Inositol-1,4,5-trisphosphate 5-phosphatase 2 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P50942 (INP52_YEAST)

Last modified November 3, 2009. Version 78. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Inositol-1,4,5-trisphosphate 5-phosphatase 2
    EC=3.1.3.36
Alternative name(s):
    Synaptojanin-like protein 2

Gene names

Name:	INP52
Synonyms:	SJL2
Ordered Locus Names:	YNL106C
ORF Names:	N2160

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	1183 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Controls the cellular levels and subcellular distribution of phosphatidylinositol 3-phosphate and phosphatidylinositol 4,5-bisphosphate. Specifically functions within the early endocytic pathway and actin organization. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19
Catalytic activity	1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H₂O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate.
Subunit structure	Interacts with ABP1 and BSP1. Ref.16 Ref.12
Subcellular location	Cytoplasm › cytoskeleton › actin patch. Ref.16 Ref.18 Ref.13
Domain	The SAC1 domain is capable of hydrolyzing phosphatidylinositol 3-phosphate (PtdIns₃P), phosphatidylinositol 4-phosphate (PtdIns₄P), and phosphatidylinositol 3,5-biphosphate (PtdIns(3,5)P2). Ref.7
Sequence similarities	Belongs to the synaptojanin family. In the central section; belongs to the inositol-1,4,5-trisphosphate 5-phosphatase family. Contains 1 SAC domain.

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Ontologies

Keywords
Biological process	Endocytosis Lipid metabolism Protein transport Transport
Cellular component	Cytoplasm Cytoskeleton
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	endocytosis Inferred from electronic annotation. Source: UniProtKB-KW phosphoinositide dephosphorylation Ref.7 Inferred from direct assay. Source: SGD protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	actin cortical patch Ref.10 Ref.16 Inferred from direct assay. Source: SGD mating projection tip Inferred from direct assay. Source: SGD vesicular fraction Ref.18 Inferred from direct assay. Source: SGD
Molecular function	phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity Ref.7 Inferred from direct assay. Source: SGD phosphatidylinositol-3-phosphatase activity Ref.7 Inferred from direct assay. Source: SGD phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Ref.7 Inferred from direct assay. Source: SGD phosphatidylinositol-4-phosphate phosphatase activity Ref.7 Inferred from direct assay. Source: SGD protein binding Ref.12 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARC40	P38328	1	EBI-28834,EBI-2777
BSP1	Q06604	4	EBI-28834,EBI-37047

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1183

1183

Inositol-1,4,5-trisphosphate 5-phosphatase 2

PRO_0000209745

Regions

Domain

167 – 507

341

SAC

Amino acid modifications

Modified residue

149

Phosphoserine Ref.22

Modified residue

152

Phosphoserine Ref.22

Modified residue

444

Phosphothreonine Ref.21

Modified residue

952

Phosphoserine Ref.22

Modified residue

962

Phosphoserine Ref.22

Modified residue

1005

Phosphoserine Ref.17

Modified residue

1011

Phosphoserine Ref.17

Modified residue

1032

Phosphothreonine Ref.20

Modified residue

1081

Phosphoserine Ref.21

Modified residue

1082

Phosphoserine Ref.22 Ref.21

Modified residue

1083

Phosphothreonine Ref.22 Ref.21

Modified residue

1133

Phosphothreonine Ref.22

Modified residue

1146

Phosphoserine Ref.22

Modified residue

1148

Phosphoserine Ref.22

Experimental info

Mutagenesis

631

E → A: Impairs completely enzyme activity. Ref.9

Mutagenesis

730

H → A: Impairs completely enzyme activity. Ref.9

Mutagenesis

771

D → A: Impairs completely enzyme activity. Ref.9

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Sequences

Sequence

Length

Mass (Da)

Tools

P50942-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 97B279870DFE6F65
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FASTA

1,183

133,331

        10         20         30         40         50         60 
MKILLSKQQT RKIAIVSETH GLVFRPINSK NSRRSTCAVE LVPKAELNGN GFRRLSNHEI 

        70         80         90        100        110        120 
YGFIGLIEIE GLMFIATITG KSKVAQPIPN KTVNKIYAVD FFCLNNSKWD FMDIDSSGYP 

       130        140        150        160        170        180 
IVTNDGDFAI SSPPSISTHS SRSSLRSSSS RSLNAQEQAP KHPCHELRKL LSNGSFYYST 

       190        200        210        220        230        240 
DFDLTCTLQK RGFTEHSLSF DDFDREFMWN SFLMDEIITY RDRLDVTAKE LLDQRGFLTT 

       250        260        270        280        290        300 
VIRGFAETIF SYINRLKVGL TIISRQSWKR AGTRFNARGI DDDGHVANFV ETEMIMYSSQ 

       310        320        330        340        350        360 
YCYAFTQIRG SLPIFWEQDT SLISPKIQIT RSVEATQPTF DEHFIRLFKK YGPVHIINLL 

       370        380        390        400        410        420 
STKSSEIQLS RRYKEQLKNS EKMKIGRDVF LTSFDFHRET SQDGFAAASR IIPKIRNTIL 

       430        440        450        460        470        480 
DAGYFSYDVK EGRLISEQDG VFRTNCLDCL DRTNLIQQTI SLAVFKLFLE DFRLVKPSSF 

       490        500        510        520        530        540 
IDDNEFVQKV NALWADNGDQ ISQIYTGTNA LKSSYSRKGK MSFSGALSDA TKSVSRMYIN 

       550        560        570        580        590        600 
NFVDKGKQQN IDTLLGKLPH QQVVELYDPI CEYVNERLLE SEEKFTTHSN INLFVGTFNV 

       610        620        630        640        650        660 
NGNSRRADLS KWLFPIGDKF KPDVVVLGLQ EVIELTAGSI LNADYTKSSF WETMVTDCLN 

       670        680        690        700        710        720 
QYEEKYLLLR VEQMSSLLIL FFARSDRAYN IKEVGGSTKK TGFGGITGNK GAVAIRFDYG 

       730        740        750        760        770        780 
ATSFCFVNTH LSAGASNIDE RRNDYNNIYR NITFPRSKTI PHHDSLFWLG DLNYRITLTN 

       790        800        810        820        830        840 
DEVRRELRAQ KDGYIDRLLQ YDQLTQEINE GVVFQGFKEP TLQFRPTYKY DYGTDNYDTS 

       850        860        870        880        890        900 
EKARTPSWTD RIIYKGENLH PLAYSDAPLK ISDHKPVYAA YRANVKFVDE KEKLNLVEKL 

       910        920        930        940        950        960 
YAEYKNTHPE ALTTGPDELS HARMEKQKES IPLDATVQSA GIKLIDLDDT SSCVSPLLSG 

       970        980        990       1000       1010       1020 
PSPQPSVVGP GGLSNVSPDK SKLNVLPPPP PTSRHNKEPS SKLLSPTKEI SIVSVSPRKG 

      1030       1040       1050       1060       1070       1080 
ESNLPALERH STPKPLPPVP ALSLSKPVSL QKSSSELQHA KETIDNGKIV PRPCPPIRRK 

      1090       1100       1110       1120       1130       1140 
SSTAPDEIST STKNSGVSTT EDPEPAKAST KPEKPPVVKK PHYLSVAANK LNTSQEHSIK 

      1150       1160       1170       1180 
VSPSNSKSEE ELPCKKKSKP KVPAKNPELE KLSVHPLKPC DPN

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. Hani J. Nature 387:93-98(1997) [PubMed: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	"The sequence of a 21.3 kb DNA fragment from the left arm of yeast chromosome XIV reveals LEU4, MET4, POL1, RAS2, and six new open reading frames." Saiz J.E., Buitrago M.J., Soler A., del Rey F., Revuelta J.L. Yeast 12:403-409(1996) [PubMed: 8701612] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1102. Strain: ATCC 96604 / S288c / FY1679.
[3]	"The DNA sequence of cosmid 14-13b from chromosome XIV of Saccharomyces cerevisiae reveals an unusually high number of overlapping open reading frames." de Antoni A., D'Angelo M., Dal Pero F., Sartorello F., Pandolfo D., Pallavicini A., Lanfranchi G., Valle G. Yeast 13:261-266(1997) [PubMed: 9090055] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 880-1183.
[4]	"Novel genes involved in endosomal traffic in yeast revealed by suppression of a targeting-defective plasma membrane ATPase mutant." Luo W.-J., Chang A. J. Cell Biol. 138:731-746(1997) [PubMed: 9265642] [Abstract] Cited for: FUNCTION.
[5]	"Identification and characterization of an essential family of inositol polyphosphate 5-phosphatases (INP51, INP52 and INP53 gene products) in the yeast Saccharomyces cerevisiae." Stolz L.E., Huynh C.V., Thorner J., York J.D. Genetics 148:1715-1729(1998) [PubMed: 9560389] [Abstract] Cited for: FUNCTION.
[6]	"Synaptojanin family members are implicated in endocytic membrane traffic in yeast." Singer-Krueger B., Nemoto Y., Daniell L., Ferro-Novick S., De Camilli P. J. Cell Sci. 111:3347-3356(1998) [PubMed: 9788876] [Abstract] Cited for: FUNCTION.
[7]	"SAC1-like domains of yeast SAC1, INP52, and INP53 and of human synaptojanin encode polyphosphoinositide phosphatases." Guo S., Stolz L.E., Lemrow S.M., York J.D. J. Biol. Chem. 274:12990-12995(1999) [PubMed: 10224048] [Abstract] Cited for: FUNCTION, DOMAIN.
[8]	"SAC1 encodes a regulated lipid phosphoinositide phosphatase, defects in which can be suppressed by the homologous Inp52p and Inp53p phosphatases." Hughes W.E., Woscholski R., Cooke F.T., Patrick R.S., Dove S.K., McDonald N.Q., Parker P.J. J. Biol. Chem. 275:801-808(2000) [PubMed: 10625610] [Abstract] Cited for: FUNCTION.
[9]	"The inositol polyphosphate 5-phosphatases and the apurinic/apyrimidinic base excision repair endonucleases share a common mechanism for catalysis." Whisstock J.C., Romero S., Gurung R., Nandurkar H., Ooms L.M., Bottomley S.P., Mitchell C.A. J. Biol. Chem. 275:37055-37061(2000) [PubMed: 10962003] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLU-631; HIS-730 AND ASP-771.
[10]	"The yeast inositol polyphosphate 5-phosphatases inp52p and inp53p translocate to actin patches following hyperosmotic stress: mechanism for regulating phosphatidylinositol 4,5-bisphosphate at plasma membrane invaginations." Ooms L.M., McColl B.K., Wiradjaja F., Wijayaratnam A.P.W., Gleeson P., Gething M.J., Sambrook J.F., Mitchell C.A. Mol. Cell. Biol. 20:9376-9390(2000) [PubMed: 11094088] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOPCATION.
[11]	"Mammalian inositol polyphosphate 5-phosphatase II can compensate for the absence of all three yeast Sac1-like-domain-containing 5-phosphatases." O'Malley C.J., McColl B.K., Kong A.M., Ellis S.L., Wijayaratnam A.P.W., Sambrook J., Mitchell C.A. Biochem. J. 355:805-817(2001) [PubMed: 11311145] [Abstract] Cited for: FUNCTION.
[12]	"Bsp1p/Ypr171p is an adapter that directly links some synaptojanin family members to the cortical actin cytoskeleton in yeast." Wicky S., Frischmuth S., Singer-Krueger B. FEBS Lett. 537:35-41(2003) [PubMed: 12606027] [Abstract] Cited for: INTERACTION WITH BSP1.
[13]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[14]	"Essential role for the myotubularin-related phosphatase Ymr1p and the synaptojanin-like phosphatases Sjl2p and Sjl3p in regulation of phosphatidylinositol 3-phosphate in yeast." Parrish W.R., Stefan C.J., Emr S.D. Mol. Biol. Cell 15:3567-3579(2004) [PubMed: 15169871] [Abstract] Cited for: FUNCTION.
[15]	"Interaction of Pik1p and Sjl proteins in membrane trafficking." Nguyen P.H., Hasek J., Kohlwein S.D., Romero C., Choi J.H., Vancura A. FEMS Yeast Res. 5:363-371(2005) [PubMed: 15691741] [Abstract] Cited for: FUNCTION.
[16]	"The phosphoinositide phosphatase Sjl2 is recruited to cortical actin patches in the control of vesicle formation and fission during endocytosis." Stefan C.J., Padilla S.M., Audhya A., Emr S.D. Mol. Cell. Biol. 25:2910-2923(2005) [PubMed: 15798181] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ABP1.
[17]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1005 AND SER-1011, MASS SPECTROMETRY.
[18]	"Sjl2p is specifically involved in early steps of endocytosis intimately linked to actin dynamics via the Ark1p/Prk1p kinases." Boettcher C., Wicky S., Schwarz H., Singer-Krueger B. FEBS Lett. 580:633-641(2006) [PubMed: 16406366] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[19]	"PtdIns(4,5)P2 turnover is required for multiple stages during clathrin-and actin-dependent endocytic internalization." Sun Y., Carroll S., Kaksonen M., Toshima J.Y., Drubin D.G. J. Cell Biol. 177:355-367(2007) [PubMed: 17452534] [Abstract] Cited for: FUNCTION.
[20]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1032, MASS SPECTROMETRY.
[21]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-444; SER-1081; SER-1082 AND THR-1083, MASS SPECTROMETRY.
[22]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-152; SER-952; SER-962; SER-1082; THR-1083; THR-1133; SER-1146 AND SER-1148, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	Z71382 Genomic DNA. Translation: CAA95982.1. Z69382 Genomic DNA. Translation: CAA93402.1. Z50161 Genomic DNA. Translation: CAA90520.1.
PIR	S63046.
RefSeq	NP_014293.1.
3D structure databases
HSSP	HSSP built from PDB template 1I9Z based on UniProtKB O43001.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2764N.
IntAct	P50942. 19 interactions.
STRING	P50942.
Proteomic databases
PeptideAtlas	P50942.
PRIDE	P50942.
Genome annotation databases
Ensembl	YNL106C; YNL106C; YNL106C; Saccharomyces cerevisiae. [Genome view]
GeneID	855618.
GenomeReviews	Gene locus YNL106C in contig Y13139_GR.
KEGG	sce:YNL106C.
NMPDR	fig\|4932.3.peg.5363.
Organism-specific databases
CYGD	YNL106c.
SGD	S000005050. INP52.
Phylogenomic databases
HOGENOM	P50942.
OMA	RKGKMSF.
Gene expression databases
ArrayExpress	P50942.
Genevestigator	P50942.
GermOnline	YNL106C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR005135. Endo/exonuclease/phosphatase. IPR000300. IPPc. IPR002013. Syja_N. [Graphical view]
Pfam	PF03372. Exo_endo_phos. 1 hit. PF02383. Syja_N. 1 hit. [Graphical view]
SMART	SM00128. IPPc. 1 hit. [Graphical view]
PROSITE	PS50275. SAC. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	979804.

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Entry information

Entry name

INP52_YEAST

Accession

Primary (citable) accession number: P50942

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 3, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents