SAC4_ARATH
ID SAC4_ARATH Reviewed; 831 AA.
AC Q7XZU1;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Phosphoinositide phosphatase SAC4;
DE Short=AtSAC4;
DE EC=3.1.3.-;
DE AltName: Full=Phosphatidylinositol 3,5-bisphosphate 5-phosphatase SAC4;
DE AltName: Full=Protein SUPPRESSOR OF ACTIN 4;
DE AltName: Full=SAC domain protein 4;
GN Name=SAC4; OrderedLocusNames=At5g20840; ORFNames=F22D1.10;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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).
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 -!- 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}.
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DR EMBL; AY227247; AAP49837.1; -; mRNA.
DR EMBL; AF296834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92896.1; -; Genomic_DNA.
DR RefSeq; NP_197584.2; NM_122091.3.
DR AlphaFoldDB; Q7XZU1; -.
DR SMR; Q7XZU1; -.
DR STRING; 3702.AT5G20840.1; -.
DR iPTMnet; Q7XZU1; -.
DR PaxDb; Q7XZU1; -.
DR PRIDE; Q7XZU1; -.
DR ProteomicsDB; 226641; -.
DR EnsemblPlants; AT5G20840.1; AT5G20840.1; AT5G20840.
DR GeneID; 832207; -.
DR Gramene; AT5G20840.1; AT5G20840.1; AT5G20840.
DR KEGG; ath:AT5G20840; -.
DR Araport; AT5G20840; -.
DR TAIR; locus:2147082; AT5G20840.
DR eggNOG; KOG1888; Eukaryota.
DR HOGENOM; CLU_003016_4_2_1; -.
DR InParanoid; Q7XZU1; -.
DR OMA; TNERKPR; -.
DR OrthoDB; 359616at2759; -.
DR PhylomeDB; Q7XZU1; -.
DR BioCyc; ARA:AT5G20840-MON; -.
DR PRO; PR:Q7XZU1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q7XZU1; baseline and differential.
DR Genevisible; Q7XZU1; AT.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
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 Hydrolase; Membrane; Reference proteome; Vacuole.
FT CHAIN 1..831
FT /note="Phosphoinositide phosphatase SAC4"
FT /id="PRO_0000421970"
FT DOMAIN 162..551
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT REGION 439..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 487..498
FT /note="Phosphatase catalytic core"
FT COMPBIAS 445..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 94047 MW; 67D1BD578EEDBBD3 CRC64;
MTSSPSVENG GSGSSGSSAL LGCMQQFKLF ETQANFYMIG WNGSGVYRIL KIDRLEASEL
NLREDSTAYT KKECYELLKR IHEGNKATGG LKLVTVCYGI IGFIKFLGPY YMLLITERRE
IGEICGHIVY EVSKSDMIAL QHSSVLCNTA NLRDENRYKR LLCMVDLTKD FFFSYSYNIM
RSFQKNICDH ESGGTLYKKM FVWNEFLTRG TRHHLRNTLW TVALVYGFFK QTILSEAGRN
FKLTLIARRS RHNAGTRYLK RGINESGNVA NDVETEQIVS EDVPVDRPMQ ISSVVQNRGS
IPLFWSQETS RMKVKPDIVL SKRDLNYEAT RVHFENLVER YGVPIIILNL IKTNERKPRE
SILRAEFANA IDFINKDLPE ENRLRFLHWD LHKHFHSKTE NVLALLGKVA ACALMLTGFF
YYQLTPAMKL EGYMSLSSSD ADTSPHNSSD DDSRDYDSLE KNCRPSKNVA NGDYDVKPSR
LQSGVLRTNC IDCLDRTNVA QYAYGWAALG QQLHALGIRD APTIELDDPL SSTLMGLYER
MGDTLAYQYG GSAAHNKVFS ERRGQWRAAT QSQEFLRTLQ RYYNNAYMDA DKQDAINIFL
GTFRPEQGSQ AVWELRSDSH SNGRSGEISM GEDEKFLVKR CLSDGNILHE SHTPMSAMSR
KNESISHRGF VSSHQVTRTH IISESSPDMP AAGDVTLSRC TPSMPSTHFF GDVQKVQHNG
SSSIYLSEQE DMSSVSNFVD IEWLSSSENL CENDHLSRPS ALTIYSTAET SSSENIITEV
KQLTPAMRES GSSSRKGKEP VETELSVHTK IRDDFPDSFK QWVAYGEALC H
