FAB1D_ARATH
ID FAB1D_ARATH Reviewed; 1456 AA.
AC Q9XID0;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Putative 1-phosphatidylinositol-3-phosphate 5-kinase FAB1D;
DE Short=Phosphatidylinositol 3-phosphate 5-kinase;
DE EC=2.7.1.150;
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 1D;
GN Name=FAB1D; OrderedLocusNames=At1g34260; ORFNames=F23M19.8;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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).
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). {ECO:0000250}.
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 -!- CAUTION: Lacks the FYVE domain, necessary to efficiently target the
CC protein to membranes containing the phosphatidylinositol-3P substrate.
CC Therefore, its molecular function remains unknown. {ECO:0000305}.
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DR EMBL; AC007454; AAD39608.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31690.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59572.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59574.1; -; Genomic_DNA.
DR PIR; G86466; G86466.
DR RefSeq; NP_001319143.1; NM_001333092.1.
DR RefSeq; NP_001321920.1; NM_001333093.1.
DR RefSeq; NP_174686.1; NM_103148.4.
DR AlphaFoldDB; Q9XID0; -.
DR SMR; Q9XID0; -.
DR STRING; 3702.AT1G34260.1; -.
DR iPTMnet; Q9XID0; -.
DR PaxDb; Q9XID0; -.
DR PRIDE; Q9XID0; -.
DR ProteomicsDB; 222361; -.
DR EnsemblPlants; AT1G34260.1; AT1G34260.1; AT1G34260.
DR EnsemblPlants; AT1G34260.2; AT1G34260.2; AT1G34260.
DR EnsemblPlants; AT1G34260.3; AT1G34260.3; AT1G34260.
DR GeneID; 840326; -.
DR Gramene; AT1G34260.1; AT1G34260.1; AT1G34260.
DR Gramene; AT1G34260.2; AT1G34260.2; AT1G34260.
DR Gramene; AT1G34260.3; AT1G34260.3; AT1G34260.
DR KEGG; ath:AT1G34260; -.
DR Araport; AT1G34260; -.
DR TAIR; locus:2026109; AT1G34260.
DR eggNOG; KOG0230; Eukaryota.
DR HOGENOM; CLU_000480_4_0_1; -.
DR InParanoid; Q9XID0; -.
DR OMA; KKVMGDN; -.
DR OrthoDB; 227882at2759; -.
DR PhylomeDB; Q9XID0; -.
DR BioCyc; ARA:AT1G34260-MON; -.
DR PRO; PR:Q9XID0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XID0; baseline and differential.
DR Genevisible; Q9XID0; AT.
DR GO; GO:0010008; C:endosome membrane; IBA:GO_Central.
DR GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd17300; PIPKc_PIKfyve; 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 Pfam; PF00118; Cpn60_TCP1; 1.
DR Pfam; PF01504; PIP5K; 1.
DR SMART; SM00330; PIPKc; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR PROSITE; PS51455; PIPK; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..1456
FT /note="Putative 1-phosphatidylinositol-3-phosphate 5-kinase
FT FAB1D"
FT /id="PRO_0000421873"
FT DOMAIN 1115..1443
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..110
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1456 AA; 164759 MW; 39812D36D423A908 CRC64;
MTPSNSLSSS ERSLSGECSV DGNSCDRGIE DECSSHSSQE DVELTKEVKV DRLERKSKSM
PSDILDILDE KSKENSVENV QFLSDREDDS DDVPVWEPPE PENPEDEVDG VFADDDDDCC
DGSKWNKASL LGELSDESSE KRKVYEENRR VMLEEADSKF KFIVSQLIKS AGFSIEESGY
WFEIVARLCW EAASMLKPAI DGKSVDPTEY IKVKCIATGS CVDSEVFKGL VFKKHAALKH
MATKYEHPRI MLVEGVLGHP ISGFSSLQSV NQDNEYLLKY VKPVVDIIEA SKPDVMLVEK
SVSRDIQKTI LDKGVTLVFD MKLHRLQRIS RCIGSPILSV DSLSSQKLKH CDSFRIEKIV
EEHNAAGESD KKPTKTLMFL EGCPTRLGCT ILLKGCHSER LKKVKEVVQY SFILAYHLML
EASFLADRHT MFSTIFAKEA TSCVVEIENF SPSPSPRESP SEAVDIPVSN GFDEQTIQIN
GEADGEKVGT WESDGDHVFS HEPYNPVIFT GFSSLSARLS KYLGFVQNPE SVPVSVDTDV
STTSNLDSIR ESEEDTAEKN EDKQPLLLDP ELPVNSSSDD GDNKSQTEND IESTLESQSI
LVLVSKRNAL RGIMCDQRHF SHIKFYKHFD VPLEKFLRDM FNQRNLCQTC VEFPEAHLYY
YAHQNKQLTI QIKRIPVAKG LAGEAKGKIW MWSRCGKCKT KNASRKSTKR VLISTAARSL
SFGKFLELSF SQQTFLNRSS SCGHSFDSDF LHFFGLGSMV AMLSYSQVAS YTVSLPPMKL
ESSILIKAGW LEKEFQTVFT KGISLFEDAA GFLKRLRSQF TNSDLRYQRA RKLLSNIEEL
LKHERCIFEE NIKNSFDKAK TIDDVSHRLL RLNRMRWELL LQALIWNYRL QSLVLSDRLL
PSSDETKIYE QGLKTVSEAG MTRYENDNKV SDSGSNGGID TPLVEHKDIP IAGASVGDND
QMAESYVPED NESQTLCSSS PDTTSPINNH FDTHLAVNVH STNGQEADKS IPVTGESLDD
EVSTSNGPHI LGWDEWFWLP FEELRSKRIV DIEKEYLLKF EYVNNFTQEN LQTVNQIITE
ESSRLRISLR DDDFIVSDYE DELSSLIACA LAHLNNEESK KPLSRCIHGS LQGFLDNNQD
SKQTDRDVSR FSSESTNRLE TLPPPEVLVT FGSVKSVGKP KYSIVSLYAD DFRDLRKRCC
SSELDYIASL SRCKPWDAKG GKSKSVFAKT LDDRFIVKEI KKTEYESFVT FATEYFKYMK
DSYDLGNQTC LAKVLGIHQV TVRQPKGGGK EIRHDLMVME NLSFSRKVTR QYDLKGALHA
RFTATSANGE DDVLLDQNFV NDMNKSPLYV SKTSKQNLQR AVYNDTSFLT SINVMDYSLL
VGVDDENHEL VCGIIDYLRQ YTWDKQLETW VKSSLVVPKN VQPTVISPID YKTRFRKFMK
THFLCVPDQW CDQGDS
