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TPPA_ARATH
ID   TPPA_ARATH              Reviewed;         385 AA.
AC   O64896; Q8RWE2;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Trehalose-phosphate phosphatase A;
DE            Short=AtTPPA;
DE            EC=3.1.3.12;
DE   AltName: Full=Trehalose 6-phosphate phosphatase;
GN   Name=TPPA; OrderedLocusNames=At5g51460; ORFNames=K17N15.1, MFG13.17;
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=9681009; DOI=10.1046/j.1365-313x.1998.00064.x;
RA   Vogel G., Aeschbacher R.A., Muller J., Boller T., Wiemken A.;
RT   "Trehalose-6-phosphate phosphatases from Arabidopsis thaliana:
RT   identification by functional complementation of the yeast tps2 mutant.";
RL   Plant J. 13:673-683(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(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] (ISOFORM 2).
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   FUNCTION.
RX   PubMed=11520870; DOI=10.1093/jexbot/52.362.1817;
RA   Vogel G., Fiehn O., Jean-Richard-dit-Bressel L., Boller T., Wiemken A.,
RA   Aeschbacher R.A., Wingler A.;
RT   "Trehalose metabolism in Arabidopsis: occurrence of trehalose and molecular
RT   cloning and characterization of trehalose-6-phosphate synthase
RT   homologues.";
RL   J. Exp. Bot. 52:1817-1826(2001).
RN   [6]
RP   GENE FAMILY.
RX   PubMed=12508064; DOI=10.1093/jxb/erg039;
RA   Eastmond P.J., Li Y., Graham I.A.;
RT   "Is trehalose-6-phosphate a regulator of sugar metabolism in plants?";
RL   J. Exp. Bot. 54:533-537(2003).
RN   [7]
RP   INDUCTION, AND NOMENCLATURE.
RX   PubMed=15181209; DOI=10.1104/pp.104.039503;
RA   Schluepmann H., van Dijken A.J.H., Aghdasi M., Wobbes B., Paul M.,
RA   Smeekens S.C.M.;
RT   "Trehalose mediated growth inhibition of Arabidopsis seedlings is due to
RT   trehalose-6-phosphate accumulation.";
RL   Plant Physiol. 135:879-890(2004).
CC   -!- FUNCTION: Removes the phosphate from trehalose 6-phosphate to produce
CC       free trehalose. Trehalose accumulation in plant may improve abiotic
CC       stress tolerance. {ECO:0000269|PubMed:11520870,
CC       ECO:0000269|PubMed:9681009}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-
CC         trehalose + phosphate; Xref=Rhea:RHEA:23420, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16551, ChEBI:CHEBI:43474, ChEBI:CHEBI:58429; EC=3.1.3.12;
CC         Evidence={ECO:0000269|PubMed:9681009};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O64896-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O64896-2; Sequence=VSP_043862;
CC   -!- TISSUE SPECIFICITY: Expressed in flowers. {ECO:0000269|PubMed:9681009}.
CC   -!- INDUCTION: By trehalose. {ECO:0000269|PubMed:15181209}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC       site. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the trehalose phosphatase family. {ECO:0000305}.
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DR   EMBL; AF007778; AAC39369.1; -; mRNA.
DR   EMBL; AB018109; BAB08662.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96085.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96086.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96087.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM70853.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM70854.1; -; Genomic_DNA.
DR   EMBL; AY093147; AAM13146.1; -; mRNA.
DR   EMBL; BT008467; AAP37826.1; -; mRNA.
DR   PIR; T52057; T52057.
DR   RefSeq; NP_001332431.1; NM_001344937.1. [O64896-2]
DR   RefSeq; NP_001332432.1; NM_001344938.1. [O64896-1]
DR   RefSeq; NP_199959.2; NM_124525.2. [O64896-2]
DR   RefSeq; NP_851171.1; NM_180840.2. [O64896-1]
DR   RefSeq; NP_974922.1; NM_203193.3. [O64896-1]
DR   AlphaFoldDB; O64896; -.
DR   SMR; O64896; -.
DR   STRING; 3702.AT5G51460.1; -.
DR   iPTMnet; O64896; -.
DR   PaxDb; O64896; -.
DR   PRIDE; O64896; -.
DR   ProteomicsDB; 232380; -. [O64896-1]
DR   EnsemblPlants; AT5G51460.1; AT5G51460.1; AT5G51460. [O64896-1]
DR   EnsemblPlants; AT5G51460.2; AT5G51460.2; AT5G51460. [O64896-2]
DR   EnsemblPlants; AT5G51460.3; AT5G51460.3; AT5G51460. [O64896-1]
DR   EnsemblPlants; AT5G51460.4; AT5G51460.4; AT5G51460. [O64896-2]
DR   EnsemblPlants; AT5G51460.5; AT5G51460.5; AT5G51460. [O64896-1]
DR   GeneID; 835220; -.
DR   Gramene; AT5G51460.1; AT5G51460.1; AT5G51460. [O64896-1]
DR   Gramene; AT5G51460.2; AT5G51460.2; AT5G51460. [O64896-2]
DR   Gramene; AT5G51460.3; AT5G51460.3; AT5G51460. [O64896-1]
DR   Gramene; AT5G51460.4; AT5G51460.4; AT5G51460. [O64896-2]
DR   Gramene; AT5G51460.5; AT5G51460.5; AT5G51460. [O64896-1]
DR   KEGG; ath:AT5G51460; -.
DR   Araport; AT5G51460; -.
DR   TAIR; locus:2153082; AT5G51460.
DR   eggNOG; KOG1050; Eukaryota.
DR   HOGENOM; CLU_037265_1_0_1; -.
DR   InParanoid; O64896; -.
DR   OMA; MIKSQPV; -.
DR   PhylomeDB; O64896; -.
DR   BioCyc; ARA:AT5G51460-MON; -.
DR   UniPathway; UPA00299; -.
DR   PRO; PR:O64896; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; O64896; baseline and differential.
DR   Genevisible; O64896; AT.
DR   GO; GO:0004805; F:trehalose-phosphatase activity; IDA:TAIR.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IDA:TAIR.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR044651; OTSB-like.
DR   InterPro; IPR003337; Trehalose_PPase.
DR   PANTHER; PTHR43768; PTHR43768; 1.
DR   Pfam; PF02358; Trehalose_PPase; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR   TIGRFAMs; TIGR00685; T6PP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; Reference proteome; Stress response.
FT   CHAIN           1..385
FT                   /note="Trehalose-phosphate phosphatase A"
FT                   /id="PRO_0000417643"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         99
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_043862"
SQ   SEQUENCE   385 AA;  43192 MW;  DE21BB6F83782CF9 CRC64;
     MDMKSGHSSP VMTDSPPISN SRLTIRQNRL PYSSAAATAI SQNNNLLLTV PRKKTGILDD
     VKSNGWLDAM KSSSPPPTIL NKDNLSNDAT DMTYREWMQL KYPSALTSFE KIMSFAKGKR
     IALFLDYDGT LSPIVEEPDC AYMSSAMRSA VQNVAKYFPT AIISGRSRDK VYEFVNLSEL
     YYAGSHGMDI MSPAGESLNH EHSRTVSVYE QGKDVNLFQP ASEFLPMIDK VLCSLIESTK
     DIKGVKVEDN KFCISVHYRN VEEKNWTLVA QCVDDVIRTY PKLRLTHGRK VLEIRPVIDW
     DKGKAVTFLL ESLGLNNCED VLPIYVGDDR TDEDAFKVLR DGPNHGYGIL VSAVPKDSNA
     FYSLRDPSEV MEFLKSLVTW KRSMG
 
 
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