SAC7_ARATH
ID SAC7_ARATH Reviewed; 597 AA.
AC Q9C5G5; Q0WM67; Q9SD03;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Phosphoinositide phosphatase SAC7;
DE Short=AtSAC7;
DE EC=3.1.3.-;
DE AltName: Full=Protein ROOT HAIR DEFECTIVE 4;
DE AltName: Full=Protein SUPPRESSOR OF ACTIN 1C;
DE Short=AtSAC1c;
DE AltName: Full=Protein SUPPRESSOR OF ACTIN 7;
DE AltName: Full=SAC domain protein 7;
DE AltName: Full=SAC1-like protein AtSAC1c;
GN Name=SAC7; Synonyms=RHD4, SAC1C; OrderedLocusNames=At3g51460;
GN ORFNames=F26O13.100;
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, SUBCELLULAR
RP LOCATION, AND INDUCTION BY WOUNDING.
RC STRAIN=cv. Wassilewskija;
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, 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=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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 309-597.
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 [7]
RP FUNCTION.
RX DOI=10.1139/b99-010;
RA Galway M.E., Lane D.C., Schiefelbein J.W.;
RT "Defective control of growth rate and cell diameter in tip-growing root
RT hairs of the rhd4 mutant of Arabidopsis thaliana.";
RL Can. J. Bot. 77:494-507(1999).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=18281508; DOI=10.1105/tpc.107.054304;
RA Thole J.M., Vermeer J.E., Zhang Y., Gadella T.W. Jr., Nielsen E.;
RT "Root hair defective4 encodes a phosphatidylinositol-4-phosphate
RT phosphatase required for proper root hair development in Arabidopsis
RT thaliana.";
RL Plant Cell 20:381-395(2008).
CC -!- FUNCTION: Phosphoinositide phosphatase that preferentially hydrolyzes
CC PtdIns(4)P. Regulates the accumulation of PtdIns(4)P on membrane
CC compartments at the tips of growing root hairs leading to proper root
CC hair development. {ECO:0000269|PubMed:12713536,
CC ECO:0000269|PubMed:18281508, ECO:0000269|Ref.7}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12713536}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:18281508}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Associated to tip-localized membranes in growing
CC root hairs (PubMed:18281508). {ECO:0000269|PubMed:18281508}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12713536,
CC ECO:0000269|PubMed:12805586}.
CC -!- INDUCTION: By wounding. {ECO:0000269|PubMed:12713536}.
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: Short, bulged and branched root hairs.
CC Accumulates elevated levels of PtdIns(4)P in roots.
CC {ECO:0000269|PubMed:18281508}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB63010.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF266459; AAP41368.1; -; mRNA.
DR EMBL; AY227250; AAP49840.1; -; mRNA.
DR EMBL; AL133452; CAB63010.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78795.1; -; Genomic_DNA.
DR EMBL; AF360267; AAK25977.1; -; mRNA.
DR EMBL; AY040078; AAK64136.1; -; mRNA.
DR EMBL; AK229963; BAF01789.1; -; mRNA.
DR PIR; T45777; T45777.
DR RefSeq; NP_190714.2; NM_115005.5.
DR AlphaFoldDB; Q9C5G5; -.
DR SMR; Q9C5G5; -.
DR BioGRID; 9627; 3.
DR IntAct; Q9C5G5; 1.
DR STRING; 3702.AT3G51460.1; -.
DR iPTMnet; Q9C5G5; -.
DR PaxDb; Q9C5G5; -.
DR PRIDE; Q9C5G5; -.
DR ProteomicsDB; 232727; -.
DR EnsemblPlants; AT3G51460.1; AT3G51460.1; AT3G51460.
DR GeneID; 824309; -.
DR Gramene; AT3G51460.1; AT3G51460.1; AT3G51460.
DR KEGG; ath:AT3G51460; -.
DR Araport; AT3G51460; -.
DR TAIR; locus:2081780; AT3G51460.
DR eggNOG; KOG1889; Eukaryota.
DR HOGENOM; CLU_003016_7_2_1; -.
DR InParanoid; Q9C5G5; -.
DR OMA; FRDINVH; -.
DR OrthoDB; 359616at2759; -.
DR PhylomeDB; Q9C5G5; -.
DR BioCyc; ARA:AT3G51460-MON; -.
DR BRENDA; 3.1.3.66; 399.
DR BRENDA; 3.1.3.B4; 399.
DR PRO; PR:Q9C5G5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9C5G5; baseline and differential.
DR Genevisible; Q9C5G5; AT.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0031520; C:plasma membrane of cell tip; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0090404; C:pollen tube tip; IDA:TAIR.
DR GO; GO:0035619; C:root hair tip; IDA:TAIR.
DR GO; GO:0043812; F:phosphatidylinositol-4-phosphate phosphatase activity; IDA:TAIR.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR GO; GO:0009611; P:response to wounding; NAS:UniProtKB.
DR GO; GO:0048768; P:root hair cell tip growth; IMP:TAIR.
DR InterPro; IPR002013; SAC_dom.
DR Pfam; PF02383; Syja_N; 1.
DR PROSITE; PS50275; SAC; 1.
PE 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Hydrolase; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..597
FT /note="Phosphoinositide phosphatase SAC7"
FT /id="PRO_0000421973"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 559..579
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 130..458
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT MOTIF 393..404
FT /note="Phosphatase catalytic core"
SQ SEQUENCE 597 AA; 68237 MW; 18C62357E3BD53DA CRC64;
METVDSRNKL HSRLRLWEFP DQYIIEPADG SGSSCLDISR VDASMKLIDQ VPESNSVRVP
KIRSIFGVVG MLKLLAGSYL VVVTESERVG SFLGHPIFKV TTLKVLPCDH SLKNSPEEQK
KMETEFSKLL SVAEKTTGLY FSYEVNLTLS SQRLHEMGDE SKSLPLWRQA EPRFLWNNYM
LEVLIDNKLD QFLLPVIQGS FNSFETAIGR DIVDITLIAR RCTRRNGTRM WRRGADLDGY
VANFVETEQI VQMNGYTSSF VQVRGSMPFM WEQVVDLTYK PKFEIVQPEE AKRIAERHFL
DLRKKYGSVL AVDLVNKQGG EGRLCEKYAT VMQHITGDDI RYLHFDFHQI CGHIHFERLS
ILYEQIEGFL EKNGYFLLNE KGEKMKEQLG VVRSNCIDCL DRTNVTQSMI GRKMLEVQLK
RIGVFGAEET ISSHLNFDEH YKILWANHGD EISIQYSGTP ALKGDFVRYG HRTAHGVLKD
GWSSLRRYYL NNFADGTKQD AIDLLQGHYI VAVSRDMAPV PQKGGLEAVA NFPVALFVVL
MSFWFATMSL KQTGSDYKHK HLFFSLLWTG ICVGMAALVR ANGRIFCNRP RLHKPRG
