TIC62_PEA
ID TIC62_PEA Reviewed; 534 AA.
AC Q8SKU2;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Protein TIC 62, chloroplastic;
DE AltName: Full=Translocon at the inner envelope membrane of chloroplasts 62;
DE Short=PsTIC62;
DE Flags: Precursor;
GN Name=TIC62;
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 385-394 AND 500-507,
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TIC40; TIC55; TIC110
RP AND PETH/FNR.
RX PubMed=12426385; DOI=10.1093/emboj/cdf621;
RA Kuechler M., Decker S., Hoermann F., Soll J., Heins L.;
RT "Protein import into chloroplasts involves redox-regulated proteins.";
RL EMBO J. 21:6136-6145(2002).
RN [2]
RP INTERACTION WITH 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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TIC110 AND PETH/FNR.
RX PubMed=18180301; DOI=10.1074/jbc.m706719200;
RA Stengel A., Benz P., Balsera M., Soll J., Boelter B.;
RT "TIC62 redox-regulated translocon composition and dynamics.";
RL J. Biol. Chem. 283:6656-6667(2008).
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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 383-408 IN COMPLEX WITH PETH/FNR.
RX PubMed=20974920; DOI=10.1073/pnas.1009124107;
RA Alte F., Stengel A., Benz J.P., Petersen E., Soll J., Groll M., Bolter B.;
RT "Ferredoxin:NADPH oxidoreductase is recruited to thylakoids by binding to a
RT polyproline type II helix in a pH-dependent manner.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:19260-19265(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:12426385,
CC ECO:0000269|PubMed:18180301}.
CC -!- SUBUNIT: Part of the Tic complex. Interacts with TIC40, TIC110 and
CC TIC55. Interacts (via C-terminus) with PETH/FNR.
CC {ECO:0000269|PubMed:12426385, ECO:0000269|PubMed:17035502,
CC ECO:0000269|PubMed:18180301, ECO:0000269|PubMed:20974920}.
CC -!- INTERACTION:
CC Q8SKU2; P10933: PETH; NbExp=5; IntAct=EBI-15606082, EBI-931306;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:12426385, ECO:0000269|PubMed:18180301}; Peripheral
CC membrane protein {ECO:0000305}. Plastid, chloroplast stroma.
CC Note=Shuttles between the membranes and the stroma, depending on the
CC redox state of the plastidic NADP(+)/NADPH pool.
CC {ECO:0000269|PubMed:18180301}.
CC -!- DOMAIN: The C-terminus (346-534) is specific for the interaction with
CC PETH/FNR.
CC -!- DOMAIN: The central region (247-346) is sufficient for binding to the
CC Tic complex.
CC -!- DOMAIN: The N-terminus has a dehydrogenase activity in vitro.
CC -!- MISCELLANEOUS: Dissociates from the Tic complex after addition of
CC NADPH, while addition of NADP(+) reduces the interaction with PETH/FNR.
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DR EMBL; AJ344551; CAC87810.2; -; mRNA.
DR PDB; 3MHP; X-ray; 1.70 A; C=383-408.
DR PDBsum; 3MHP; -.
DR AlphaFoldDB; Q8SKU2; -.
DR SMR; Q8SKU2; -.
DR DIP; DIP-59467N; -.
DR IntAct; Q8SKU2; 2.
DR TCDB; 3.A.9.1.1; the chloroplast envelope protein translocase (cept or tic-toc) family.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0098807; C:chloroplast thylakoid membrane protein complex; IEA:EnsemblPlants.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR044719; TIC62.
DR PANTHER; PTHR47285; PTHR47285; 2.
DR Pfam; PF13460; NAD_binding_10; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Membrane; Plastid;
KW Plastid inner membrane; Protein transport; Repeat; Transit peptide;
KW Transport.
FT TRANSIT 1..64
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 65..534
FT /note="Protein TIC 62, chloroplastic"
FT /id="PRO_5000067772"
FT REPEAT 387..408
FT /note="1"
FT REPEAT 450..471
FT /note="2"
FT REPEAT 511..532
FT /note="3"
FT REGION 50..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..532
FT /note="3 X 22 AA approximate repeats"
FT COMPBIAS 50..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 91..120
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT TURN 390..393
FT /evidence="ECO:0007829|PDB:3MHP"
SQ SEQUENCE 534 AA; 56901 MW; 9D3DB5EF4ECA7008 CRC64;
MPMEVFSLTS TAIPSTLTRR DTAADKPSPH LNLSKYSHFM RYPLTTTLTN NRIRSSSSSS
SSIRAQASGS TKSSTAEGIP EKTDSKDDNL VFVAGATGKV GSRTVRELIK LGFKVRAGVR
NAQKAGALVQ SVKQLKLDGA SGGGEAVEKL EIVECDLEKA DQIGSALGNA STVICAIGAS
EKEIFDITGP CRIDYRATKN LVDAATVAKV NHFILVTSLG TNKFGLPAAI LNLFWGVLIW
KRKAEEALLA SGIPYTIVRP GGMERPTDAY KETHNVTLST EDTLFGGQVS NLQVAELMAI
MAKNPDLSYC KIVEVIAETT APLTPAEKLL TRIPSQRPYI PSPKKVQKAD TATVSNTGPS
ANVVAEVPSI APQKETASKP VAKTEQPLSP YTAYDDLKPP SSPSPTKPSE KKQINISDAV
PTPISSDTPS SIQEIDGISQ TTSSSKGKES LSPYAAYPDL KPPSSPSPSV PTTSLSKRDT
VVVSSNGPAQ LSVEDTPKNE EQHLHEPKSR PLSPYAMYED LKPPASPSPS FRKS
