FAB1_SCHPO
ID FAB1_SCHPO Reviewed; 1932 AA.
AC O59722; O43072;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=1-phosphatidylinositol 3-phosphate 5-kinase fab1;
DE Short=Phosphatidylinositol 3-phosphate 5-kinase;
DE EC=2.7.1.150;
DE AltName: Full=Diphosphoinositide kinase;
DE AltName: Full=Type III PIP kinase;
DE Short=PIPkin-III;
GN Name=fab1; Synonyms=ste12; ORFNames=SPBC3E7.01, SPBC6B1.11c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11895483; DOI=10.1046/j.1356-9597.2001.00510.x;
RA Morishita M., Morimoto F., Kitamura K., Koga T., Fukui Y., Maekawa H.,
RA Yamashita I., Shimoda C.;
RT "Phosphatidylinositol 3-phosphate 5-kinase is required for the cellular
RT response to nutritional starvation and mating pheromone signals in
RT Schizosaccharomyces pombe.";
RL Genes Cells 7:199-215(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis
CC and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
CC Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on
CC the fifth hydroxyl of the myo-inositol ring, to form
CC phosphatidylinositol 3,5-bisphosphate. Required for endocytic-vacuolar
CC pathway and nuclear migration. The product of the reaction, PI(3,5)P2
CC is an important regulator of vacuole homeostasis perhaps by controlling
CC membrane flux to and/or from the vacuole. PI(3,5)P2 regulates the
CC transition between trans-SNARE complex formation and vacuole membrane
CC fusion (By similarity). Required for survival under conditions of
CC nitrogen starvation. May have a role in the secretion of pheromone
CC peptides (PubMed:11895483). {ECO:0000250|UniProtKB:P34756,
CC ECO:0000269|PubMed:11895483}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:13609,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57923,
CC ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.150;
CC Evidence={ECO:0000269|PubMed:11895483};
CC -!- SUBUNIT: Component of the PI(3,5)P2 regulatory complex, at least
CC composed of fab1, fig4/SPAC1093.03 and vac14/SPBC25H2.03. Vac14
CC nucleates the assembly of the complex and serves as a scaffold.
CC {ECO:0000250|UniProtKB:P34756}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11895483}.
CC Note=During cell fusion of opposite mating types, migrates to the
CC isthmus. {ECO:0000269|PubMed:11895483}.
CC -!- DOMAIN: The chaperone-containing TCP1 (CCT) domain is essential for the
CC interaction with the scaffold protein vac14/SPBC25H2.03.
CC {ECO:0000250|UniProtKB:P34756}.
CC -!- DOMAIN: The conserved cysteine-rich (CCR) domain contacts
CC intramolecularly the C-terminus, including the kinase domain, and this
CC interaction negatively regulates PI(3) 5-kinase activity.
CC {ECO:0000250|UniProtKB:P34756}.
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DR EMBL; CU329671; CAA17054.1; -; Genomic_DNA.
DR PIR; T40375; T40375.
DR PIR; T40652; T40652.
DR RefSeq; NP_596090.2; NM_001022005.3.
DR AlphaFoldDB; O59722; -.
DR SMR; O59722; -.
DR BioGRID; 277669; 7.
DR STRING; 4896.SPBC3E7.01.1; -.
DR iPTMnet; O59722; -.
DR MaxQB; O59722; -.
DR PaxDb; O59722; -.
DR PRIDE; O59722; -.
DR EnsemblFungi; SPBC3E7.01.1; SPBC3E7.01.1:pep; SPBC3E7.01.
DR GeneID; 2541154; -.
DR KEGG; spo:SPBC3E7.01; -.
DR PomBase; SPBC3E7.01; fab1.
DR VEuPathDB; FungiDB:SPBC3E7.01; -.
DR eggNOG; KOG0230; Eukaryota.
DR HOGENOM; CLU_000480_3_1_1; -.
DR InParanoid; O59722; -.
DR OMA; HRQYVHG; -.
DR PhylomeDB; O59722; -.
DR BRENDA; 2.7.1.150; 5613.
DR PRO; PR:O59722; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0010008; C:endosome membrane; IBA:GO_Central.
DR GO; GO:0000329; C:fungal-type vacuole membrane; ISO:PomBase.
DR GO; GO:0070772; C:PAS complex; ISO:PomBase.
DR GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISO:PomBase.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR CDD; cd17300; PIPKc_PIKfyve; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.800.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR044769; PIKfyve_PIPKc.
DR InterPro; IPR002498; PInositol-4-P-5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF01504; PIP5K; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00330; PIPKc; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51455; PIPK; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1932
FT /note="1-phosphatidylinositol 3-phosphate 5-kinase fab1"
FT /id="PRO_0000185450"
FT DOMAIN 1590..1916
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT ZN_FING 60..119
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 457..721
FT /note="CCT domain"
FT /evidence="ECO:0000250|UniProtKB:P34756"
FT REGION 763..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..1231
FT /note="CCR domain"
FT /evidence="ECO:0000250|UniProtKB:P34756"
FT REGION 1346..1371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1457..1504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1522..1544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1475..1492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1522..1538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ SEQUENCE 1932 AA; 220135 MW; B9826516D4504229 CRC64;
MSEVETPTAA SPTFPVETSH RLDTLHTSST EQIIKDSENV VHTTLKLPTS TLSREFWMKD
ERTNNCSLCE TEFTLFRRKH HCRICGKIIC KYCLKEAPGF IFRLQGSIKV CRPCASILVN
NYSRSQLFNH SLNESKNRDL TEQHPFVTLD ELNSNDQVLS SFGDLSSTFE MPNNIHPPEV
APMIAIPSSR SNYDSPGWAH HSIFLDWSKR NLDSNVINVE DSESGKYNAL TITNSYDAGP
SSVSTDYRPV NFGKVPSYSK LRKNKAFSSA KVSDMYLSAD ERNRLEDFSK GDRGLSFVNL
SPNIKATSYD RLSTVINEPF ISRSSSLTDE RGLADSGNSY HHFSDSDDES LFNDGLGLSF
HANSAIIKQR QQNVASIQRY GNESYLSNFL KAFLPKTVCD YLFPSSTIPD GLPALIENFN
ARVDKVNHPG GTEEPLPYQG KSRASSVVTS SKSTCILPPW ILFSDSFNQL VCTFLGKLLF
QMLNDEGVDS PMQWVLCLPK ILLKMALDLG PDIRSGDDID VRSYVKIKKI PGGSIQDCFL
VNGVLFSKKA SSKSMDRSLR RPRIALLTFS LDYACDEQRI LSLDLIISQQ EEYIINLVNR
ICMLKPNLVF AQGQIPSIAL KYFEEHGVIA FHGLKESVLY DIARCCRADI ISSIDKLSLC
PRLGTCGRFQ LRTYVVDENK GLRKTFAILD RCSERLGCTI VLRGADYNQL SKVKKIVELV
VLIAYHIKLE CALLRDKFVN MPELFETTYQ SLSRKSLPSF ASTAADKEKS QNHEKKSLNS
DNQSLRPLEN ENQSVSSTQG SNSPLELINN LPASDDYSSI TKALKTRFLT FSPFLSKPLP
RLLNQVNYYQ FIRNKLLKDV KLHPYSPTGS FVMKQSENDN VEESYEESYK FFCIDERYHF
LEKQWTLYYS HSKLMFSPFS SQRIILLYSI INKETSVPCI GPERCLLEFY RETDCTLGQY
IEDSCLNTNV SCGGEYCKTN DMLWHYRSYV HGNSRISVFL ESFSCPVPGL EEKIIMWSYC
KFCKKNTHIT VMSEETWKYS FGKYLEFMFY NSQIRDRFEF CDHSVMAQHV HYFGYCNMAL
RFQRDLIEIF ELFVPSVTLR NNPSYIKELK EKEYKRLKGV IEKCLSSVAS RINQIKCDWV
TDPEKFESCT SEISKFRTLL SSDYTELYSE FDSIYLNSST SDYLSLNSIL RVLQGKMVKW
EQRFLDYQRL YLPSYKELSK IAAAQIKKVF LERPLSQTPL DLPETLENTQ IDIYPSFKTE
STDDQLEKVT QTNVASNKRV APYADSMANV GSPESDCFSV ATSSDIPKAN IDFTNDISTQ
NTFPASPVSN SGFSRQTYPN ISQRQGVNML SHKRKSASTS DRRFVNASST SGMNMPISSS
ISAKISSIQN STKYSPRKPI PAKDVRVSSL VRRFEELSLQ LQEKQKRDEE LIKARRKRAL
PVVPSKPVVE VFNDLNEAFD DENSEDENGI NDTKENRATE SNFSGVDSMS KERENVSSNE
DNSPEAFEDI FGILFKNESG LEEQQNLEPS SQMDKEGSKL PTSGPLADKT SVYRILSAFW
NEWNSLNPPP FEFPLQPTEH MFSDSNVIIR EDEPSSLISF TLSSPDYLSK MVEIEDSMDE
ALTNQGLQGS TQFKIENLML KPTGTHLKYQ FEEGSARLSC KVFFAEQFSA LRRACGCEET
FVTSLARCSL WESSGGKSGS AFLKTFDKKY ILKVLSRLES DSLLNFAPAY FDYISKVFFH
ELPTALTKIF GFYRVDIRNP TTGTICKTDI MIMENVFYDE CPSRIFDLKG SMRNRHVEST
GKVDEVLLDE NLVELIYESP IFVSEQLKSL LHSCLWNDTL FLSKLNIMDY SLIVGIDYTK
KELYVGIIDF IRTYTWDKKL ESWVKEKGLV GRGPEPTIVT PKQYKNRFRK AMDCYILASQ
DFETGEGFKF CE
