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TPPB_ARATH
ID   TPPB_ARATH              Reviewed;         374 AA.
AC   Q9C9S4; O64897;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Trehalose-phosphate phosphatase B;
DE            Short=AtTPPB;
DE            EC=3.1.3.12;
DE   AltName: Full=Trehalose 6-phosphate phosphatase;
GN   Name=TPPB; OrderedLocusNames=At1g78090; ORFNames=T11I11.2;
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], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP   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=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   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   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: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   -!- TISSUE SPECIFICITY: Expressed in flowers. {ECO:0000269|PubMed:9681009}.
CC   -!- INDUCTION: By trehalose. {ECO:0000269|PubMed:15181209}.
CC   -!- SIMILARITY: Belongs to the trehalose phosphatase family. {ECO:0000305}.
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DR   EMBL; AF007779; AAC39370.1; -; mRNA.
DR   EMBL; AC012680; AAG52092.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE36066.1; -; Genomic_DNA.
DR   EMBL; BT002801; AAO22625.1; -; mRNA.
DR   EMBL; BT004348; AAO42342.1; -; mRNA.
DR   PIR; H96809; H96809.
DR   PIR; T52058; T52058.
DR   RefSeq; NP_177932.1; NM_106458.4.
DR   AlphaFoldDB; Q9C9S4; -.
DR   SMR; Q9C9S4; -.
DR   STRING; 3702.AT1G78090.1; -.
DR   PaxDb; Q9C9S4; -.
DR   PRIDE; Q9C9S4; -.
DR   ProteomicsDB; 234623; -.
DR   EnsemblPlants; AT1G78090.1; AT1G78090.1; AT1G78090.
DR   GeneID; 844144; -.
DR   Gramene; AT1G78090.1; AT1G78090.1; AT1G78090.
DR   KEGG; ath:AT1G78090; -.
DR   Araport; AT1G78090; -.
DR   TAIR; locus:2194704; AT1G78090.
DR   eggNOG; KOG1050; Eukaryota.
DR   HOGENOM; CLU_037265_1_2_1; -.
DR   InParanoid; Q9C9S4; -.
DR   OMA; NRLVEWK; -.
DR   OrthoDB; 974358at2759; -.
DR   PhylomeDB; Q9C9S4; -.
DR   UniPathway; UPA00299; -.
DR   PRO; PR:Q9C9S4; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C9S4; baseline and differential.
DR   Genevisible; Q9C9S4; 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   Hydrolase; Reference proteome; Stress response.
FT   CHAIN           1..374
FT                   /note="Trehalose-phosphate phosphatase B"
FT                   /id="PRO_0000417644"
FT   CONFLICT        86
FT                   /note="V -> D (in Ref. 1; AAC39370)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   374 AA;  42449 MW;  B8209AF73CC26732 CRC64;
     MTNQNVIVSD RKPILGLKTI TVSVSNSPLF SNSFPTYFNF PRRKLLKLLE AADKNNLVVA
     PKITSMIDSM RDSSPTRLRS SSYDSVSDND DKTSWIVRFP SALNMFDEIV NAAKGKQIVM
     FLDYDGTLSP IVEDPDKAFI THEMREVVKD VASNFPTAIV TGRSIEKVRS FVQVNEIYYA
     GSHGMDIEGP TNENSNGQSN ERVLFQPARE FLPMIEKVVN ILEEKTKWIP GAMVENNKFC
     LSVHFRRVDE KRWPALAEVV KSVLIDYPKL KLTQGRKVLE IRPTIKWDKG QALNFLLKSL
     GYENSDDVVP VYIGDDRTDE DAFKVLRERG QGFGILVSKV PKDTNASYSL QDPSQVNKFL
     ERLVEWKRKT VGEE
 
 
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