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TIC32_PEA
ID   TIC32_PEA               Reviewed;         316 AA.
AC   Q6RVV4;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, 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=PsTIC32 {ECO:0000303|PubMed:15180984};
GN   Name=TIC32 {ECO:0000303|PubMed:15180984};
GN   Synonyms=HP32 {ECO:0000303|PubMed:15286175},
GN   IEP32 {ECO:0000303|PubMed:15286175};
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 12-23 AND 176-194,
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH TIC110.
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   [2]
RP   PROTEIN SEQUENCE OF 10-23, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP   TIC22.
RX   PubMed=15286175; DOI=10.1242/jcs.01265;
RA   Nada A., Soll J.;
RT   "Inner envelope protein 32 is imported into chloroplasts by a novel
RT   pathway.";
RL   J. Cell Sci. 117:3975-3982(2004).
RN   [3]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
RP   CALMODULIN AND TIC110.
RX   PubMed=17035502; DOI=10.1073/pnas.0607150103;
RA   Chigri F., Hoermann F., Stamp A., Stammers D.K., Boelter B., Soll J.,
RA   Vothknecht U.C.;
RT   "Calcium regulation of chloroplast protein translocation is mediated by
RT   calmodulin binding to Tic32.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:16051-16056(2006).
RN   [4]
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. Has a
CC       NADPH-dependent dehydrogenase activity, but only after preincubation
CC       with lipids. {ECO:0000269|PubMed:17035502}.
CC   -!- SUBUNIT: Part of the Tic complex. Interacts with TIC110 (via N-
CC       terminus) and with calmodulin in a calcium-dependent manner. Interacts
CC       with TIC22 during import into chloroplast.
CC       {ECO:0000269|PubMed:15180984, ECO:0000269|PubMed:15286175,
CC       ECO:0000269|PubMed:17035502}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC       {ECO:0000269|PubMed:15180984, ECO:0000269|PubMed:15286175}.
CC   -!- DOMAIN: The N-terminus (1-10) forms an essential portion of the
CC       targeting information.
CC   -!- MISCELLANEOUS: NADPH and calmodulin binding is mutually exclusive.
CC       Dissociates from TIC110 after addition of NADPH.
CC   -!- MISCELLANEOUS: Imported into the chloroplast in the absence of a
CC       cleavable N-terminal pre-sequence. Not imported via the Toc complex.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AY488758; AAS38575.1; -; mRNA.
DR   AlphaFoldDB; Q6RVV4; -.
DR   SMR; Q6RVV4; -.
DR   DIP; DIP-61294N; -.
DR   IntAct; Q6RVV4; 3.
DR   EnsemblPlants; Psat6g193560.1; Psat6g193560.1.cds; Psat6g193560.
DR   Gramene; Psat6g193560.1; Psat6g193560.1.cds; Psat6g193560.
DR   GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
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   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Calmodulin-binding; Chloroplast; Direct protein sequencing; Membrane; NADP;
KW   Oxidoreductase; Plastid; Plastid inner membrane; Protein transport;
KW   Transport.
FT   CHAIN           1..316
FT                   /note="Short-chain dehydrogenase TIC 32, chloroplastic"
FT                   /id="PRO_0000413677"
FT   REGION          298..314
FT                   /note="Interaction with calmodulin"
FT                   /evidence="ECO:0000269|PubMed:17035502"
FT   ACT_SITE        193
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00334"
FT   BINDING         37..43
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KES3"
FT   BINDING         89..90
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KES3"
FT   BINDING         116
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KES3"
FT   BINDING         137
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KES3"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KES3"
SQ   SEQUENCE   316 AA;  34317 MW;  13E2009456492158 CRC64;
     MWPFSSKKGV SGFSGSSTAE QVTHGIDATG LTAIVTGASS GIGAETTRVL ALRGAHVIMG
     VRNMVAAKDV KDTILKDIPS AKVDAIELDL SSLDSVKKFA SEFNSSGRPL NILINNAGIM
     ACPFKLSKDN IELQFATNHI GHFLLTNLLL DTMKKTTRES KKEGRIVNVA SEAHRFAYPE
     GIRFDKINDQ SSYNNWRAYG QSKLANVLHA NQLTKHLKED GVNITANSLH PGTIVTNLFR
     HNSAVNGLIN VIGKLVLKNV QQGAATTCYV ALHPQVKGVS GEYFSDSNVY KTTPHGKDVD
     LAKKLWDFSI NLVKQK
 
 
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