FAB1B_ARATH
ID FAB1B_ARATH Reviewed; 1791 AA.
AC Q9LUM0; Q0WPY8;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=1-phosphatidylinositol-3-phosphate 5-kinase FAB1B;
DE Short=Phosphatidylinositol 3-phosphate 5-kinase;
DE EC=2.7.1.150;
DE AltName: Full=FYVE finger-containing phosphoinositide kinase;
DE AltName: Full=PIKfyve;
DE AltName: Full=Phosphatidylinositol 3-phosphate 5-kinase type III;
DE Short=PIPkin-III;
DE Short=Type III PIP kinase;
DE AltName: Full=Protein FORMS APLOID AND BINUCLEATE CELLS 1B;
GN Name=FAB1B; OrderedLocusNames=At3g14270; ORFNames=MLN21.6;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-845.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY, AND REVIEW.
RX PubMed=12226484; DOI=10.1104/pp.004770;
RA Mueller-Roeber B., Pical C.;
RT "Inositol phospholipid metabolism in Arabidopsis. Characterized and
RT putative isoforms of inositol phospholipid kinase and phosphoinositide-
RT specific phospholipase C.";
RL Plant Physiol. 130:22-46(2002).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=19846542; DOI=10.1104/pp.109.146159;
RA Whitley P., Hinz S., Doughty J.;
RT "Arabidopsis FAB1/PIKfyve proteins are essential for development of viable
RT pollen.";
RL Plant Physiol. 151:1812-1822(2009).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=21173023; DOI=10.1104/pp.110.167981;
RA Hirano T., Matsuzawa T., Takegawa K., Sato M.H.;
RT "Loss-of-function and gain-of-function mutations in FAB1A/B impair
RT endomembrane homeostasis, conferring pleiotropic developmental
RT abnormalities in Arabidopsis.";
RL Plant Physiol. 155:797-807(2011).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21412048; DOI=10.4161/psb.6.4.15023;
RA Hirano T., Sato M.H.;
RT "Arabidopsis FAB1A/B is possibly involved in the recycling of auxin
RT transporters.";
RL Plant Signal. Behav. 6:583-585(2011).
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 (By similarity). Plays an
CC important role in maintenance of endomembrane homeostasis including
CC endocytosis, vacuole formation, and vacuolar acidification processes.
CC Required for development of viable pollen. Might mediate recycling of
CC auxin transporters. {ECO:0000250, ECO:0000269|PubMed:19846542,
CC ECO:0000269|PubMed:21173023, ECO:0000269|PubMed:21412048}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Component of the PI(3,5)P2 regulatory complex at least
CC composed of ATG18, SAC/FIG4, FAB1 and VAC14. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:21173023};
CC Peripheral membrane protein {ECO:0000269|PubMed:21173023}.
CC -!- TISSUE SPECIFICITY: Ubiquitous with highest expression levels in the
CC root hair zone, pollen, and stamens. {ECO:0000269|PubMed:19846542}.
CC -!- DISRUPTION PHENOTYPE: Leaf-curling phenotype. Root growth inhibition,
CC root gravitropic response, and hyposensitivity to exogenous auxin.
CC Fab1a and fab1b double mutant displays an abnormal vacuolar phenotype
CC late in pollen development leading to inviable pollen
CC (PubMed:19846542). {ECO:0000269|PubMed:19846542,
CC ECO:0000269|PubMed:21173023, ECO:0000269|PubMed:21412048}.
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DR EMBL; AB022220; BAB01033.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75496.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65157.1; -; Genomic_DNA.
DR EMBL; AK228922; BAF00811.1; -; mRNA.
DR RefSeq; NP_001319548.1; NM_001338116.1.
DR RefSeq; NP_188044.1; NM_112285.4.
DR AlphaFoldDB; Q9LUM0; -.
DR SMR; Q9LUM0; -.
DR STRING; 3702.AT3G14270.1; -.
DR iPTMnet; Q9LUM0; -.
DR PaxDb; Q9LUM0; -.
DR PRIDE; Q9LUM0; -.
DR ProteomicsDB; 230632; -.
DR EnsemblPlants; AT3G14270.1; AT3G14270.1; AT3G14270.
DR EnsemblPlants; AT3G14270.2; AT3G14270.2; AT3G14270.
DR GeneID; 820647; -.
DR Gramene; AT3G14270.1; AT3G14270.1; AT3G14270.
DR Gramene; AT3G14270.2; AT3G14270.2; AT3G14270.
DR KEGG; ath:AT3G14270; -.
DR Araport; AT3G14270; -.
DR TAIR; locus:2091050; AT3G14270.
DR eggNOG; KOG0230; Eukaryota.
DR HOGENOM; CLU_000480_4_0_1; -.
DR InParanoid; Q9LUM0; -.
DR OMA; SNHRWSE; -.
DR OrthoDB; 227882at2759; -.
DR PhylomeDB; Q9LUM0; -.
DR BioCyc; ARA:AT3G14270-MON; -.
DR BRENDA; 2.7.1.150; 399.
DR PRO; PR:Q9LUM0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUM0; baseline and differential.
DR Genevisible; Q9LUM0; AT.
DR GO; GO:0005768; C:endosome; IDA:TAIR.
DR GO; GO:0010008; C:endosome membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IGI:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010256; P:endomembrane system organization; IGI:TAIR.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009555; P:pollen development; IGI:TAIR.
DR GO; GO:0090332; P:stomatal closure; IMP:TAIR.
DR GO; GO:0007033; P:vacuole organization; IGI:TAIR.
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; 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; 2.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00330; PIPKc; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51455; PIPK; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Endosome; Kinase; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1791
FT /note="1-phosphatidylinositol-3-phosphate 5-kinase FAB1B"
FT /id="PRO_0000421871"
FT DOMAIN 1433..1758
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT ZN_FING 39..105
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 166..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1769..1791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1077..1111
FT /evidence="ECO:0000255"
FT COMPBIAS 279..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..345
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1212..1226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ SEQUENCE 1791 AA; 200831 MW; 859835D68E56039F CRC64;
MGTRDSNNRT FSEIVGLIKS WLPWRSEPAT VSRDFWMPDQ SCRVCYECDC QFTLINRRHH
CRHCGRVFCG KCTANSIPFA PSDLRTPRED WERIRVCNYC FRQWEQGDGG PHVSNITELS
TSPSETSLLS SKTSTTANSS SFALGSMPGL IGLNQRVHHG SDVSLHGVSS METSVTKQGK
ETSRRSSFIA TDVEDPSRFA LNSIRSDDEY DEYGAYQTDI ETSHSPRANE YYGPMEYNGM
GIDDVPCKHL GGETADQKSL SGSPLIHQCL ESLIREGSEQ FQKKSEHDGR DECEASSPAD
ISDDQVVEPV DFENNGLLWV PPEPENEEDE RESALFDEED NEGDASGEWG YLRPSTSFGS
GEYRGEDRTT EEHKKAMKNV VDGHFRALLA QLLQVENISV SDEEGKESWL EIITSLSWEA
ANLLKPDMSK SGGMDPGGYV KVKCLASGFR HDSMVVKGVV CKKNVVNRRM STKIEKARLL
ILGGGLEYQR VSNQLSSFDT LLQQEKDHLK MAVAKIHAER PNILLVEKSV SRFAQEYLLA
KDISLVLNIK RPLLDRIARC TGAQIIPSVD HLSSQKLGYC ENFRVDRYPE EHGSTGQVGK
KVVKTLMYFE HCPKPLGFTI LLRGANEDEL KKVKHVVQYG VFAAYHLALE TSFLADEGAS
PELPLNSPIT VALPDKSTSI ERSISTVPGF TVSTYEKSPT MLSCAEPQRA NSVPVSELLS
TTTNLSIQKD IPPIPYGSGW QAREINPSFV FSRHNISLNL PDRVIESRNS DLSGRSVPVD
TPADKSNPIV VADETTNNSL HLSGQGFVRK SSQIGTSIMV ENQDNGSELT IAQQQNNEKP
KETQSQKEEF PPSPSDHQSI LVSLSSRSVW KGTVCERSHL FRIKYYGSFD KPLGRFLRDH
LFDQSYRCRS CEMPSEAHVH CYTHRQGSLT ISVKKLQDYL LPGEKEGKIW MWHRCLRCPR
LNGFPPATLR VVMSDAAWGL SFGKFLELSF SNHAAASRVA CCGHSLHRDC LRFYGFGNMV
ACFRYATIDV HSVYLPPSIL SFNYENQDWI QRETDEVIER AELLFSEVLN AISQIAEKGF
RRRIGELEEV LQKEKAEFEE NMQKILHREV NEGQPLVDIL ELYRIHRQLL FQSYMWDHRL
INASTLHKLE NSDDTKREEN EKPPLAKSQT LPEMNAGTNS LLTGSEVNLN PDGDSTGDTG
SLNNVQKEAD TNSDLYQEKD DGGEVSPSKT LPDTSYPLEN KVDVRRTQSD GQIVMKNLSA
TLDAAWIGER QTSVEIPTNN KVSLPPSTMS NSSTFPPISE GLMPIDLPEQ QNEFKVAYPV
SPALPSKNYE NSEDSVSWLS VPFLNFYRSI NKNFLLSSQK LDTFGEHSPI YISSFREAEL
QGGPRLLLPV GLNDIVVPVY DDEPTSMIAY ALMSPEYQRQ TSAEGESLVS YPSELNIPRP
VDDTIFDPSR SNGSVDESIL SISSSRSTSL LDPLSYTKAL HARVSYGEDG TLGKVKYTVT
CYYAKRFEAL RGICLPSELE YIRSLSRCKK WGAQGGKSNV FFAKTLDDRF IIKQVTKTEL
ESFIKFAPAY FKYLSESIST KSPTCLAKIL GIYQVATKQL KSGKETKMDV LIMENLLFGR
TVKRLYDLKG SSRARYNPDS SGSNKVLLDQ NLIEAMPTSP IFVGNKAKRL LERAVWNDTA
FLALGDVMDY SLLVGVDEEK NELVLGIIDF LRQYTWDKHL ESWVKFTGIL GGPKNEAPTV
ISPKQYKRRF RKAMTTYFLM VPDQWSPPNV VANNSKSDQP EETSQAGTQA E
