SAC1_ARATH
ID SAC1_ARATH Reviewed; 912 AA.
AC Q7XZU3; O80557; Q9SKA4;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Phosphatidylinositol-3-phosphatase SAC1;
DE Short=AtSAC1;
DE EC=3.1.3.64 {ECO:0000250|UniProtKB:P32368};
DE AltName: Full=Factor-induced gene 4-like protein;
DE Short=AtFIG4;
DE AltName: Full=Phosphatidylinositol 3,5-bisphosphate 5-phosphatase SAC1 {ECO:0000303|PubMed:15805481};
DE AltName: Full=Phosphatidylinositol-4-phosphate phosphatase {ECO:0000250|UniProtKB:P32368};
DE AltName: Full=Protein FRAGILE FIBER 7;
DE AltName: Full=Protein SUPPRESSOR OF ACTIN 1;
DE AltName: Full=SAC domain protein 1;
GN Name=SAC1; Synonyms=FIG4, FRA7; OrderedLocusNames=At1g22620;
GN ORFNames=F12K8.3, T22J18.20;
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Despres B., Delseny M., Devic M.;
RT "Cloning of AtFIG4 an Arabidopsis gene similar to the yeast FIG4 gene.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=15805481; DOI=10.1105/tpc.105.031377;
RA Zhong R., Burk D.H., Nairn C.J., Wood-Jones A., Morrison W.H. III, Ye Z.H.;
RT "Mutation of SAC1, an Arabidopsis SAC domain phosphoinositide phosphatase,
RT causes alterations in cell morphogenesis, cell wall synthesis, and actin
RT organization.";
RL Plant Cell 17:1449-1466(2005).
CC -!- FUNCTION: Phosphoinositide phosphatase which catalyzes the hydrolysis
CC of phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2)
CC (PubMed:15805481). Can also catalyze the hydrolysis of
CC phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol
CC 4-phosphate (PtdIns(4)P) (By similarity). Required for normal cell
CC morphogenesis, cell wall synthesis, and actin organization
CC (PubMed:15805481). {ECO:0000250|UniProtKB:P32368,
CC ECO:0000269|PubMed:15805481}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64;
CC Evidence={ECO:0000250|UniProtKB:P32368};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12317;
CC Evidence={ECO:0000250|UniProtKB:P32368};
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; Evidence={ECO:0000269|PubMed:15805481};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-
CC phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:55652, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58178;
CC Evidence={ECO:0000250|UniProtKB:P32368};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55653;
CC Evidence={ECO:0000250|UniProtKB:P32368};
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}. Golgi apparatus
CC {ECO:0000269|PubMed:15805481}.
CC -!- TISSUE SPECIFICITY: Ubiquitous with higher expression level in both
CC young elongating and nonelongating stems. Detected in vascular tissues.
CC {ECO:0000269|PubMed:12805586, ECO:0000269|PubMed:15805481}.
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:0000269|PubMed:12805586,
CC ECO:0000269|PubMed:15805481}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC25523.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF18517.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY227244; AAP49834.1; -; mRNA.
DR EMBL; AF266460; AAQ13339.1; -; mRNA.
DR EMBL; AC003979; AAC25523.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC006551; AAF18517.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30261.1; -; Genomic_DNA.
DR PIR; T00781; T00781.
DR RefSeq; NP_173676.2; NM_102109.4.
DR AlphaFoldDB; Q7XZU3; -.
DR SMR; Q7XZU3; -.
DR STRING; 3702.AT1G22620.1; -.
DR iPTMnet; Q7XZU3; -.
DR PaxDb; Q7XZU3; -.
DR PRIDE; Q7XZU3; -.
DR ProMEX; Q7XZU3; -.
DR ProteomicsDB; 226683; -.
DR EnsemblPlants; AT1G22620.1; AT1G22620.1; AT1G22620.
DR GeneID; 838868; -.
DR Gramene; AT1G22620.1; AT1G22620.1; AT1G22620.
DR KEGG; ath:AT1G22620; -.
DR Araport; AT1G22620; -.
DR TAIR; locus:2009477; AT1G22620.
DR eggNOG; KOG1888; Eukaryota.
DR HOGENOM; CLU_003016_4_0_1; -.
DR InParanoid; Q7XZU3; -.
DR OMA; KRKCCAH; -.
DR PhylomeDB; Q7XZU3; -.
DR BioCyc; ARA:AT1G22620-MON; -.
DR PRO; PR:Q7XZU3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q7XZU3; baseline and differential.
DR Genevisible; Q7XZU3; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
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; IDA:UniProtKB.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:TAIR.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009832; P:plant-type cell wall biogenesis; IMP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
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 1: Evidence at protein level;
KW Golgi apparatus; Hydrolase; Membrane; Reference proteome; Vacuole.
FT CHAIN 1..912
FT /note="Phosphatidylinositol-3-phosphatase SAC1"
FT /id="PRO_0000421967"
FT DOMAIN 173..575
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..912
FT /note="Required for subcellular localization"
FT REGION 740..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 511..522
FT /note="Phosphatase catalytic core"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 912 AA; 102812 MW; 27789DDFA77C3786 CRC64;
MAKSENSTTS TFSSFANKIQ PSNDAESDPD SYALEKFKLY ETRARFYLVG SDRNKRFFRV
LKIDRSEPSE LNISEDPVVY SPQEIKSLLQ RIAEGNRATG GLAFVAKVYG IAGCAKFMES
YYLVLVTKRR QIGCICGHAI YAIDESQMIS VPHATIQSDV ANSKTELRYK KLLSSVDLTK
DFFYSYTYPI MQSLQKNVLS SGEEGMPYDN IFVWNSYLTQ PIRSRCNNTI WTLALVHGHF
KQIRLSIYGR DFSVTLVSRR SRHFAGTRYL KRGVNDRGRV ANDVETEQLV LDDEAGSCKG
KMSSVVQMRG SIPLFWSQEA SRFSPKPDIF LQRYDPTYES TKMHFEDLVN RYGNPIIVLN
LIKTVEKRPR EMVLRREFAN AVGYLNSIFR EENHLKFIHW DFHKFAKSKS ANVLAVLGAV
ASEALDLTGL YFSGKPKIVK KKASQLSHAN TAREPSLRDL RAYSAELSRG ESANDILSAL
ANREKEMKLT QQKKDEGTNS SAPRYQSGVL RTNCIDCLDR TNVAQYAYGL AALGRQLHAM
GLSDTPKIDP DSSIAAALMD MYQSMGDALA QQYGGSAAHN TVFPERQGKW KATTQSREFL
KSIKRYYSNT YTDGEKQDAI NLFLGYFQPQ EGKPALWELD SDYYLHVSGI GDDIFPDIGV
QSIAKPMSGI GVNLAPVPAF RDDFSRKKLT SFDKLIEQTC SSIKNVRLCS ETDQRPGGNT
GSTGVAPDAA EIQLKSPNWL FGSRKPEESS SATKSGADDS EKGVTSTERV NDFCNLDWLS
KSDRHQGDIF QRYLSITSTN EANGWYGGTL LGDQDENSEI YRHYAQFCQC PAMEPFENDH
EFEQNFAEVL RMNTIDVMDI EEEETEMESD FNEYTQIGSD LGIIPMQCKH FASDPCWLAR
WLVGDDKVPK VI
