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TPPD_ARATH
ID   TPPD_ARATH              Reviewed;         369 AA.
AC   Q67XC9; Q8LCM4; Q9C8B3;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Probable trehalose-phosphate phosphatase D;
DE            Short=AtTPPD;
DE            EC=3.1.3.12;
DE   AltName: Full=Trehalose 6-phosphate phosphatase;
GN   Name=TPPD; OrderedLocusNames=At1g35910; ORFNames=F10O5.8;
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 [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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   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 (By similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC   -!- SIMILARITY: Belongs to the trehalose phosphatase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG51089.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC027032; AAG51089.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE31836.1; -; Genomic_DNA.
DR   EMBL; AK176890; BAD44653.1; -; mRNA.
DR   EMBL; AY086513; AAM63513.1; -; mRNA.
DR   PIR; A86481; A86481.
DR   RefSeq; NP_564464.1; NM_103289.5.
DR   AlphaFoldDB; Q67XC9; -.
DR   SMR; Q67XC9; -.
DR   STRING; 3702.AT1G35910.1; -.
DR   PaxDb; Q67XC9; -.
DR   PRIDE; Q67XC9; -.
DR   ProteomicsDB; 228296; -.
DR   EnsemblPlants; AT1G35910.1; AT1G35910.1; AT1G35910.
DR   GeneID; 840493; -.
DR   Gramene; AT1G35910.1; AT1G35910.1; AT1G35910.
DR   KEGG; ath:AT1G35910; -.
DR   Araport; AT1G35910; -.
DR   TAIR; locus:2007651; AT1G35910.
DR   eggNOG; KOG1050; Eukaryota.
DR   HOGENOM; CLU_037265_1_2_1; -.
DR   InParanoid; Q67XC9; -.
DR   OMA; FQAANEF; -.
DR   OrthoDB; 974358at2759; -.
DR   PhylomeDB; Q67XC9; -.
DR   UniPathway; UPA00299; -.
DR   PRO; PR:Q67XC9; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q67XC9; baseline and differential.
DR   Genevisible; Q67XC9; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0015927; F:trehalase activity; IDA:TAIR.
DR   GO; GO:0004805; F:trehalose-phosphatase activity; IDA:TAIR.
DR   GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
DR   GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.1000; -; 2.
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   2: Evidence at transcript level;
KW   Hydrolase; Reference proteome; Stress response.
FT   CHAIN           1..369
FT                   /note="Probable trehalose-phosphate phosphatase D"
FT                   /id="PRO_0000417646"
FT   REGION          63..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        79
FT                   /note="P -> T (in Ref. 4; AAM63513)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        266
FT                   /note="R -> S (in Ref. 4; AAM63513)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   369 AA;  41598 MW;  FB606D1627C9AAC7 CRC64;
     MTNHNALISD AKGSIGVAVR VPNQSLFSPG GGRYISIPRK KLVQKLEADP SQTRIHTWIE
     AMRASSPTRT RPGNISPLPE SDEEDEYSSW MAQHPSALTM FEEIAEASKG KQIVMFLDYD
     GTLSPIVENP DRAYMSEEMR EAVKGVARYF PTAIVTGRCR DKVRRFVKLP GLYYAGSHGM
     DIKGPSKRNK HNKNNKGVLF QAANEFLPMI DKVSKCLVEK MRDIEGANVE NNKFCVSVHY
     RCVDQKDWGL VAEHVTSILS EYPKLRLTQG RKVLEIRPTI KWDKGKALEF LLESLGFANS
     NDVLPIYIGD DRTDEDAFKV LRNKGQGFGI LVSKIPKETS ATYSLQEPSE VGEFLQRLVE
     WKQMSLRGR
 
 
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