Reviewed, UniProtKB/Swiss-Prot O43001 (SYJ1_SCHPO)

Names and origin

Protein names

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

Gene names

Name:	syj1
ORF Names:	SPBC2G2.02

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	1076 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Controls the cellular levels and subcellular distribution of phosphatidylinositol 3-phosphate and phosphatidylinositol 4,5-bisphosphate. Involved in distinct membrane trafficking and signal transduction pathways. Highly active against a range of soluble and lipid inositol phosphates. Active in dephosphorylating the 5-position of Ins(1,4,5)P3 and Ins(1,3,4,5)P4 and to a lesser extent Ins(1,4,5,6)P4. The enzyme is also active against PI(4,5)P2 presented in sonicated vesicles and Triton mixed micelles, and somewhat less active against PI(3,5)P2 in unilamellar vesicles. Activity against PI(3,5)P2 drops sharply when this substrate is presented in mixed micelles. Also hydrolyzes PIP3 to produce PI(3,4)P2. Ref.2
Catalytic activity	1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate. Ref.4
Cofactor	Magnesium. Ref.2
Subcellular location	Cytoplasm. Note: Localizes at the cell tip and the barrier septum. Ref.3
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.
Biophysicochemical properties	Kinetic parameters: KM=57.8 µM for Ins(1,4,5)P3 (at pH 7.4 and 30 degrees Celsius) KM=10.9 µM for Ins(2,4,5)P3 (at pH 7.4 and 30 degrees Celsius) KM=75.9 µM for Ins(2,4)P2 (at pH 7.4 and 30 degrees Celsius) KM=5860 µM for p-nitrophenyl phosphate (at pH 7 and 30 degrees Celsius) KM=182 µM for 3-O-methylfluorescein phosphate (at pH 7 and 30 degrees Celsius) KM=530 µM for magnesium ions KM=12 µM for manganese ions KM=6.39 µM for nickel ions KM=14.5 µM for cobalt ions pH dependence: Optimum pH is about 7.4.

Ontologies

Keywords
Biological process	Lipid metabolism Protein transport Transport
Cellular component	Cytoplasm
Ligand	Magnesium
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	inositol lipid-mediated signaling Inferred by curator. Source: GeneDB_SPombe lipid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	barrier septum Ref.3 Inferred from direct assay. Source: GeneDB_SPombe cell tip Ref.3 Inferred from direct assay. Source: GeneDB_SPombe cytosol Ref.3 Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	inositol-polyphosphate 5-phosphatase activity Ref.2 Inferred from direct assay. Source: GeneDB_SPombe magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1076

1076

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

PRO_0000209736

Regions

Domain

144 – 474

331

SAC

Region

534 – 880

347

Catalytic

Compositional bias

1000 – 1048

49

Pro-rich

Experimental info

Mutagenesis

597

1

E → A or Q: Reduces the catalytic activity by 3 to 4 orders of magnitude. Ref.2

Secondary structure

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1076

Helix Strand Turn

Details...

Helix

536 – 545

10

Turn

546 – 548

3

Helix

549 – 551

3

Beta strand

553 – 566

14

Helix

577 – 580

4

Beta strand

583 – 585

3

Beta strand

589 – 596

8

Helix

611 – 627

17

Beta strand

635 – 643

9

Beta strand

646 – 653

8

Helix

654 – 659

6

Beta strand

660 – 669

10

Beta strand

680 – 688

9

Beta strand

691 – 699

9

Helix

707 – 720

14

Helix

724 – 726

3

Beta strand

729 – 740

12

Beta strand

745 – 747

3

Helix

749 – 757

9

Helix

761 – 765

5

Helix

769 – 775

7

Beta strand

778 – 780

3

Beta strand

816 – 823

8

Beta strand

825 – 831

7

Beta strand

836 – 839

4

Beta strand

842 – 853

12

Helix

855 – 876

22

Sequences

	Sequence		Length	Mass (Da)
	O43001-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 5E26C9BF43AF20B8	FASTA	1,076	121,822
	10 20 30 40 50 60 MQCLLREKPR SLALVNKDHA LMFHSVPQNK NSLSVCVAEF TALSEKPLEG FRKISSHRIY 70 80 90 100 110 120 GTLGLIELEG SNFLCVISGA SEVARVRDKE RVFRIMEVCF YSVNRSNWDH IRQENYSPDI 130 140 150 160 170 180 PDGYDTDTQG YDSYKYAAEP FSSLRKLLTN GSFYFSLDFD ITTRLQLRTS QTMTEPQYDS 190 200 210 220 230 240 MHTQFMWNEF MLRQLIKFRS HLNGDEKSAL DGCRFFTCAI RGFASTEQFK LGIQTIRLSL 250 260 270 280 290 300 ISRLSSLRAG TRFLSRGVDD DGNVANFVET ETILDSSKYC VSYCQVRGSI PIFWEQEGVQ 310 320 330 340 350 360 MFGQKIDITR SLEATRAAFE KHFTSLIEEY GPVHIINLLG TGSGERSLSE RLRQHIQLSP 370 380 390 400 410 420 EKDLIHLTEF DYHSQIRSFE DANKIRPMIY SDAETFGFYF ENNEGQSIVV QDGVFRTNCL 430 440 450 460 470 480 DCLDRTNVIQ NLVSRVFLEQ VMIYTRQNAG YDFWQVHSTI WANNGDALAR IYTGTGALKS 490 500 510 520 530 540 SFTRKGKLSI AGALNDLSKS VGRMYINNFQ DKGRQETIDL LLGRLIDQHP VILYDPIHEY 550 560 570 580 590 600 VNHELRKREN EFSEHKNVKI FVASYNLNGC SATTKLENWL FPENTPLADI YVVGFQEIVQ 610 620 630 640 650 660 LTPQQVISAD PAKRREWESC VKRLLNGKCT SGPGYVQLRS GQLVGTALMI FCKESCLPSI 670 680 690 700 710 720 KNVEGTVKKT GLGGVSGNKG AVAIRFDYED TGLCFITSHL AAGYTNYDER DHDYRTIASG 730 740 750 760 770 780 LRFRRGRSIF NHDYVVWFGD FNYRISLTYE EVVPCIAQGK LSYLFEYDQL NKQMLTGKVF 790 800 810 820 830 840 PFFSELPITF PPTYKFDIGT DIYDTSDKHR VPAWTDRILY RGELVPHSYQ SVPLYYSDHR 850 860 870 880 890 900 PIYATYEANI VKVDREKKKI LFEELYNQRK QEVRDASQTS YTLIDIAGSV AGKPNLIPHL 910 920 930 940 950 960 PANGVDKIKQ PSSERSKWWF DDGLPAKSIA APPGPEYRLN PSRPINPFEP TAEPDWISNT 970 980 990 1000 1010 1020 KQSFDKKSSL IDSIPALSPA PSSLARSSVS SQRSSTSIIP IKPNKPTKPD HLVAPRVKPL 1030 1040 1050 1060 1070 LPPRSGSSSS GVPAPNLTPV NVPPTPPPRK SSASQRSGDL LASSPEESSI SWKPLV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[2]	"Comparative mechanistic and substrate specificity study of inositol polyphosphate 5-phosphatase Schizosaccharomyces pombe Synaptojanin and SHIP2." Chi Y., Zhou B., Wang W.-Q., Chung S.-K., Kwon Y.-U., Ahn Y.-H., Chang Y.-T., Tsujishita Y., Hurley J.H., Zhang Z.-Y. J. Biol. Chem. 279:44987-44995(2004) [PubMed: 15316017] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, MUTAGENESIS OF GLU-597.
[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(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]	"Specificity determinants in phosphoinositide dephosphorylation: crystal structure of an archetypal inositol polyphosphate 5-phosphatase." Tsujishita Y., Guo S., Stolz L.E., York J.D., Hurley J.H. Cell 105:379-389(2001) [PubMed: 11348594] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 534-880, CATALYTIC ACTIVITY.

Cross-references

Sequence databases

EMBLGenBankDDBJ

CU329671 Genomic DNA. Translation: CAA17882.1.

PIR

T40141.

RefSeq

NP_596431.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I9Y	X-ray	2.00	A	534-880	[»]
1I9Z	X-ray	1.80	A	534-880	[»]

ModBase

Search...

Genome annotation databases

GeneID

2540270.

KEGG

spo:SPBC2G2.02.

NMPDR

fig|4896.1.peg.2297.

Organism-specific databases

GeneDB_Spombe

SPBC2G2.02.

Phylogenomic databases

OMA

O43001. IISKQSW.

Enzyme and pathway databases

BRENDA

3.1.3.36. 653.

Gene expression databases

ArrayExpress

O43001.

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...

Entry information

Entry name

SYJ1_SCHPO

Accession

Primary (citable) accession number: O43001

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	June 1, 1998
Last modified:	May 5, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)