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TRNH6_ARATH
ID   TRNH6_ARATH             Reviewed;         262 AA.
AC   Q9ZW13; F4IKL4;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Tropinone reductase homolog At2g29290 {ECO:0000305};
DE            EC=1.1.1.- {ECO:0000305};
GN   OrderedLocusNames=At2g29290 {ECO:0000312|Araport:AT2G29290};
GN   ORFNames=F16P2.33 {ECO:0000312|EMBL:AAC95208.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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;
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   [4]
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   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=19027726; DOI=10.1016/j.cbi.2008.10.040;
RA   Persson B., Kallberg Y., Bray J.E., Bruford E., Dellaporta S.L.,
RA   Favia A.D., Duarte R.G., Joernvall H., Kavanagh K.L., Kedishvili N.,
RA   Kisiela M., Maser E., Mindnich R., Orchard S., Penning T.M., Thornton J.M.,
RA   Adamski J., Oppermann U.;
RT   "The SDR (short-chain dehydrogenase/reductase and related enzymes)
RT   nomenclature initiative.";
RL   Chem. Biol. Interact. 178:94-98(2009).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9ZW13-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9ZW13-2; Sequence=VSP_057495;
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. SDR65C subfamily. {ECO:0000305}.
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DR   EMBL; AC004561; AAC95208.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08228.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08229.1; -; Genomic_DNA.
DR   EMBL; BT010409; AAQ62410.1; -; mRNA.
DR   EMBL; AK175125; BAD42888.1; -; mRNA.
DR   PIR; E84694; E84694.
DR   RefSeq; NP_001118408.1; NM_001124936.2. [Q9ZW13-1]
DR   RefSeq; NP_180490.2; NM_128483.3. [Q9ZW13-2]
DR   AlphaFoldDB; Q9ZW13; -.
DR   SMR; Q9ZW13; -.
DR   STRING; 3702.AT2G29290.2; -.
DR   PaxDb; Q9ZW13; -.
DR   PRIDE; Q9ZW13; -.
DR   ProteomicsDB; 242802; -. [Q9ZW13-1]
DR   EnsemblPlants; AT2G29290.1; AT2G29290.1; AT2G29290. [Q9ZW13-2]
DR   EnsemblPlants; AT2G29290.2; AT2G29290.2; AT2G29290. [Q9ZW13-1]
DR   GeneID; 817478; -.
DR   Gramene; AT2G29290.1; AT2G29290.1; AT2G29290. [Q9ZW13-2]
DR   Gramene; AT2G29290.2; AT2G29290.2; AT2G29290. [Q9ZW13-1]
DR   KEGG; ath:AT2G29290; -.
DR   Araport; AT2G29290; -.
DR   TAIR; locus:2043052; AT2G29290.
DR   eggNOG; KOG0725; Eukaryota.
DR   HOGENOM; CLU_010194_1_1_1; -.
DR   InParanoid; Q9ZW13; -.
DR   OMA; LTTHIAC; -.
DR   PhylomeDB; Q9ZW13; -.
DR   BioCyc; ARA:AT2G29290-MON; -.
DR   PRO; PR:Q9ZW13; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZW13; baseline and differential.
DR   Genevisible; Q9ZW13; AT.
DR   GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   InterPro; IPR045000; TR.
DR   PANTHER; PTHR42898; PTHR42898; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..262
FT                   /note="Tropinone reductase homolog At2g29290"
FT                   /id="PRO_0000432361"
FT   ACT_SITE        159
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         13..37
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P50162"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P50162"
FT   VAR_SEQ         1..22
FT                   /note="MDKRWSLQGMNALVTGGTKGIG -> MESSR (in isoform 2)"
FT                   /id="VSP_057495"
SQ   SEQUENCE   262 AA;  28406 MW;  6E84BDE7487F19AD CRC64;
     MDKRWSLQGM NALVTGGTKG IGEAVVEELS ILGARVHTCA RDETQLQERL REWQEKGFQV
     TTSICDVSLR EQREKLMETV SSLFQGKLNI LVNNVGTLML KPTTEYTAEE FSFLMATNLD
     SAFHISQLAH PLLKASGSGS IVLMSSIAGV VHVGVGSIYG ATKGAMNQLA RNLACEWASD
     NIRTNAICPW LITTPLISDL LSVEEMKKEA EERTPMGRVG EANEVSPLVA FLCLPAASYI
     TGQVICVDGG LTVNGFSYQP HA
 
 
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