SAC6_ARATH
ID SAC6_ARATH Reviewed; 593 AA.
AC Q7X911; Q9FKY0;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Phosphoinositide phosphatase SAC6;
DE Short=AtSAC6;
DE EC=3.1.3.-;
DE AltName: Full=Protein IMPAIRED IN BABA-INDUCED STERILITY 2;
DE AltName: Full=Protein SUPPRESSOR OF ACTIN 1B;
DE Short=AtSAC1b;
DE AltName: Full=Protein SUPPRESSOR OF ACTIN 6;
DE AltName: Full=SAC domain protein 6;
DE AltName: Full=SAC1-like protein AtSAC1b;
GN Name=SAC6; Synonyms=IBS2, SAC1B; OrderedLocusNames=At5g66020;
GN ORFNames=K2A18.9;
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], TISSUE SPECIFICITY, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Wassilewskija; TISSUE=Flower bud;
RX PubMed=12713536; DOI=10.1046/j.1365-313x.2003.01720.x;
RA Despres B., Bouissonnie F., Wu H.J., Gomord V., Guilleminot J., Grellet F.,
RA Berger F., Delseny M., Devic M.;
RT "Three SAC1-like genes show overlapping patterns of expression in
RT Arabidopsis but are remarkably silent during embryo development.";
RL Plant J. 34:293-306(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, DOMAIN, TISSUE SPECIFICITY, AND
RP INDUCTION BY SALT.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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 DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=15722464; DOI=10.1105/tpc.104.029728;
RA Ton J., Jakab G., Toquin V., Flors V., Iavicoli A., Maeder M.N.,
RA Metraux J.-P., Mauch-Mani B.;
RT "Dissecting the beta-aminobutyric acid-induced priming phenomenon in
RT Arabidopsis.";
RL Plant Cell 17:987-999(2005).
CC -!- FUNCTION: Phosphoinositide phosphatase that hydrolyzes PtdIns(3)P and
CC PtdIns(4)P. Involved in priming for different defense responses.
CC {ECO:0000269|PubMed:12713536, ECO:0000269|PubMed:15722464}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12713536}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12713536}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in flowers.
CC {ECO:0000269|PubMed:12713536, ECO:0000269|PubMed:12805586}.
CC -!- INDUCTION: By salt stress. {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 -!- DISRUPTION PHENOTYPE: Impaired in BABA-induced sterility (ibs) and
CC BABA-induced protection against P.syringae, H.parasitica, and salt.
CC Affected in the priming for callose deposition.
CC {ECO:0000269|PubMed:15722464}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10407.1; 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; AF266458; AAP41367.1; -; mRNA.
DR EMBL; AY227249; AAP49839.1; -; mRNA.
DR EMBL; AB011474; BAB10407.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED98142.1; -; Genomic_DNA.
DR RefSeq; NP_201403.2; NM_125999.3.
DR AlphaFoldDB; Q7X911; -.
DR SMR; Q7X911; -.
DR STRING; 3702.AT5G66020.1; -.
DR iPTMnet; Q7X911; -.
DR PaxDb; Q7X911; -.
DR PRIDE; Q7X911; -.
DR ProteomicsDB; 226617; -.
DR EnsemblPlants; AT5G66020.1; AT5G66020.1; AT5G66020.
DR GeneID; 836732; -.
DR Gramene; AT5G66020.1; AT5G66020.1; AT5G66020.
DR KEGG; ath:AT5G66020; -.
DR Araport; AT5G66020; -.
DR TAIR; locus:2156907; AT5G66020.
DR eggNOG; KOG1889; Eukaryota.
DR HOGENOM; CLU_003016_7_2_1; -.
DR InParanoid; Q7X911; -.
DR OMA; NQSKMET; -.
DR OrthoDB; 359616at2759; -.
DR PhylomeDB; Q7X911; -.
DR BioCyc; ARA:AT5G66020-MON; -.
DR PRO; PR:Q7X911; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q7X911; baseline and differential.
DR Genevisible; Q7X911; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043812; F:phosphatidylinositol-4-phosphate phosphatase activity; IBA:GO_Central.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR InterPro; IPR030069; SAC6.
DR InterPro; IPR002013; SAC_dom.
DR PANTHER; PTHR45662:SF12; PTHR45662:SF12; 1.
DR Pfam; PF02383; Syja_N; 1.
DR PROSITE; PS50275; SAC; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Hydrolase; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..593
FT /note="Phosphoinositide phosphatase SAC6"
FT /id="PRO_0000421972"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 555..575
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 128..456
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT MOTIF 391..402
FT /note="Phosphatase catalytic core"
SQ SEQUENCE 593 AA; 67626 MW; 03272BA0818B97C2 CRC64;
MVSRLKIHSG LRLWEFPDQY VIEPTDGSSA SCLDISRLDG SMKLIDQVAE CNSLRVPKIR
SIFGVVGMLK LLAGSYLVVV TESESVGSFL GHPIYKINSL KFLPCDHSLE NPHEEQKKME
TDDYSRLLSV AERTTGLYFS YEINLTLTAQ RLHDLGDESK LLPLWRQAEP RFLWNNYMLE
VLIDNKLDQF LLPVIQGSFH SFQTAIGRDI VDITLIARRC SRRNGTRMWR RGADPDGYVA
NFVETEQIVR MNGYTSSFVQ IRGSMPFMWE QIVDLTYKPK FEIVQPEEAA RIAERHFLDL
RKKYGSVLAV DLVNKHGGEG RLSERFAGAM QHITGDDVRY LHFDFHHICG HIHFERLAIL
YEQMEDFLEK NGYFLLNEKG EKMKEQLGIV RTNCIDCLDR TNVTQSMIGR KLLELQLKRI
GVFGAEETIR SHQNFDECYK ILWANHGDDI SIQYSGTPAL KGDFVRYGQR TIQGVLQDGW
NALARYYLNN FADGTKQDAI DLVQGHYIVA VSRDMAPVPR KRGLEAVANF PVALTVILIS
FWFATMSVKQ VGSGYKHLLF SLVWAGISVA VAALVRANGR IFCNRPSLHK PRS
