FAB1C_ARATH
ID FAB1C_ARATH Reviewed; 1648 AA.
AC Q9SSJ8; Q8VZ86;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Putative 1-phosphatidylinositol-3-phosphate 5-kinase FAB1C;
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 1C;
GN Name=FAB1C; OrderedLocusNames=At1g71010; ORFNames=F15H11.20;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 736-1648.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL38344.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC008148; AAD55502.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35150.1; -; Genomic_DNA.
DR EMBL; AY065168; AAL38344.1; ALT_INIT; mRNA.
DR EMBL; BT010349; AAQ56792.1; -; mRNA.
DR RefSeq; NP_177257.3; NM_105770.6.
DR AlphaFoldDB; Q9SSJ8; -.
DR SMR; Q9SSJ8; -.
DR STRING; 3702.AT1G71010.1; -.
DR iPTMnet; Q9SSJ8; -.
DR PaxDb; Q9SSJ8; -.
DR PRIDE; Q9SSJ8; -.
DR ProteomicsDB; 230843; -.
DR EnsemblPlants; AT1G71010.1; AT1G71010.1; AT1G71010.
DR GeneID; 843440; -.
DR Gramene; AT1G71010.1; AT1G71010.1; AT1G71010.
DR KEGG; ath:AT1G71010; -.
DR Araport; AT1G71010; -.
DR TAIR; locus:2013965; AT1G71010.
DR eggNOG; KOG0230; Eukaryota.
DR HOGENOM; CLU_000480_4_0_1; -.
DR InParanoid; Q9SSJ8; -.
DR OMA; MERNGYE; -.
DR OrthoDB; 227882at2759; -.
DR PhylomeDB; Q9SSJ8; -.
DR BioCyc; ARA:AT1G71010-MON; -.
DR PRO; PR:Q9SSJ8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SSJ8; baseline and differential.
DR Genevisible; Q9SSJ8; AT.
DR GO; GO:0010008; C:endosome membrane; IBA:GO_Central.
DR GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IDA:TAIR.
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 GO; GO:0090332; P:stomatal closure; IMP:TAIR.
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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..1648
FT /note="Putative 1-phosphatidylinositol-3-phosphate 5-kinase
FT FAB1C"
FT /id="PRO_0000421872"
FT DOMAIN 1316..1639
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT REGION 97..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1648 AA; 185494 MW; B3410E494497299B CRC64;
MGIPDGSLLD LIDKVRSWIT SDSSDSLFLL SSSKQDFGIM PIVSKMCHDC GTKVEQGYCC
LSCGSCWCKS CSDTEESKMK LCRECDAEVR ELRVKSYDKV HPRDSPDPPS SLATESESLA
SSLEIRDCRN MASIRCYPSR GEEEEARYCG KQLLSPSSDN YQDSSDIESG SVSARHELFS
CKSSAGSSPH DSPLRNNFSP LGRFVQHAKD LRSPTVCSFD NHQEQLLADN LVKPGQGVLE
QEDHEEEEDK LQQPLDFENN GRIWYPPPPE DENDDAESNY FHYDDEDDDI GDSATEFSLS
SSFSSHIPTK EKLGENSNEP LRTVVHDHFR ALVAELLRGE ELSPSDDGSA GEWLDIVTAL
AWQAANFVKP DTRAGGSMDP GNYVKIKCVA SGNQNESILI RGIVCSKNIT HKRMISQYKN
PRVMLLAGSL EYQRVAGQLA SFNTLLQQEN EHMKAIIAKI ESLRPNVLLV EKSASSYAQQ
YLLEKEISLV LNVKRSLLDR IARCTGAVLC PSLDSISTAR LGHCELFRTE RVLEQHEAGN
QSNRKPSRTL MYFEGCPRRL GCTVVLRGSC REELKKVKHV IQYAVFAAYH LSLETSFLAD
EGASLPKIRL KQPGMVRTAS QRRIIDEGIS LITQSPTETD SQALLETAAH EDEHTAPMPE
HEVCESLCED FDPTQIFPPS SEVETEQSDT LNGDFANNLV TRSYSSNQLN DLHEPTLCLS
SEIPETPTQQ PSGEEDNGRG EEENQLVNPQ DLPQHESFYE DDVSSEYFSA ADSHQSILVS
FSSRCVLKES VCERSRLLRI KFYGSFDKPL GRYLKDDLFD KTSSCRSCKE LVDAHVLCYS
HQNGNLTINV RRLPSMKLPG EQDGKIWMWH RCLRCAHVDG VPPATRRVVM SDAAWGLSFG
KFLELSFSNH ATANRVASCG HSLQRDCLRF YGFGNMVAFF RYSPINILTV LLPPSMLEFN
SHPQQEWIRT EAAELVGKMR TMYTEISDML NRMEEKSSLL EPEQSEACDL HSRIIGLIDQ
LVKEKDEYDD ALQPIFEENL QIQGSLDILE LNRLRRALMI GAHAWDHQLY LLNSQLKKAS
VFKTGDDNAP RNPEMHDPPK IDRRMQEGSD ERDEQSHTDS EANGDNKDPE NIPSPGTSLS
ERIDSAWLGS FQNLEKAETI AETEGFSAVN SSLRRLARPI RVQSFDSAIR FQERIQKGLP
PSSLYLSTLR SFHASGEYRN MVRDPVSNVM RTYSQMLPLE VQKLDLIVGS APTYISSASQ
MADGARMLIP QRGLNDIVVP VYDDDPASVV SYAINSKEYK EWIVNKGLAS SSSSSNLNNR
ESEPSAFSTW RSLSMDVDYI QHAVYGSSQD DRKSPHLTIS FSDRASSSST ATEGKVKFSV
TCYFATQFDT LRKTCCPSEV DFVRSLSRCQ RWSAQGGKSN VYFAKSLDER FIIKQVVKTE
LDSFEDFAPE YFKYLKESLS SGSPTCLAKI LGIYQVSIKH PKGGKETKMD LMVMENLFYN
RRISRIYDLK GSARSRYNPN TSGADKVLLD MNLLETLRTE PIFLGSKAKR SLERAIWNDT
NFLASVDVMD YSLLVGFDEE RKELVLGIID FMRQYTWDKH LETWVKASGI LGGPKNASPT
IVSPKQYKRR FRKAMTTYFL TVPEPWTS
