SAC2_ARATH
ID SAC2_ARATH Reviewed; 808 AA.
AC Q94A27; Q9LJG4;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Phosphoinositide phosphatase SAC2;
DE Short=AtSAC2;
DE EC=3.1.3.-;
DE AltName: Full=Phosphatidylinositol 3,5-bisphosphate 5-phosphatase SAC2;
DE AltName: Full=Protein SUPPRESSOR OF ACTIN 2;
DE AltName: Full=SAC domain protein 2;
GN Name=SAC2; OrderedLocusNames=At3g14205; ORFNames=MAG2.20;
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 [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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 -!- 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=BAB02988.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY227245; AAP49835.1; -; mRNA.
DR EMBL; AP000600; BAB02988.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75486.1; -; Genomic_DNA.
DR EMBL; AY050432; AAK91448.1; -; mRNA.
DR EMBL; AY093999; AAM16260.1; -; mRNA.
DR RefSeq; NP_566481.1; NM_112277.4.
DR AlphaFoldDB; Q94A27; -.
DR SMR; Q94A27; -.
DR STRING; 3702.AT3G14205.1; -.
DR iPTMnet; Q94A27; -.
DR PaxDb; Q94A27; -.
DR PRIDE; Q94A27; -.
DR ProteomicsDB; 232865; -.
DR EnsemblPlants; AT3G14205.1; AT3G14205.1; AT3G14205.
DR GeneID; 820638; -.
DR Gramene; AT3G14205.1; AT3G14205.1; AT3G14205.
DR KEGG; ath:AT3G14205; -.
DR Araport; AT3G14205; -.
DR TAIR; locus:505006345; AT3G14205.
DR eggNOG; KOG1888; Eukaryota.
DR HOGENOM; CLU_003016_4_2_1; -.
DR InParanoid; Q94A27; -.
DR OMA; TRTYWRV; -.
DR OrthoDB; 359616at2759; -.
DR PhylomeDB; Q94A27; -.
DR BioCyc; ARA:AT3G14205-MON; -.
DR PRO; PR:Q94A27; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q94A27; baseline and differential.
DR Genevisible; Q94A27; 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 GO; GO:0007033; P:vacuole organization; IEA:InterPro.
DR InterPro; IPR043573; Fig4-like.
DR InterPro; IPR030213; SAC2_plant.
DR InterPro; IPR002013; SAC_dom.
DR PANTHER; PTHR45738; PTHR45738; 1.
DR PANTHER; PTHR45738:SF8; PTHR45738:SF8; 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..808
FT /note="Phosphoinositide phosphatase SAC2"
FT /id="PRO_0000421968"
FT DOMAIN 158..551
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT REGION 429..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 487..498
FT /note="Phosphatase catalytic core"
SQ SEQUENCE 808 AA; 91632 MW; 9221AF74C9F4D1E8 CRC64;
MAASERSIDK EVDMGSSFLQ KFRLYETRSS FYMIGRDKNR TSWRVLKLDR TEPAEVNIYE
DSTAYTEAEC FETLRRIHEG NRSSGGLKFV TTCYGIIGFI RFLGPYYMLI ITKRKKLGEI
CGHTVYGVAK SKIITIPHAS VLSNVAYSKD EKRYKRLLCT VDLTKDFFFS YSYHIMHTLQ
RNLSNNVEGH TYYESMFVWN EYLTRRIRNN VKDCMWTVAL VYGFFKQVKL SVSEKNFRLT
LISRRSRHYA GTRYLKRGVN EKGRVANDVE TEQIVFEEAQ DGNPGRISSV VQNRGSIPLF
WSQETSRLNI KPDIILSPKD PNFEATRLHF ENLGRRYGNP IIILNLIKTR EKRPRETILR
AEFANAIRFI NKGLSKEDRL RPLHWDLHKH SRKKGTNVLA ILGRLATYAL NLTSIFYCQL
TPDLRGEGFQ NQNPSTLEND DGECSTYDPP SKDETAPNLV VENGNDSKDA KEDQQKEVTM
LQKGVLRTNC IDCLDRTNVA QYAYGLVAFG RQLHALGLTE STNIDLDNPL AEDLMGIYET
MGDTLALQYG GSAAHNKIFC ERRGQWRAAT QSQEFFRTLQ RYYSNAYMDA EKQDAINVFL
GYFQPQSDKP ALWELGSDQH YNAARFLANS VPETSRSTMK RSLSESSIIS ESSPAALGPV
GRHGLAEKDE EVKGLSDSAP EISTSETAKI AASLSAPPPI LEELGLDDIL ENDCFCCDGN
GEQCTCAAFD MDWVSSSGNS CEDESCGRAT VVRSFETIPE SRKIESEICV VETVGSNSRK
GNKEEEEAIS GIPEGYVRWV MDEDGHFW
