Reviewed, UniProtKB/Swiss-Prot O59722 (FAB1_SCHPO)

Names and origin

Protein names

Recommended name:
    1-phosphatidylinositol-3-phosphate 5-kinase fab1
      Short name=Phosphatidylinositol-3-phosphate 5-kinase
    EC=2.7.1.150
Alternative name(s):
    Type III PIP kinase
      Short name=PIPkin-III
    Diphosphoinositide kinase

Gene names

Name:	fab1
Synonyms:	ste12
ORF Names:	SPBC3E7.01, SPBC6B1.11c

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	1932 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2) By similarity. Catalyzes the phosphorylation of phosphatidylinositol-3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol-3,5-bisphosphate. Required for endocytic-vacuolar pathway and nuclear migration. The product of the reaction it catalyzes functions as an important regulator of vacuole homeostasis perhaps by controlling membrane flux to and/or from the vacuole By similarity. Required for survival under conditions of nitrogen starvation. May have a role in the secretion of pheromone peptides.
Catalytic activity	ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate.
Subunit structure	Component of the PI(3,5)P2 regulatory complex, at least composed of fab1, fig4/SPAC1093.03 and vac14/SPBC25H2.03 By similarity. Vac14 nucleates the assembly of the complex and serves as a scaffold By similarity.
Subcellular location	Cytoplasm. Note: During cell fusion of opposite mating types, migrates to the isthmus. Ref.1
Sequence similarities	Contains 1 FYVE-type zinc finger. Contains 1 PIPK domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular protein metabolic process Inferred from electronic annotation. Source: InterPro cellular response to nitrogen starvation Non-traceable author statement. Source: GeneDB_SPombe endocytosis Traceable author statement. Source: GeneDB_SPombe intracellular protein transport Inferred by curator. Source: GeneDB_SPombe pheromone-dependent signal transduction involved in conjugation with cellular fusion Inferred from mutant phenotype. Source: GeneDB_SPombe phosphatidylinositol metabolic process Inferred by curator. Source: GeneDB_SPombe
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	1-phosphatidylinositol-3-phosphate 5-kinase activity Ref.1 Inferred from direct assay. Source: GeneDB_SPombe 1-phosphatidylinositol-4-phosphate 5-kinase activity Inferred from electronic annotation. Source: EC ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1932	1932	1-phosphatidylinositol-3-phosphate 5-kinase fab1		PRO_0000185450
Regions
	Domain	1590 – 1916	327	PIPK
	Zinc finger	60 – 119	60	FYVE-type

Sequences

	Sequence		Length	Mass (Da)
	O59722-1 [UniParc]. Last modified May 16, 2003. Version 2. Checksum: B9826516D4504229	FASTA	1,932	220,135
	10 20 30 40 50 60 MSEVETPTAA SPTFPVETSH RLDTLHTSST EQIIKDSENV VHTTLKLPTS TLSREFWMKD 70 80 90 100 110 120 ERTNNCSLCE TEFTLFRRKH HCRICGKIIC KYCLKEAPGF IFRLQGSIKV CRPCASILVN 130 140 150 160 170 180 NYSRSQLFNH SLNESKNRDL TEQHPFVTLD ELNSNDQVLS SFGDLSSTFE MPNNIHPPEV 190 200 210 220 230 240 APMIAIPSSR SNYDSPGWAH HSIFLDWSKR NLDSNVINVE DSESGKYNAL TITNSYDAGP 250 260 270 280 290 300 SSVSTDYRPV NFGKVPSYSK LRKNKAFSSA KVSDMYLSAD ERNRLEDFSK GDRGLSFVNL 310 320 330 340 350 360 SPNIKATSYD RLSTVINEPF ISRSSSLTDE RGLADSGNSY HHFSDSDDES LFNDGLGLSF 370 380 390 400 410 420 HANSAIIKQR QQNVASIQRY GNESYLSNFL KAFLPKTVCD YLFPSSTIPD GLPALIENFN 430 440 450 460 470 480 ARVDKVNHPG GTEEPLPYQG KSRASSVVTS SKSTCILPPW ILFSDSFNQL VCTFLGKLLF 490 500 510 520 530 540 QMLNDEGVDS PMQWVLCLPK ILLKMALDLG PDIRSGDDID VRSYVKIKKI PGGSIQDCFL 550 560 570 580 590 600 VNGVLFSKKA SSKSMDRSLR RPRIALLTFS LDYACDEQRI LSLDLIISQQ EEYIINLVNR 610 620 630 640 650 660 ICMLKPNLVF AQGQIPSIAL KYFEEHGVIA FHGLKESVLY DIARCCRADI ISSIDKLSLC 670 680 690 700 710 720 PRLGTCGRFQ LRTYVVDENK GLRKTFAILD RCSERLGCTI VLRGADYNQL SKVKKIVELV 730 740 750 760 770 780 VLIAYHIKLE CALLRDKFVN MPELFETTYQ SLSRKSLPSF ASTAADKEKS QNHEKKSLNS 790 800 810 820 830 840 DNQSLRPLEN ENQSVSSTQG SNSPLELINN LPASDDYSSI TKALKTRFLT FSPFLSKPLP 850 860 870 880 890 900 RLLNQVNYYQ FIRNKLLKDV KLHPYSPTGS FVMKQSENDN VEESYEESYK FFCIDERYHF 910 920 930 940 950 960 LEKQWTLYYS HSKLMFSPFS SQRIILLYSI INKETSVPCI GPERCLLEFY RETDCTLGQY 970 980 990 1000 1010 1020 IEDSCLNTNV SCGGEYCKTN DMLWHYRSYV HGNSRISVFL ESFSCPVPGL EEKIIMWSYC 1030 1040 1050 1060 1070 1080 KFCKKNTHIT VMSEETWKYS FGKYLEFMFY NSQIRDRFEF CDHSVMAQHV HYFGYCNMAL 1090 1100 1110 1120 1130 1140 RFQRDLIEIF ELFVPSVTLR NNPSYIKELK EKEYKRLKGV IEKCLSSVAS RINQIKCDWV 1150 1160 1170 1180 1190 1200 TDPEKFESCT SEISKFRTLL SSDYTELYSE FDSIYLNSST SDYLSLNSIL RVLQGKMVKW 1210 1220 1230 1240 1250 1260 EQRFLDYQRL YLPSYKELSK IAAAQIKKVF LERPLSQTPL DLPETLENTQ IDIYPSFKTE 1270 1280 1290 1300 1310 1320 STDDQLEKVT QTNVASNKRV APYADSMANV GSPESDCFSV ATSSDIPKAN IDFTNDISTQ 1330 1340 1350 1360 1370 1380 NTFPASPVSN SGFSRQTYPN ISQRQGVNML SHKRKSASTS DRRFVNASST SGMNMPISSS 1390 1400 1410 1420 1430 1440 ISAKISSIQN STKYSPRKPI PAKDVRVSSL VRRFEELSLQ LQEKQKRDEE LIKARRKRAL 1450 1460 1470 1480 1490 1500 PVVPSKPVVE VFNDLNEAFD DENSEDENGI NDTKENRATE SNFSGVDSMS KERENVSSNE 1510 1520 1530 1540 1550 1560 DNSPEAFEDI FGILFKNESG LEEQQNLEPS SQMDKEGSKL PTSGPLADKT SVYRILSAFW 1570 1580 1590 1600 1610 1620 NEWNSLNPPP FEFPLQPTEH MFSDSNVIIR EDEPSSLISF TLSSPDYLSK MVEIEDSMDE 1630 1640 1650 1660 1670 1680 ALTNQGLQGS TQFKIENLML KPTGTHLKYQ FEEGSARLSC KVFFAEQFSA LRRACGCEET 1690 1700 1710 1720 1730 1740 FVTSLARCSL WESSGGKSGS AFLKTFDKKY ILKVLSRLES DSLLNFAPAY FDYISKVFFH 1750 1760 1770 1780 1790 1800 ELPTALTKIF GFYRVDIRNP TTGTICKTDI MIMENVFYDE CPSRIFDLKG SMRNRHVEST 1810 1820 1830 1840 1850 1860 GKVDEVLLDE NLVELIYESP IFVSEQLKSL LHSCLWNDTL FLSKLNIMDY SLIVGIDYTK 1870 1880 1890 1900 1910 1920 KELYVGIIDF IRTYTWDKKL ESWVKEKGLV GRGPEPTIVT PKQYKNRFRK AMDCYILASQ 1930 DFETGEGFKF CE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Phosphatidylinositol 3-phosphate 5-kinase is required for the cellular response to nutritional starvation and mating pheromone signals in Schizosaccharomyces pombe." Morishita M., Morimoto F., Kitamura K., Koga T., Fukui Y., Maekawa H., Yamashita I., Shimoda C. Genes Cells 7:199-215(2002) [PubMed: 11895483] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
[2]	"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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329671 Genomic DNA. Translation: CAA17054.1.
PIR	T40375. T40652.
RefSeq	NP_596090.2.
3D structure databases
HSSP	HSSP built from PDB template 1DVP based on UniProtKB Q960X8.
ModBase	Search...
Protein-protein interaction databases
STRING	O59722.
Genome annotation databases
GeneID	2541154.
GenomeReviews	Gene locus fab1 in contig CU329671_GR.
KEGG	spo:SPBC3E7.01.
Organism-specific databases
GeneDB_Spombe	SPBC3E7.01.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-004849-MON.
BRENDA	2.7.1.68. 653.
Gene expression databases
ArrayExpress	O59722.
Family and domain databases
InterPro	IPR002423. Cpn60/TCP-1. IPR002498. PInositol-4-P-5-kinase_core. IPR016034. PInositol-4P-5-kinase_core_sub. IPR000306. Znf_FYVE. IPR017455. Znf_FYVE-rel. [Graphical view]
Pfam	PF00118. Cpn60_TCP1. 1 hit. PF01363. FYVE. 1 hit. PF01504. PIP5K. 1 hit. [Graphical view]
SMART	SM00064. FYVE. 1 hit. SM00330. PIPKc. 1 hit. [Graphical view]
PROSITE	PS51455. PIPK. 1 hit. PS50178. ZF_FYVE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FAB1_SCHPO

Accession

Primary (citable) accession number: O59722
Secondary accession number(s): O43072

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2003
Last sequence update:	May 16, 2003
Last modified:	November 3, 2009
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)