SAC8_ARATH
ID SAC8_ARATH Reviewed; 588 AA.
AC Q96328;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Phosphoinositide phosphatase SAC8;
DE Short=AtSAC8;
DE EC=3.1.3.-;
DE AltName: Full=Protein SUPPRESSOR OF ACTIN 1A;
DE Short=AtSAC1a;
DE AltName: Full=Protein SUPPRESSOR OF ACTIN 8;
DE AltName: Full=Putative transmembrane protein G5p;
DE Short=AtG5;
DE AltName: Full=SAC domain protein 8;
DE AltName: Full=SAC1-like protein AtSAC1a;
GN Name=SAC8; Synonyms=G5, SAC1A; OrderedLocusNames=At3g51830;
GN ORFNames=ATEM1.8;
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].
RC STRAIN=cv. Columbia;
RA Grellet F., Gaubier P., Wu H.-J., Laudie M., Berger C., Delseny M.;
RT "Structure of the Arabidopsis thaliana Em1 locus.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10645728; DOI=10.1023/a:1006395324818;
RA Comella P., Wu H.-J., Laudie M., Berger C., Cooke R., Delseny M.,
RA Grellet F.;
RT "Fine sequence analysis of 60 kb around the Arabidopsis thaliana AtEm1
RT locus on chromosome III.";
RL Plant Mol. Biol. 41:687-700(1999).
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 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).
RN [6]
RP TISSUE SPECIFICITY, FUNCTION, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Phosphoinositide phosphatase that hydrolyzes PtdIns(3)P and
CC PtdIns(4)P. {ECO:0000269|PubMed:12713536}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12713536}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12713536}.
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=Q96328-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous with a higher level of expression in
CC young seedlings than in other tissues. {ECO:0000269|PubMed:12713536,
CC 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; U72504; AAB18128.1; -; mRNA.
DR EMBL; AY227251; AAP49841.1; -; mRNA.
DR EMBL; AF049236; AAC14410.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78849.1; -; Genomic_DNA.
DR EMBL; AY080659; AAL86335.1; -; mRNA.
DR EMBL; AY133741; AAM91675.1; -; mRNA.
DR PIR; T51154; T51154.
DR RefSeq; NP_190751.2; NM_115042.3. [Q96328-1]
DR AlphaFoldDB; Q96328; -.
DR SMR; Q96328; -.
DR BioGRID; 9664; 1.
DR IntAct; Q96328; 1.
DR STRING; 3702.AT3G51830.1; -.
DR iPTMnet; Q96328; -.
DR PaxDb; Q96328; -.
DR PRIDE; Q96328; -.
DR ProteomicsDB; 226663; -. [Q96328-1]
DR EnsemblPlants; AT3G51830.1; AT3G51830.1; AT3G51830. [Q96328-1]
DR GeneID; 824346; -.
DR Gramene; AT3G51830.1; AT3G51830.1; AT3G51830. [Q96328-1]
DR KEGG; ath:AT3G51830; -.
DR Araport; AT3G51830; -.
DR TAIR; locus:2074398; AT3G51830.
DR eggNOG; KOG1889; Eukaryota.
DR HOGENOM; CLU_003016_7_2_1; -.
DR InParanoid; Q96328; -.
DR OMA; YFMVNSD; -.
DR OrthoDB; 359616at2759; -.
DR PhylomeDB; Q96328; -.
DR BioCyc; ARA:AT3G51830-MON; -.
DR PRO; PR:Q96328; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q96328; baseline and differential.
DR Genevisible; Q96328; 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 InterPro; IPR002013; SAC_dom.
DR Pfam; PF02383; Syja_N; 1.
DR PROSITE; PS50275; SAC; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Hydrolase; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..588
FT /note="Phosphoinositide phosphatase SAC8"
FT /id="PRO_0000421974"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 555..575
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 129..455
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT REGION 37..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 390..401
FT /note="Phosphatase catalytic core"
SQ SEQUENCE 588 AA; 66464 MW; 6ADC187B7CC3753D CRC64;
MEIAPSTSRF KLYDQFELLE FPDKYVVKPI ESPEEGFSVN RRDGNIKPLD ENASSGSPTR
VSTIYGVGGT IRLLAGTYLL VITSREEVGN FLGLPIFRVT AMKFLPCNEA LRFATAQEKK
DETYFRTLLQ ALETTPGLYF SYETDLTLNL QRRCKLAEGW NRKPMWKQAD PRYVWNWHLL
EDLIECKLDG FIIPILQGSY QVAELKLKNS PAVVSIMSRR CTRRLGTRMW RRGANLEGDA
ANFVESEQIV EINGFKFSLL QVRGSIPLLW EQIVDLSYKP RLKINKHEET PKVVQRHFHD
LCQRYGEIMA VDLTDQHGDE GALSKAYATE MEKLPDVRYV SFDFHQVCGT TNFDNLGVLY
EQIGDEFEKQ GYFLVDADEN ILEEQKGVIR SNCIDCLDRT NVTQSFMGQK SLNLQLQRIG
VCDSTECIST FEDDYTKFRT IWAEQGDEVS LQYAGTYALK GDLVRYGKQT MTGAIKDGLS
AMSRYYLNNF QDGVRQDALD LISGRYTVGT HSPSQLQPIG SQPSFLPVAS ALLIGGVTVT
SFTIHQAGRN TQQYLASALW AGVTAGVVAM IKANGRHLTS RPRLCHLI
