SAC3_ARATH
ID SAC3_ARATH Reviewed; 818 AA.
AC Q7XZU2; Q8LPQ2; Q9LXL2;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Phosphoinositide phosphatase SAC3;
DE Short=AtSAC3;
DE EC=3.1.3.-;
DE AltName: Full=Phosphatidylinositol 3,5-bisphosphate 5-phosphatase SAC3;
DE AltName: Full=Protein SUPPRESSOR OF ACTIN 3;
DE AltName: Full=SAC domain protein 3;
GN Name=SAC3; OrderedLocusNames=At3g43220; ORFNames=F7K15_70;
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 [MRNA], GENE FAMILY, DOMAIN, AND TISSUE SPECIFICITY.
RX PubMed=12805586; DOI=10.1104/pp.103.021444;
RA Zhong R., Ye Z.-H.;
RT "The SAC domain-containing protein gene family in Arabidopsis.";
RL Plant Physiol. 132:544-555(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
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 {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3-phosphate) + phosphate; Xref=Rhea:RHEA:32955,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57923,
CC ChEBI:CHEBI:58088;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; 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: Vacuole membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q7XZU2-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous with a higher level of expression in
CC young seedlings than in other tissues. {ECO:0000269|PubMed:12805586}.
CC -!- DOMAIN: The phosphatase catalytic core motif (or RXNCXDCLDRTN motif)
CC from the SAC domain is found in metal-independent protein phosphatases
CC and inositol polyphosphate phosphatases. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM19844.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB89043.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY227246; AAP49836.1; -; mRNA.
DR EMBL; AL353871; CAB89043.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77775.1; -; Genomic_DNA.
DR EMBL; AY094477; AAM19844.1; ALT_FRAME; mRNA.
DR PIR; T49236; T49236.
DR RefSeq; NP_189908.2; NM_114190.3. [Q7XZU2-1]
DR AlphaFoldDB; Q7XZU2; -.
DR SMR; Q7XZU2; -.
DR STRING; 3702.AT3G43220.1; -.
DR iPTMnet; Q7XZU2; -.
DR PaxDb; Q7XZU2; -.
DR PRIDE; Q7XZU2; -.
DR ProteomicsDB; 232726; -. [Q7XZU2-1]
DR EnsemblPlants; AT3G43220.1; AT3G43220.1; AT3G43220. [Q7XZU2-1]
DR GeneID; 823397; -.
DR Gramene; AT3G43220.1; AT3G43220.1; AT3G43220. [Q7XZU2-1]
DR KEGG; ath:AT3G43220; -.
DR Araport; AT3G43220; -.
DR TAIR; locus:2084711; AT3G43220.
DR eggNOG; KOG1888; Eukaryota.
DR InParanoid; Q7XZU2; -.
DR OrthoDB; 359616at2759; -.
DR PhylomeDB; Q7XZU2; -.
DR BioCyc; ARA:AT3G43220-MON; -.
DR PRO; PR:Q7XZU2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q7XZU2; baseline and differential.
DR Genevisible; Q7XZU2; AT.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043813; F:phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity; IBA:GO_Central.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR InterPro; IPR043573; Fig4-like.
DR InterPro; IPR002013; SAC_dom.
DR PANTHER; PTHR45738; PTHR45738; 1.
DR Pfam; PF02383; Syja_N; 1.
DR PROSITE; PS50275; SAC; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Membrane; Reference proteome; Vacuole.
FT CHAIN 1..818
FT /note="Phosphoinositide phosphatase SAC3"
FT /id="PRO_0000421969"
FT DOMAIN 153..546
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT REGION 426..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 482..493
FT /note="Phosphatase catalytic core"
FT COMPBIAS 439..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 818 AA; 92747 MW; 8E2A79CAB5D4E82B CRC64;
MSSSTDDAGT TTHSLQEFKL FETQSNFYMI GWDGSGVYRV LKIDRLDPSE LNISQDSTHY
TKKECYELLK RIHEGNKATG GLKLVTLCYG IIGFVKFLGP YYMLLITERR HIGDLFGHSV
YAVSKSEIVA LHNSTVQCNF ANSRDENRYK RLLCMVDLTK DFFFSYSYNV MRSYQKNVCN
YETGHNLYEK MFVWNEFLTR GIRHHLRNTL WTVALVYGFF KQASLSESGK DFKITLIARR
SRHNAGTRYL KRGVNRNGDV ANDVETEQIV SEDVPEDHPM QISSVVQNRG SIPLFWSQET
SRLNLKPDIV LSKKEPNYEA TRLHFDNLVE RYGNPIIILN LIKTKERRPR ESILREEFVN
AIDFINKDLP EENRLRFLHW DLHKHFRSKT KNVLALLCKV ATCALMLTDL FYYQVTPAMT
IEDSMSLSSS SDADTGDISP HTSSDDDNGD HDSLEKKSSR SKNIAYGKCD VKPPRLQSGV
LRTNCIDCLD RTNVAQYAYG WAALGQQLHV LGIRDVPAIE LDDPLAISLM GLYERMGDTL
AHQYGGSAAH NKVFSERRGQ WRAATQSQEF LRTLQRYYNN AYMDADKQDA INIFLGTFQP
EQGMPAIWEL RSNSLSNGRN GEMNIGKDER FLVKRCLSDG DFLHESCTPL SAMSSNHESM
PQKGFSAPLQ HVSHILSESS SDIPVSNDVA LSRCTPSMPR KQLFGDVQKV HRFGSDQVYF
GGEEDMSSVS NFVDIEWLSS ENPCENALFD RSSELTRNLT AETSSTENSV NGVGQSAPTI
SESGSSSSKG KEPMGTKIRE DFPDSFKEWV AYGEALCH
