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SAC5_ARATH
ID   SAC5_ARATH              Reviewed;         785 AA.
AC   Q8RW97; Q0WMR5; Q9LQI5;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Phosphoinositide phosphatase SAC5;
DE            Short=AtSAC5;
DE            EC=3.1.3.-;
DE   AltName: Full=Phosphatidylinositol 3,5-bisphosphate 5-phosphatase SAC5;
DE   AltName: Full=Protein SUPPRESSOR OF ACTIN 5;
DE   AltName: Full=SAC domain protein 5;
GN   Name=SAC5; OrderedLocusNames=At1g17340; ORFNames=F28G4.21;
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=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   [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;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 221-785.
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.
CC   -!- FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis
CC       and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
CC       {ECO:0000250}.
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;
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}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous with a higher level of expression in
CC       young seedlings than in other tissues. {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   -!- SEQUENCE CAUTION:
CC       Sequence=AAF97309.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY227248; AAP49838.1; -; mRNA.
DR   EMBL; AC007843; AAF97309.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE29574.1; -; Genomic_DNA.
DR   EMBL; AY093760; AAM10384.1; -; mRNA.
DR   EMBL; BT002292; AAN72303.1; -; mRNA.
DR   EMBL; AK229748; BAF01585.1; -; mRNA.
DR   PIR; H86309; H86309.
DR   RefSeq; NP_173177.2; NM_101595.6.
DR   AlphaFoldDB; Q8RW97; -.
DR   SMR; Q8RW97; -.
DR   BioGRID; 23545; 1.
DR   IntAct; Q8RW97; 1.
DR   STRING; 3702.AT1G17340.1; -.
DR   iPTMnet; Q8RW97; -.
DR   PaxDb; Q8RW97; -.
DR   PRIDE; Q8RW97; -.
DR   ProteomicsDB; 226662; -.
DR   EnsemblPlants; AT1G17340.1; AT1G17340.1; AT1G17340.
DR   GeneID; 838305; -.
DR   Gramene; AT1G17340.1; AT1G17340.1; AT1G17340.
DR   KEGG; ath:AT1G17340; -.
DR   Araport; AT1G17340; -.
DR   TAIR; locus:2029105; AT1G17340.
DR   eggNOG; KOG1888; Eukaryota.
DR   HOGENOM; CLU_003016_4_2_1; -.
DR   InParanoid; Q8RW97; -.
DR   OMA; SNAFARW; -.
DR   OrthoDB; 359616at2759; -.
DR   PhylomeDB; Q8RW97; -.
DR   BioCyc; ARA:AT1G17340-MON; -.
DR   PRO; PR:Q8RW97; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8RW97; baseline and differential.
DR   Genevisible; Q8RW97; AT.
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; IBA:GO_Central.
DR   GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Hydrolase; Membrane; Reference proteome; Vacuole.
FT   CHAIN           1..785
FT                   /note="Phosphoinositide phosphatase SAC5"
FT                   /id="PRO_0000421971"
FT   DOMAIN          158..533
FT                   /note="SAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT   REGION          688..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           469..480
FT                   /note="Phosphatase catalytic core"
FT   CONFLICT        282
FT                   /note="G -> S (in Ref. 5; BAF01585)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   785 AA;  89837 MW;  FE4A672D35ABD331 CRC64;
     MGSEPRFEPR PELIDLPVLQ KFKLYATPSN FYLIGRDENK SFRRILKIDR RDQNELNLFE
     DPTRYTKDEM RELKRRMIVG NEESGGFKAI TTCYGIIGFV RFLEPYYMLL ITKRKKVGEI
     CGHTVYGIAE SQMIAIPHPS IQSKVAKSEA ELRYKKLLSV VDLSKNFYFS YTYHLMYSLQ
     KNIGNTERGN PHDNTMFVWN SFLTREIRKI LQNSIWTVAL IYGFFQQTKC SVSGEKFVFT
     IIARRSRHYA GTRYLRRGVN DIGRVANDVE TEQIVSKVVP AGQKIPITSV VQVRGSIPLF
     WSQEASVFNP QPEIILNKKD ANYEATQHHF QNLRQRYGNR IIILNLLKTV TGEKKHRETI
     LRGEFAKTIR FINKGMDREH RLKAIHFDLS KHYKKGADGA FNHLCIFSRK SLELTDLFYC
     KAPSGVGAEE VIYDSFFNNP IPSQDEEASS PEKEDMKADI FLLQNGVLRT NCIDCLDRTN
     FAQYAHGLVS LGHQLRTLGI SGPPVVDLNN PLAIELMDAY QKMGNTLAMQ YGGSEAHSKM
     FCDLRGNWNM VMRQRDIFTA VRRYYSNAYQ DSDKQNAINV FLGHFRPRLG RPALWELDSD
     QHNIGRSGSN LDIENMRPLI RRSFSDNIIM DCDLNLEELV RENSQPTYEG LNGGVSGTNL
     EFPFYETEPA SLSFLSVMRN EELMRETGSG QMFQGSSSNS DSHRPNDIPG FSHSYVTKFT
     PAEDIFERGS SKSVSSDNLF TDRDESVTSL TNTNSSFEFP IMGGSDLLPG FSNAFARWVF
     SARAW
 
 
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