ID FAB1_YEAST Reviewed; 2278 AA.
AC P34756; D6VTQ0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 3.
DT 27-MAR-2024, entry version 203.
DE RecName: Full=1-phosphatidylinositol 3-phosphate 5-kinase FAB1 {ECO:0000305};
DE Short=Phosphatidylinositol 3-phosphate 5-kinase;
DE EC=2.7.1.150;
DE AltName: Full=Formation of aploid and binucleate cells protein 1 {ECO:0000303|PubMed:7663021};
DE AltName: Full=Styryl dye vacuolar localization protein 7 {ECO:0000303|PubMed:9751732};
DE AltName: Full=Type III PIP kinase;
DE Short=PIPkin-III;
GN Name=FAB1 {ECO:0000303|PubMed:7663021};
GN Synonyms=SVL7 {ECO:0000303|PubMed:9751732}; OrderedLocusNames=YFR019W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7663021; DOI=10.1091/mbc.6.5.525;
RA Yamamoto A., Dewald D.B., Boronenkov I.V., Anderson R.A., Emr S.D.,
RA Koshland D.;
RT "Novel PI(4)P 5-kinase homologue, Fab1p, essential for normal vacuole
RT function and morphology in yeast.";
RL Mol. Biol. Cell 6:525-539(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 2275.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9811604; DOI=10.1016/s0960-9822(07)00513-1;
RA Cooke F.T., Dove S.K., McEwen R.K., Painter G., Holmes A.B., Hall M.N.,
RA Michell R.H., Parker P.J.;
RT "The stress-activated phosphatidylinositol 3-phosphate 5-kinase Fab1p is
RT essential for vacuole function in S. cerevisiae.";
RL Curr. Biol. 8:1219-1222(1998).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9763421; DOI=10.1083/jcb.143.1.65;
RA Gary J.D., Wurmser A.E., Bonangelino C.J., Weisman L.S., Emr S.D.;
RT "Fab1p is essential for PtdIns(3)P 5-kinase activity and the maintenance of
RT vacuolar size and membrane homeostasis.";
RL J. Cell Biol. 143:65-79(1998).
RN [6]
RP FUNCTION.
RX PubMed=9751732; DOI=10.1073/pnas.95.20.11721;
RA Zheng B., Wu J.N., Schober W., Lewis D.E., Vida T.;
RT "Isolation of yeast mutants defective for localization of vacuolar vital
RT dyes.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11721-11726(1998).
RN [7]
RP ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=11889142; DOI=10.1083/jcb.200201002;
RA Bonangelino C.J., Nau J.J., Duex J.E., Brinkman M., Wurmser A.E.,
RA Gary J.D., Emr S.D., Weisman L.S.;
RT "Osmotic stress-induced increase of phosphatidylinositol 3,5-bisphosphate
RT requires Vac14p, an activator of the lipid kinase Fab1p.";
RL J. Cell Biol. 156:1015-1028(2002).
RN [8]
RP ACTIVITY REGULATION.
RX PubMed=11950935; DOI=10.1091/mbc.01-10-0498;
RA Gary J.D., Sato T.K., Stefan C.J., Bonangelino C.J., Weisman L.S.,
RA Emr S.D.;
RT "Regulation of Fab1 phosphatidylinositol 3-phosphate 5-kinase pathway by
RT Vac7 protein and Fig4, a polyphosphoinositide phosphatase family member.";
RL Mol. Biol. Cell 13:1238-1251(2002).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP FUNCTION.
RX PubMed=16492811; DOI=10.1083/jcb.200512105;
RA Duex J.E., Tang F., Weisman L.S.;
RT "The Vac14p-Fig4p complex acts independently of Vac7p and couples PI3,5P2
RT synthesis and turnover.";
RL J. Cell Biol. 172:693-704(2006).
RN [12]
RP IDENTIFICATION IN THE PI(3,5)P2 REGULATORY COMPLEX, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF GLY-864, AND DOMAIN.
RX PubMed=19037259; DOI=10.1038/emboj.2008.248;
RA Jin N., Chow C.Y., Liu L., Zolov S.N., Bronson R., Davisson M.,
RA Petersen J.L., Zhang Y., Park S., Duex J.E., Goldowitz D., Meisler M.H.,
RA Weisman L.S.;
RT "VAC14 nucleates a protein complex essential for the acute interconversion
RT of PI3P and PI(3,5)P(2) in yeast and mouse.";
RL EMBO J. 27:3221-3234(2008).
RN [13]
RP IDENTIFICATION IN THE PI(3,5)P2 REGULATORY COMPLEX, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF CYS-262; THR-1017; CYS-1243 AND ASP-2134, AND DOMAIN.
RX PubMed=18653468; DOI=10.1091/mbc.e08-04-0405;
RA Botelho R.J., Efe J.A., Teis D., Emr S.D.;
RT "Assembly of a Fab1 phosphoinositide kinase signaling complex requires the
RT Fig4 phosphoinositide phosphatase.";
RL Mol. Biol. Cell 19:4273-4286(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1953, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186; SER-1627; SER-1630 AND
RP SER-1938, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP DOMAIN, AND MUTAGENESIS OF GLN-1419; ASP-1486; THR-1491; THR-2250; GLN-2253
RP AND ARG-2264.
RX PubMed=28148651; DOI=10.1091/mbc.e16-06-0390;
RA Lang M.J., Strunk B.S., Azad N., Petersen J.L., Weisman L.S.;
RT "An intramolecular interaction within the lipid kinase Fab1 regulates
RT cellular phosphatidylinositol 3,5-bisphosphate lipid levels.";
RL Mol. Biol. Cell 28:858-864(2017).
RN [18]
RP FUNCTION, AND MUTAGENESIS OF THR-2250.
RX PubMed=30427760; DOI=10.1091/mbc.e18-08-0505;
RA Miner G.E., Sullivan K.D., Guo A., Jones B.C., Hurst L.R., Ellis E.C.,
RA Starr M.L., Fratti R.A.;
RT "Phosphatidylinositol 3,5-bisphosphate regulates the transition between
RT trans-SNARE complex formation and vacuole membrane fusion.";
RL Mol. Biol. Cell 30:201-208(2019).
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 (PubMed:16492811,
CC PubMed:9811604). Required for endocytic-vacuolar pathway and nuclear
CC migration (PubMed:9751732, PubMed:16492811, PubMed:9811604). The
CC product of the reaction, PI(3,5)P2 is an important regulator of vacuole
CC homeostasis perhaps by controlling membrane flux to and/or from the
CC vacuole (PubMed:9811604, PubMed:9763421). PI(3,5)P2 regulates the
CC transition between trans-SNARE complex formation and vacuole membrane
CC fusion (PubMed:30427760). Hyperosmotic shock-induced increase in the
CC levels of PtdIns(3,5)P2 requires the presence of VAC7, VAC14, and/or
CC FIG4 (PubMed:16492811). {ECO:0000269|PubMed:16492811,
CC ECO:0000269|PubMed:30427760, ECO:0000269|PubMed:9751732,
CC ECO:0000269|PubMed:9763421, ECO:0000269|PubMed:9811604}.
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:9811604};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC phosphate) + ATP = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,5-phosphate) + ADP + H(+); Xref=Rhea:RHEA:42348,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:78994,
CC ChEBI:CHEBI:78995, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:9811604};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42349;
CC Evidence={ECO:0000305|PubMed:9811604};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC -!- ACTIVITY REGULATION: Activated by VAC14 and VAC7. VAC14 acts as a
CC specific osmotic response regulator. {ECO:0000269|PubMed:11889142,
CC ECO:0000269|PubMed:11950935}.
CC -!- SUBUNIT: Component of the PI(3,5)P2 regulatory complex, composed of
CC ATG18, FIG4, FAB1, VAC14 and VAC7. VAC14 nucleates the assembly of the
CC complex and serves as a scaffold. {ECO:0000269|PubMed:18653468,
CC ECO:0000269|PubMed:19037259}.
CC -!- INTERACTION:
CC P34756; P42837: FIG4; NbExp=4; IntAct=EBI-6754, EBI-28407;
CC P34756; Q06708: VAC14; NbExp=9; IntAct=EBI-6754, EBI-27189;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:11889142,
CC ECO:0000269|PubMed:18653468, ECO:0000269|PubMed:19037259,
CC ECO:0000269|PubMed:9763421}; Peripheral membrane protein
CC {ECO:0000269|PubMed:18653468, ECO:0000269|PubMed:19037259}. Endosome
CC membrane {ECO:0000269|PubMed:11889142, ECO:0000269|PubMed:9763421};
CC Peripheral membrane protein {ECO:0000269|PubMed:11889142,
CC ECO:0000269|PubMed:9763421}. Note=Localization to the vacuole membrane
CC requires VAC14 and FIG4. {ECO:0000269|PubMed:18653468,
CC ECO:0000269|PubMed:19037259}.
CC -!- DOMAIN: The chaperone-containing TCP1 (CCT) domain is essential for the
CC interaction with the scaffold protein VAC14.
CC {ECO:0000269|PubMed:18653468, ECO:0000269|PubMed:19037259}.
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:0000269|PubMed:18653468, ECO:0000269|PubMed:28148651}.
CC -!- MISCELLANEOUS: Present with 149 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U01017; AAA81360.1; -; Genomic_DNA.
DR EMBL; D50617; BAA09258.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12460.2; -; Genomic_DNA.
DR PIR; S56274; S56274.
DR RefSeq; NP_116674.2; NM_001179984.2.
DR AlphaFoldDB; P34756; -.
DR SMR; P34756; -.
DR BioGRID; 31172; 393.
DR ComplexPortal; CPX-3088; PAS complex.
DR DIP; DIP-6784N; -.
DR IntAct; P34756; 9.
DR MINT; P34756; -.
DR STRING; 4932.YFR019W; -.
DR SwissLipids; SLP:000000854; -.
DR CarbonylDB; P34756; -.
DR GlyGen; P34756; 17 sites, 1 O-linked glycan (17 sites).
DR iPTMnet; P34756; -.
DR MaxQB; P34756; -.
DR PaxDb; 4932-YFR019W; -.
DR PeptideAtlas; P34756; -.
DR EnsemblFungi; YFR019W_mRNA; YFR019W; YFR019W.
DR GeneID; 850574; -.
DR KEGG; sce:YFR019W; -.
DR AGR; SGD:S000001915; -.
DR SGD; S000001915; FAB1.
DR VEuPathDB; FungiDB:YFR019W; -.
DR eggNOG; KOG0230; Eukaryota.
DR GeneTree; ENSGT00940000156307; -.
DR HOGENOM; CLU_000480_3_1_1; -.
DR InParanoid; P34756; -.
DR OMA; QEKVVEW; -.
DR OrthoDB; 5481504at2759; -.
DR BioCyc; MetaCyc:YFR019W-MONOMER; -.
DR BioCyc; YEAST:YFR019W-MONOMER; -.
DR BRENDA; 2.7.1.150; 984.
DR BioGRID-ORCS; 850574; 0 hits in 10 CRISPR screens.
DR ChiTaRS; FAB1; yeast.
DR PRO; PR:P34756; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P34756; Protein.
DR GO; GO:0010008; C:endosome membrane; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0070772; C:PAS complex; IDA:SGD.
DR GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
DR GO; GO:1903100; P:1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate metabolic process; NAS:ComplexPortal.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IDA:SGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010511; P:regulation of phosphatidylinositol biosynthetic process; NAS:ComplexPortal.
DR CDD; cd03334; Fab1_TCP; 1.
DR CDD; cd17300; PIPKc_PIKfyve; 1.
DR Gene3D; 3.30.810.10; 2-Layer Sandwich; 1.
DR Gene3D; 3.50.7.10; GroEL; 1.
DR Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR044769; PIKfyve_PIPKc.
DR InterPro; IPR027483; PInositol-4-P-4/5-kinase_C_sf.
DR InterPro; IPR002498; PInositol-4-P-4/5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
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 PANTHER; PTHR45748; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE-RELATED; 1.
DR PANTHER; PTHR45748:SF7; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE-RELATED; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF01504; PIP5K; 2.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00330; PIPKc; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR PROSITE; PS51455; PIPK; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Endosome; Kinase; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Vacuole; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..2278
FT /note="1-phosphatidylinositol 3-phosphate 5-kinase FAB1"
FT /id="PRO_0000185451"
FT DOMAIN 1932..2266
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT ZN_FING 240..299
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..676
FT /note="Required for localization to the vacuole membrane"
FT REGION 76..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..1039
FT /note="CCT domain"
FT /evidence="ECO:0000269|PubMed:18653468,
FT ECO:0000269|PubMed:19037259"
FT REGION 1181..1500
FT /note="CCR domain"
FT /evidence="ECO:0000269|PubMed:18653468,
FT ECO:0000269|PubMed:28148651"
FT REGION 1506..1627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1766..1804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1891..1972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1506..1551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1552..1616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1766..1784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1891..1949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1630
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1938
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1953
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 262
FT /note="C->S: Cells show growth at 38 degrees Celsius.
FT Failure to localize to the vacuole membrane."
FT /evidence="ECO:0000269|PubMed:18653468"
FT MUTAGEN 864
FT /note="G->E: Loss of interaction with VAC14. Failure to
FT localize to the vacuole membrane."
FT /evidence="ECO:0000269|PubMed:19037259"
FT MUTAGEN 1017
FT /note="T->I: Cells are defective for growth at 38 degrees
FT Celsius."
FT /evidence="ECO:0000269|PubMed:18653468"
FT MUTAGEN 1243
FT /note="C->A: Cells are defective for growth at 38 degrees
FT Celsius and show single-lobed, enlarged vacuoles."
FT /evidence="ECO:0000269|PubMed:18653468"
FT MUTAGEN 1419
FT /note="Q->R: Impairs intramolecular interaction with the
FT kinase domain. Leads to elevated PI(3,5)P2 levels."
FT /evidence="ECO:0000269|PubMed:28148651"
FT MUTAGEN 1486
FT /note="D->N: Impairs intramolecular interaction with the
FT kinase domain. Leads to elevated PI(3,5)P2 levels."
FT /evidence="ECO:0000269|PubMed:28148651"
FT MUTAGEN 1491
FT /note="T->A: Impairs intramolecular interaction with the
FT kinase domain. Leads to elevated PI(3,5)P2 levels."
FT /evidence="ECO:0000269|PubMed:28148651"
FT MUTAGEN 2134
FT /note="D->R: Cells are defective for growth at 38 degrees
FT Celsius. PtdIns(3,5)P2 levels are severely reduced."
FT /evidence="ECO:0000269|PubMed:18653468"
FT MUTAGEN 2250
FT /note="T->A: Impairs intramolecular interaction with the
FT CCR domain, leading to a hyperactive kinase mutant;
FT elevates PI(3,5)P2 levels."
FT /evidence="ECO:0000269|PubMed:28148651,
FT ECO:0000269|PubMed:30427760"
FT MUTAGEN 2253
FT /note="Q->R: Impairs intramolecular interaction with the
FT CCR domain, leading to a hyperactive kinase mutant."
FT /evidence="ECO:0000269|PubMed:28148651"
FT MUTAGEN 2264
FT /note="R->A: Impairs intramolecular interaction with the
FT CCR domain, leading to a hyperactive kinase mutant."
FT /evidence="ECO:0000269|PubMed:28148651"
FT CONFLICT 2275
FT /note="R -> W (in Ref. 2; BAA09258)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2278 AA; 257420 MW; 1A0A30E13165DE41 CRC64;
MSSEEPHASI SFPDGSHVRS SSTGTSSVNT IDATLSRPNY IKKPSLHIMS TSTTSTTTDL
VTNPILSNIS VPKISPPTSS SIATATSTSH VTGTASHSNI KANANTSTSV NKKNLPPTTS
GRIPSSTIKR YPSRYKPSHS LQLPIKNDSN FKRSSIYASK STVTAIPIRN NRPISMQNSY
ARTPDSDHDD VGDEVSSIKS ASSSLTASLS KSFLFAFYNN RKKDKTSNNG VLSKEYWMKD
ESSKECFSCG KTFNTFRRKH HCRICGQIFC SSCTLLIDGD RFGCHAKMRV CYNCYEHADT
YEDSSDEEND STMQLNEPRS RSRSRSSNTN PYSHSHSHLH LISQDNHNGT DLHDPVAATD
NPQQQNEVYL LNDDDVQSIM TSGEDSKLFI STPPPPPKMA IPATKQGGSL EISFDSENDR
ALHYQDDNPG RHHHLDSVPT RYTIRDMDNI SHYDTNSNST LRPHYNTNNS TITINNLNNT
TSNNSNYNNT NSNSNINNPA HSLRRSIFHY VSSNSVNKDS NNSSATPASS AQSSSILDPA
NRIIGNYAHR NYKFKFNYNS KGPSQQNDTA NGNNDNNNNN NNNNNNNNNN SASGIADNNN
IPSNDNGTTF TLDKKKRNPL TKSKSTSAYL EYPLNEEDSS EDEGSMSIYS VLNDDHKTDN
PIRSMRNSTK SFQRAQASLQ RMRFRRKSKS KHFPNNSKSS IYRDLNFLTN STPNLLSVVS
DDNLYDDSSP LQDKASSSAA SRLTDRKFSN SSGSNNNSNS NSNINTDPWK RIASISGFKL
KKEKKRELNE VSLLHMHALL KQLLNDQEIS NLQEWITLLD GALRKVLRTI LNARDLNTLD
FRQTYVKIKR ISGGSPQNSE YIDGVVFSKA LPSKTMPRHL KNPRILLIMF PLEYQKNNNH
FLSIESVFRQ EREYLDKLVS RLKSLHPDII YVGANVSGYA LELLNDSGIV VQFNMKPQVI
ERIAKLTEAD IAISVDKLAT NIKMGECETF EVKSYIYGNI SKTYTFLRGC NPELGGTILL
RGDSLENLRK IKQVSEFMVY AIFSLKLESS FFNDNFIQLS TDVYLKRAES KKLQVFEGYF
ADFLIKFNNR ILTVSPTVDF PIPFLLEKAR GLEKKLIERI NQYESESDLD RQTQLNMLQG
LESTITKKHL GNLIKFLHEM EIENLELEFQ KRSRQWEVSY SSSQNLLGTG SHQSITVLYS
MVSTKTATPC VGPQIVTIDY FWDSDISIGQ FIENVVGTAR YPCQQGCNGL YLDHYRSYVH
GSGKVDVLIE KFQTRLPKLK DIILTWSYCK KCGTSTPILQ ISEKTWNHSF GKYLEVMFWS
YKDSVTGIGK CPHDFTKDHV KYFGYNDLVV RLEYSDLEVH ELITPPRKIK WKPHIDIKLK
VELYYKILEK INNFYGSVLS RLERIKLDSM TKDKVLSGQA KIIELKSNAT EEQKLMLQDL
DTFYADSPCD QHLPLNLVIK SLYDKAVNWN STFAIFAKSY LPSETDISRI TAKQLKKLFY
DSSRKDSEDK KSLHDEKAKT RKPEKNELPL EGLKDVEKPK IDSKNTTENR DRTNEPQNAV
TITTFKDDTP IIPTSGTSHL TVTPSASSVS SSLTPQTEER PPISRSGTGI SMTHDKSTRP
NIRKMSSDSS LCGLASLANE YSKNNKVSKL ATFFDQMHFD ALSKEFELER ERERLQLNKD
KYQAIRLQTS TPIVEIYKNV KDAVDEPLHS RSSGNNLSSA NVKTLEAPVG EHSRANNCNP
PNLDQNLETE LENSISQWGE NILNPSGKTT ASTHLNSKPV VKETSENPKS IVRESDNSKS
EPLPPVITTT TVNKVESTPQ PEKSLLMKTL SNFWADRSAY LWKPLVYPTC PSEHIFTDSD
VIIREDEPSS LIAFCLSTSD YRNKMMNLNV QQQQQQQTAE AAPAKTGGNS GGTTQTGDPS
VNISPSVSTT SHNKGRDSEI SSLVTTKEGL LNTPPIEGAR DRTPQESQTH SQANLDTLQE
LEKIMTKKTA THLRYQFEEG LTVMSCKIFF TEHFDVFRKI CDCQENFIQS LSRCVKWDSN
GGKSGSGFLK TLDDRFIIKE LSHAELEAFI KFAPSYFEYM AQAMFHDLPT TLAKVFGFYQ
IQVKSSISSS KSYKMDVIIM ENLFYEKKTT RIFDLKGSMR NRHVEQTGKA NEVLLDENMV
EYIYESPIHV REYDKKLLRA SVWNDTLFLA KMNVMDYSLV IGIDNEGYTL TVGIIDFIRT
FTWDKKLESW VKEKGLVGGA SVIKQPTVVT PRQYKKRFRE AMERYILMVP DPWYREGN
//
