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TIC32_ARATH
ID   TIC32_ARATH             Reviewed;         322 AA.
AC   A2RVM0; B3H4I7; O81739; Q0WTU0; Q8L9T6;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Short-chain dehydrogenase TIC 32, chloroplastic {ECO:0000303|PubMed:15180984};
DE            EC=1.1.1.-;
DE   AltName: Full=Translocon at the inner envelope membrane of chloroplasts 32 {ECO:0000303|PubMed:15180984};
DE            Short=AtTIC32 {ECO:0000303|PubMed:15180984};
GN   Name=TIC32 {ECO:0000303|PubMed:15180984};
GN   OrderedLocusNames=At4g23430 {ECO:0000312|Araport:AT4G23430};
GN   ORFNames=F16G20.130 {ECO:0000312|EMBL:CAA20464.1};
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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;
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.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=15033972; DOI=10.1074/jbc.m401968200;
RA   Vojta A., Alavi M., Becker T., Hoermann F., Kuechler M., Soll J.,
RA   Thomson R., Schleiff E.;
RT   "The protein translocon of the plastid envelopes.";
RL   J. Biol. Chem. 279:21401-21405(2004).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15180984; DOI=10.1074/jbc.m402817200;
RA   Hoermann F., Kuechler M., Sveshnikov D., Oppermann U., Li Y., Soll J.;
RT   "Tic32, an essential component in chloroplast biogenesis.";
RL   J. Biol. Chem. 279:34756-34762(2004).
RN   [8]
RP   REVIEW.
RX   PubMed=20100520; DOI=10.1016/j.bbamcr.2010.01.015;
RA   Kovacs-Bogdan E., Soll J., Bolter B.;
RT   "Protein import into chloroplasts: the Tic complex and its regulation.";
RL   Biochim. Biophys. Acta 1803:740-747(2010).
CC   -!- FUNCTION: Involved in protein precursor import into chloroplasts. Part
CC       of the redox regulon consisting of TIC32, TIC 55 and TIC62.
CC       {ECO:0000269|PubMed:15180984}.
CC   -!- SUBUNIT: Part of the Tic complex. Interacts with TIC110.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC       {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=A2RVM0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2RVM0-2; Sequence=VSP_041955;
CC       Name=3;
CC         IsoId=A2RVM0-3; Sequence=VSP_041954, VSP_041955;
CC   -!- TISSUE SPECIFICITY: Expressed in leaves and roots.
CC       {ECO:0000269|PubMed:15033972}.
CC   -!- DISRUPTION PHENOTYPE: Embryo lethal. {ECO:0000269|PubMed:15180984}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA20464.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79298.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL031326; CAA20464.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161559; CAB79298.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE84753.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84754.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84755.1; -; Genomic_DNA.
DR   EMBL; AK227455; BAE99458.1; -; mRNA.
DR   EMBL; BT030011; ABN04749.1; -; mRNA.
DR   EMBL; AY088231; AAM65772.1; -; mRNA.
DR   PIR; T05381; T05381.
DR   RefSeq; NP_001119035.1; NM_001125563.1. [A2RVM0-3]
DR   RefSeq; NP_567681.1; NM_118472.3. [A2RVM0-2]
DR   RefSeq; NP_849428.1; NM_179097.3. [A2RVM0-1]
DR   AlphaFoldDB; A2RVM0; -.
DR   SMR; A2RVM0; -.
DR   BioGRID; 13731; 4.
DR   STRING; 3702.AT4G23430.2; -.
DR   iPTMnet; A2RVM0; -.
DR   PaxDb; A2RVM0; -.
DR   PRIDE; A2RVM0; -.
DR   EnsemblPlants; AT4G23430.1; AT4G23430.1; AT4G23430. [A2RVM0-2]
DR   EnsemblPlants; AT4G23430.2; AT4G23430.2; AT4G23430. [A2RVM0-1]
DR   EnsemblPlants; AT4G23430.3; AT4G23430.3; AT4G23430. [A2RVM0-3]
DR   GeneID; 828442; -.
DR   Gramene; AT4G23430.1; AT4G23430.1; AT4G23430. [A2RVM0-2]
DR   Gramene; AT4G23430.2; AT4G23430.2; AT4G23430. [A2RVM0-1]
DR   Gramene; AT4G23430.3; AT4G23430.3; AT4G23430. [A2RVM0-3]
DR   KEGG; ath:AT4G23430; -.
DR   Araport; AT4G23430; -.
DR   TAIR; locus:2117969; AT4G23430.
DR   eggNOG; KOG1208; Eukaryota.
DR   HOGENOM; CLU_010194_44_0_1; -.
DR   InParanoid; A2RVM0; -.
DR   OMA; PAKCEQL; -.
DR   PhylomeDB; A2RVM0; -.
DR   PRO; PR:A2RVM0; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; A2RVM0; baseline and differential.
DR   Genevisible; A2RVM0; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0009706; C:chloroplast inner membrane; IDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Chloroplast; Membrane; Oxidoreductase; Plastid;
KW   Plastid inner membrane; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..322
FT                   /note="Short-chain dehydrogenase TIC 32, chloroplastic"
FT                   /id="PRO_0000413676"
FT   REGION          298..314
FT                   /note="Interaction with calmodulin"
FT                   /evidence="ECO:0000250|UniProtKB:Q6RVV4"
FT   ACT_SITE        192
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00334"
FT   BINDING         36..42
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KES3"
FT   BINDING         88..89
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KES3"
FT   BINDING         115
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KES3"
FT   BINDING         136
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KES3"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KES3"
FT   VAR_SEQ         139..148
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_041954"
FT   VAR_SEQ         191..192
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_041955"
FT   CONFLICT        217
FT                   /note="K -> E (in Ref. 3; BAE99458)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   322 AA;  34740 MW;  22B3DF0CA39B8A10 CRC64;
     MWFFGSKGAS GFSSRSTAEE VTHGVDGTGL TAIVTGASSG IGVETARVLS LRGVHVVMAV
     RNTDSGAKVK EDIVKQVPGA KLDVMELDLS SMQSVRKFAS EYKSTGLPLN LLINNAGIMA
     CPFMLSKDNI ELQFATNHLG HFLLTKLLLD TMKSTSRESK REGRIVNLSS EAHRFSYPEG
     VRFDKINDKS SYSSMRAYGQ SKLCNVLHAN ELTKQLKEDG VNITANSLHP GAIMTNLGRY
     FNPYLAVAVG AVAKYILKSV PQGAATTCYV ALNPQVAGVS GEYFQDSNIA KPLPLVKDTE
     LAKKVWDFST KLTDSQSGES SS
 
 
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