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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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