ID   SAC9_ARATH              Reviewed;        1630 AA.
AC   Q7XZU0; Q0WUS3; Q9M1Z7;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Probable phosphoinositide phosphatase SAC9;
DE            Short=AtSAC9;
DE            EC=3.1.3.-;
DE   AltName: Full=Protein SUPPRESSOR OF ACTIN 9;
DE   AltName: Full=SAC domain protein 9;
GN   Name=SAC9; Synonyms=CFS; OrderedLocusNames=At3g59770; ORFNames=F24G16.40;
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;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=15923324; DOI=10.1104/pp.105.061317;
RA   Williams M.E., Torabinejad J., Cohick E., Parker K., Drake E.J.,
RA   Thompson J.E., Hortter M., Dewald D.B.;
RT   "Mutations in the Arabidopsis phosphoinositide phosphatase gene SAC9 lead
RT   to overaccumulation of PtdIns(4,5)P2 and constitutive expression of the
RT   stress-response pathway.";
RL   Plant Physiol. 138:686-700(2005).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=16453058; DOI=10.1007/s11120-006-9041-4;
RA   Gong P., Wu G., Ort D.R.;
RT   "Slow dark deactivation of Arabidopsis chloroplast ATP synthase caused by a
RT   mutation in a nonplastidic SAC domain protein.";
RL   Photosyn. Res. 88:133-142(2006).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [8]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=21698459; DOI=10.1007/s00425-011-1454-4;
RA   Vollmer A.H., Youssef N.N., DeWald D.B.;
RT   "Unique cell wall abnormalities in the putative phosphoinositide
RT   phosphatase mutant AtSAC9.";
RL   Planta 234:993-1005(2011).
CC   -!- FUNCTION: Probable phosphoinositide phosphatase that could be involved
CC       in stress signaling. {ECO:0000269|PubMed:15923324}.
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=Q7XZU0-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Most abundant in the roots with lower
CC       expression levels throughout the leaves and shoot.
CC       {ECO:0000269|PubMed:12805586, ECO:0000269|PubMed:15923324}.
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   -!- DISRUPTION PHENOTYPE: Characteristics of a constitutive stress
CC       response, including dwarfism, closed stomata, and accumulation of
CC       anthocyanin and reactive-oxygen species. Accumulates elevated levels of
CC       PtdIns(4,5)P(2) and Ins(1,4,5)P(3) in roots. Hypersensitivity to salt
CC       stress. Late flowering, shorter roots with less lateral branching and
CC       low fertility. Abnormalities of cell wall and membrane structures in
CC       primary root cells. {ECO:0000269|PubMed:15923324,
CC       ECO:0000269|PubMed:16453058, ECO:0000269|PubMed:21698459}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB75796.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY227252; AAP49842.1; -; mRNA.
DR   EMBL; AL138647; CAB75796.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE79965.1; -; Genomic_DNA.
DR   EMBL; AK227068; BAE99125.1; -; mRNA.
DR   PIR; T47801; T47801.
DR   RefSeq; NP_191536.2; NM_115839.4. [Q7XZU0-1]
DR   AlphaFoldDB; Q7XZU0; -.
DR   SMR; Q7XZU0; -.
DR   STRING; 3702.AT3G59770.3; -.
DR   iPTMnet; Q7XZU0; -.
DR   PaxDb; Q7XZU0; -.
DR   PRIDE; Q7XZU0; -.
DR   ProteomicsDB; 226642; -. [Q7XZU0-1]
DR   EnsemblPlants; AT3G59770.1; AT3G59770.1; AT3G59770. [Q7XZU0-1]
DR   GeneID; 825146; -.
DR   Gramene; AT3G59770.1; AT3G59770.1; AT3G59770. [Q7XZU0-1]
DR   KEGG; ath:AT3G59770; -.
DR   Araport; AT3G59770; -.
DR   eggNOG; KOG1888; Eukaryota.
DR   InParanoid; Q7XZU0; -.
DR   PhylomeDB; Q7XZU0; -.
DR   PRO; PR:Q7XZU0; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q7XZU0; baseline and differential.
DR   Genevisible; Q7XZU0; AT.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   CDD; cd00201; WW; 1.
DR   InterPro; IPR002013; SAC_dom.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   Pfam; PF02383; Syja_N; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF51045; SSF51045; 1.
DR   PROSITE; PS50275; SAC; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; Reference proteome.
FT   CHAIN           1..1630
FT                   /note="Probable phosphoinositide phosphatase SAC9"
FT                   /id="PRO_0000421975"
FT   DOMAIN          147..527
FT                   /note="SAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT   DOMAIN          508..542
FT                   /note="WW"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   MOTIF           456..467
FT                   /note="Phosphatase catalytic core; degenerate"
FT   CONFLICT        315
FT                   /note="R -> G (in Ref. 4; BAE99125)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1630 AA;  180063 MW;  9E1BA48B5760A120 CRC64;
     MDLHPPGGSK KTSVVVVTLD TGEVYVIASL LSKADTQVIY IDPTTGILRY NGKPGLDNFK
     SEREALDYIT NGSRGGVRSS VYARAILGYA VLGSFGMLLV ATRLNPSIPD LPGGGCVYTV
     AESQWVKIPL YNPQPQGKGE TKNIQELTEL DIDGKHYFCD TRDITRPFPS RMPLQSPDDE
     FVWNRWLSVP FKNIGLPEHC VILLQGFAEY RPFGSSGQLE GIVALMARRS RLHPGTRYLA
     RGINSCSGTG NEVECEQLVW IPKRNGQSIA FNSYIWRRGT IPIWWGAELK MTAAEAEIYV
     ADRDPYKGST EYYQRLSKRY DTRNLDAPVG ENQKKKAFVP IVCVNLLRSG EGKSECILVQ
     HFEESMNFIK SSGKLPYTRV HLINYDWHAS VKLKGEQQTI EGLWMYLKSP TMAIGISEGD
     YLPSRQRLKD CRGEVICIDD IEGAFCLRSH QNGVIRFNCA DSLDRTNAAS FFGGLQVFVE
     QCRRLGISLD TDLGYGHNSV NNQGGYNAPL PPGWEKRADA VTGKSYYIDH NTKTTTWSHP
     CPDKPWKRLD MRFEEFKRST ILSPVSELAD LFLQQGDIHA TLYTGSKAMH SQILNIFSEE
     SGAFKQFSAA QKNMKITLQR RYKNAMVDSS RQKQLEMFLG MRLFKHLPSI PVQPLHVLSR
     PSGFFLKPVP NMSESSNDGS SLLSIKRKDI TWLCPQAADI VELFIYLSEP CHVCQLLLTI
     SHGADDLTCP STVDVRTGRH IEDLKLVVEG ASIPRCANGT NLLVPLPGPI SSEDMAVTGA
     GARLHEKDTS SLSLLYDFEE LEGQLDFLTR VVAVTFYPAG AVRIPMTLGQ IEVLGISLPW
     KGMFTCERTG GRLAELARKP DEDGSPFSSC SDLNPFAATT SLQAETVSTP VQQKDPFPSN
     LLDLLTGEDS SSDPFPQPVV ECIASGGNDM LDFLDEAVVE YRGSDTVPDG SVPQNKRPKD
     SGAHLYLNCL KSLAGPNMAK KLEFVEAMKL EIERLRLNIS AAERDRALLS IGIDPATINP
     NSSYDELYIG RLCKIANALA VMGQASLEDK IIASIGLEKL ENNVIDFWNI TRIGEGCDGG
     MCQVRAEVNK SPVGSSTKSS RGESGSVFLC FQCMKKACKF CCAGKGALLL SKSYSRDTAN
     GGGSLADVSA TSIGSDHYIC KKCCSSIVLE ALIVDYVRVM VSLRRSGRVD NAGREALNEV
     FGSNITNHLA VRGQPSPNRE DFNFLRQILG KEESLSEFPF ASFLHKVETA TDSAPFFSLL
     TPLNLASSNA YWKAPPSADS VEAAIVLNTL SDVSSVILLV SPCGYSDADA PTVQIWASSD
     INKEARTLMG KWDVQSFIRS SPELSGSEKS GRAPRHIKFA FKNPVRCRII WITLRLPRLG
     SSSSVSLDKN INLLSLDENP FAPIPRRASF GATIENDPCI HAKHILVTGN TVRDKTLQSV
     ESMSVRNWLD RAPRLNRFLI PLETERPMEN DLVLELYLQP ASPLAAGFRL DAFSAIKPRV
     THSPSSDVVD IWDPTSVIME DRHVSPAILY IQVSVLQEQY KMVTIAEYRL PEARDGTKLY
     FDFPKQIQAQ RVSFKLLGDV AAFTDEPAEA VDLSSRASPF AAGLSLANRI KLYYYADPYE
     VGKWTSLSSV