Inositol-1,4,5-trisphosphate 5-phosphatase 3 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot Q12271 (INP53_YEAST)

Last modified June 16, 2009. Version 59. 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 3
    EC=3.1.3.36
Alternative name(s):
    Synaptojanin-like protein 3
    Suppressor of PMA1 protein 2

Gene names

Name:	INP53
Synonyms:	SJL3, SOP2
Ordered Locus Names:	YOR109W
ORF Names:	YOR3231w

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	1107 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. Plays an essential role in a TGN (trans Golgi network)-to-early endosome pathway. Involved in clathrin-mediated protein sorting at the TGN. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.16 Ref.17
Catalytic activity	1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H₂O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate.
Subunit structure	Interacts with BSP1 and CHC1. Ref.13 Ref.12
Subcellular location	Cytoplasm. Note: Cytoplasmic punctate structures. Hyperosmotic stress causes translocation to actin patches. Ref.10 Ref.14
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.6 Ref.10 Ref.13 The 5-phosphatase domain (residues 568 to 856) selectively removes the phosphate group at the 5' position of inositol of phosphatidylinositol 4,5-biphosphate (PtdIns(4,5)P2). Ref.6 Ref.10 Ref.13 The C-terminal proline-rich domain is required for the function and associates with clathrin heavy chain CHC1. Ref.6 Ref.10 Ref.13
Miscellaneous	Present with 1520 molecules/cell in log phase SD medium. Ref.15
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 Protein transport Transport
Cellular component	Cytoplasm
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.6 Inferred from direct assay. Source: SGD protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	actin cortical patch Ref.10 Inferred from direct assay. Source: SGD vesicular fraction Inferred from direct assay. Source: SGD
Molecular function	phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity Ref.6 Inferred from direct assay. Source: SGD phosphatidylinositol-3-phosphatase activity Ref.6 Inferred from direct assay. Source: SGD phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Ref.6 Inferred from direct assay. Source: SGD phosphatidylinositol-4-phosphate phosphatase activity Ref.6 Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
APL2	P36000	1	EBI-36688,EBI-2206
APL4	Q12028	1	EBI-36688,EBI-33025
CHC1	P22137	1	EBI-36688,EBI-4766
GGA2	P38817	1	EBI-36688,EBI-7569

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1107

1107

Inositol-1,4,5-trisphosphate 5-phosphatase 3

PRO_0000268681

Regions

Domain

142 – 482

341

SAC

Compositional bias

957 – 989

Pro-rich

Amino acid modifications

Modified residue

903

Phosphoserine Ref.20

Modified residue

932

Phosphoserine Ref.20

Modified residue

933

Phosphoserine Ref.20

Modified residue

934

Phosphoserine Ref.20

Modified residue

975

Phosphoserine Ref.20

Modified residue

986

Phosphoserine Ref.20 Ref.19

Modified residue

988

Phosphothreonine Ref.20

Modified residue

1029

Phosphoserine Ref.20

Modified residue

1030

Phosphothreonine Ref.20

Modified residue

1031

Phosphoserine Ref.20

Modified residue

1035

Phosphoserine Ref.20

Modified residue

1039

Phosphoserine Ref.20

Modified residue

1061

Phosphothreonine Ref.20

Modified residue

1105

Phosphothreonine Ref.18

Experimental info

Mutagenesis

421

C → A: Reduces hydrolysis of PtdIns(4)P; when associated with A-424 and A-427. Ref.13

Mutagenesis

424

C → A: Reduces hydrolysis of PtdIns(4)P; when associated with A-421 and A-427. Ref.13

Mutagenesis

427

R → A: Reduces hydrolysis of PtdIns(4)P; when associated with A-421 and A-424. Ref.13

Mutagenesis

746

D → A: Abolishes hydrolysis of PtdIns(4,5)P2; when associated with A-748. Ref.13

Mutagenesis

748

N → A: Abolishes hydrolysis of PtdIns(4,5)P2; when associated with A-746. Ref.13

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Sequences

Sequence

Length

Mass (Da)

Tools

Q12271-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 1E024F15085261EA
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FASTA

1,107

124,577

        10         20         30         40         50         60 
MIIFVSEEPE RRLAIVSNLY ALVLKPVGKK PSDKPLCAIE LLQKNDLKKY GFKRLTSHEI 

        70         80         90        100        110        120 
FGVIGLIEVN GLLFVGAITG KSKVAQPCPG ETVNKIFAVD FFCLNDNSWD FIEIDSSGYP 

       130        140        150        160        170        180 
VLPETASTEY QDALPKHPCY ELKKLLSNGS FYYSSDFDLT STLQHRGYGQ HSLSTDTYEE 

       190        200        210        220        230        240 
EYMWNSFLMQ EMITYRDHLD TNLKQILDDE GFLTTVIRGF AETFVSYVKK LKVALTIISK 

       250        260        270        280        290        300 
QSWKRAGTRF NARGVDDEAN VANFVETEFI MYSSQYCYAF TQIRGSIPVF WEQGTSLINP 

       310        320        330        340        350        360 
RVQITRSFEA TQPVFDKHIM KSVEKYGPVH VVNLLSTKSS EIELSKRYKE HLTHSKKLNF 

       370        380        390        400        410        420 
NKDIFLTEFD FHKETSQEGF SGVRKLIPLI LDSLLSSGYY SYDVREKKNI SEQHGIFRTN 

       430        440        450        460        470        480 
CLDCLDRTNL AQQIISLAAF RTFLEDFRLI SSNSFIDDDD FVSKHNTLWA DHGDQISQIY 

       490        500        510        520        530        540 
TGTNALKSSF SRKGKMSLAG ALSDATKSVS RIYINNFMDK EKQQNIDTLL GRLPYQKAVQ 

       550        560        570        580        590        600 
LYDPVNEYVS TKLQSMSDKF TSTSNINLLI GSFNVNGATK KVDLSKWLFP IGEKFKPDIV 

       610        620        630        640        650        660 
VLGLQEVIEL SAGSILNADY SKSSFWENLV GDCLNQYDDK YLLLRVEQMT SLLILFFVKA 

       670        680        690        700        710        720 
DKAKYVKQVE GATKKTGFRG MAGNKGAVSI RFEYGATSFC FVNSHLAAGA TNVEERRSDY 

       730        740        750        760        770        780 
ESIVRGITFT RTKMIPHHDS IFWLGDMNYR INLPNEDVRR ELLNQEEGYI DKLLHFDQLT 

       790        800        810        820        830        840 
LGINSGSVFE GFKEPTLKFR PTYKYDPGTG TYDSSEKERT PSWTDRIIYK GENLLPLSYS 

       850        860        870        880        890        900 
DAPIMISDHR PVYAAYRAKI TFVDDKERLS LKKRLFTEYK QEHPEEPGSL ISDLLSLDLD 

       910        920        930        940        950        960 
NKSTDGFKSS SESSLLDIDP IMAQPTASSV ASSSPVSSAS ASLQPVRTQN SSQSRTPIKK 

       970        980        990       1000       1010       1020 
PVLRPPPPPA HKSVSAPAPS TSKEKSPTPQ TSTASLSSVT KNIQENKPLA QNRRIPPPGF 

      1030       1040       1050       1060       1070       1080 
SQNILTPKST SNLASPMSSK VDLYNSASES TRSAQDARQQ TPTAFAASRD VNGQPEALLG 

      1090       1100 
DENPIEPEEK AKLNHMTLDS WQPLTPK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequencing and analysis of 130 kb from yeast chromosome XV." Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C., Schwager C., Paces V., Sander C., Ansorge W. Yeast 13:655-672(1997) [PubMed: 9200815] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. Kleine K. Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"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.
[4]	"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.
[5]	"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.
[6]	"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.
[7]	"Disruption of six unknown open reading frames from Saccharomyces cerevisiae reveals two genes involved in vacuolar morphogenesis and one gene required for sporulation." Saiz J.E., de Los Angeles Santos M., Vazquez de Aldana C.R., Revuelta J.L. Yeast 15:155-164(1999) [PubMed: 10029994] [Abstract] Cited for: FUNCTION.
[8]	"Synthetic genetic interactions with temperature-sensitive clathrin in Saccharomyces cerevisiae. Roles for synaptojanin-like Inp53p and dynamin-related Vps1p in clathrin-dependent protein sorting at the trans-Golgi network." Bensen E.S., Costaguta G., Payne G.S. Genetics 154:83-97(2000) [PubMed: 10628971] [Abstract] Cited for: FUNCTION.
[9]	"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.
[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, DOMAIN, SUBCELLULAR LOCATION.
[11]	"A novel mechanism for localizing membrane proteins to yeast trans-Golgi network requires function of synaptojanin-like protein." Ha S.-A., Bunch J.T., Hama H., DeWald D.B., Nothwehr S.F. Mol. Biol. Cell 12:3175-3190(2001) [PubMed: 11598201] [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]	"The synaptojanin-like protein Inp53/Sjl3 functions with clathrin in a yeast TGN-to-endosome pathway distinct from the GGA protein-dependent pathway." Ha S.-A., Torabinejad J., DeWald D.B., Wenk M.R., Lucast L., De Camilli P., Newitt R.A., Aebersold R., Nothwehr S.F. Mol. Biol. Cell 14:1319-1333(2003) [PubMed: 12686590] [Abstract] Cited for: FUNCTION, DOMAINS, MUTAGENESIS OF CYS-421; CYS-424; ARG-427; ASP-746 AND ASN-748, INTERACTION WITH CHC1.
[14]	"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].
[15]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[16]	"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.
[17]	"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.
[18]	"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-1105, MASS SPECTROMETRY.
[19]	"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 SER-986, MASS SPECTROMETRY.
[20]	"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-903; SER-932; SER-933; SER-934; SER-975; SER-986; THR-988; SER-1029; THR-1030; SER-1031; SER-1035; SER-1039 AND THR-1061, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	X94335 Genomic DNA. Translation: CAA64029.1. Z75017 Genomic DNA. Translation: CAA99307.1.
PIR	S61667.
RefSeq	NP_014752.1.
3D structure databases
HSSP	HSSP built from PDB template 1I9Z based on UniProtKB O43001.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2555N.
IntAct	Q12271. 6 interactions.
Proteomic databases
PeptideAtlas	Q12271.
Genome annotation databases
Ensembl	YOR109W. Saccharomyces cerevisiae. [Contig view]
GeneID	854276.
GenomeReviews	Gene locus YOR109W in contig Y13140_GR.
KEGG	sce:YOR109W.
NMPDR	fig\|4932.3.peg.5855.
Organism-specific databases
CYGD	YOR109w.
SGD	S000005635. INP53.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	Q12271.
OMA	Q12271. IISKQSW.
Enzyme and pathway databases
BRENDA	3.1.3.36. 250.
Gene expression databases
ArrayExpress	Q12271.
GermOnline	YOR109W. 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	976236.

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Entry information

Entry name

INP53_YEAST

Accession

Primary (citable) accession number: Q12271

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 59 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

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

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents