD SPQLDYESDA VRLLAEMYHG HGDAIALQYG GSLLVNTLDT
510 520 530 540 550
YRKNNQWSST SRDLIESVKR FYSNSFVDFQ RQEAISLFLG NFTVHGKIVV
560 570 580 590 600
FGEKRLQALT EKFKNGQLVR RDYRYWWTPV YVNQELRCKN AYCDSIQRKG
610 620 630 640 650
IKFPANYFDN VYTPNSISSF SEVLLPNLIS TLNFAPLSLI PLLRKSFLPL
660 670 680 690 700
SYNGFGIEAP SLNPFIPRRN QPRDMFKTSA EEENEDEDED DDKFRRVSLY
710 720 730 740 750
KWLFNNEERP VHKFIRKRLH QIPVSNKVQP RDQKQPDFKI PNTDINVYKI
760 770 780 790 800
HFQYNNISGL ADNYTLLSKH DRAMYNNYAD YSPDKIKEIK EKELNTYNDY
810 820 830
FNSAISENPT LKSDRSEKVA FYSAWITDYK ST
Length:832
Mass (Da):96,035
Last modified:June 13, 2012 - v3
Checksum:i0F76CCC03DBFF43E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB60248.4.
RefSeqiNP_001018284.3. NM_001020079.3.

Genome annotation databases

EnsemblFungiiSPAC1093.03.1; SPAC1093.03.1:pep; SPAC1093.03.
GeneIDi3361401.
KEGGispo:SPAC1093.03.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB60248.4.
RefSeqiNP_001018284.3. NM_001020079.3.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi280477. 38 interactions.
MINTiMINT-4700749.
STRINGi4896.SPAC1093.03-1.

Proteomic databases

MaxQBiQ7Z9H9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1093.03.1; SPAC1093.03.1:pep; SPAC1093.03.
GeneIDi3361401.
KEGGispo:SPAC1093.03.

Organism-specific databases

PomBaseiSPAC1093.03.

Phylogenomic databases

eggNOGiCOG5329.
HOGENOMiHOG000168063.
InParanoidiQ7Z9H9.
OMAiDIRDYSD.
OrthoDBiEOG7DRJBN.

Enzyme and pathway databases

ReactomeiREACT_272691. Synthesis of PIPs at the Golgi membrane.
REACT_281363. Synthesis of PIPs at the early endosome membrane.
REACT_306644. Synthesis of PIPs at the late endosome membrane.

Miscellaneous databases

NextBioi20811452.

Family and domain databases

InterProiIPR002013. SAC_dom.
[Graphical view]
PfamiPF02383. Syja_N. 1 hit.
[Graphical view]
PROSITEiPS50275. SAC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Comparative functional genomics of the fission yeasts."
    Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.
    , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
    Science 332:930-936(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVISION OF GENE MODEL.
  3. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFIG4_SCHPO
AccessioniPrimary (citable) accession number: Q7Z9H9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 13, 2012
Last modified: April 1, 2015
This is version 67 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.