TIC62_ARATH
ID TIC62_ARATH Reviewed; 641 AA.
AC Q8H0U5; Q9LHN0;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Protein TIC 62, chloroplastic {ECO:0000303|PubMed:12426385};
DE AltName: Full=Translocon at the inner envelope membrane of chloroplasts 62 {ECO:0000303|PubMed:12426385};
DE Short=AtTIC62 {ECO:0000303|PubMed:12426385};
DE Flags: Precursor;
GN Name=TIC62 {ECO:0000303|PubMed:12426385};
GN OrderedLocusNames=At3g18890 {ECO:0000312|Araport:AT3G18890};
GN ORFNames=MCB22.6 {ECO:0000312|EMBL:BAB03098.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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 FUNCTION.
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 [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-64, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER ARG-63, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
RP 3D-STRUCTURE MODELING.
RX PubMed=17374152; DOI=10.1186/1471-2148-7-43;
RA Balsera M., Stengel A., Soll J., Boelter B.;
RT "Tic62: a protein family from metabolism to protein translocation.";
RL BMC Evol. Biol. 7:43-43(2007).
RN [9]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION
RP WITH LFNR1 AND LFNR2, AND DISRUPTION PHENOTYPE.
RX PubMed=20040542; DOI=10.1105/tpc.109.069815;
RA Benz J.P., Stengel A., Lintala M., Lee Y.H., Weber A., Philippar K.,
RA Guegel I.L., Kaieda S., Ikegami T., Mulo P., Soll J., Boelter B.;
RT "Arabidopsis Tic62 and ferredoxin-NADP(H) oxidoreductase form light-
RT regulated complexes that are integrated into the chloroplast redox poise.";
RL Plant Cell 21:3965-3983(2009).
RN [10]
RP INTERACTION WITH LFNR1 AND LFNR2.
RX PubMed=20934402; DOI=10.1016/j.bbabio.2010.10.001;
RA Mulo P.;
RT "Chloroplast-targeted ferredoxin-NADP(+) oxidoreductase (FNR): structure,
RT function and location.";
RL Biochim. Biophys. Acta 1807:927-934(2011).
RN [11]
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 [12]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=26941088; DOI=10.1105/tpc.15.01027;
RA Yang C., Hu H., Ren H., Kong Y., Lin H., Guo J., Wang L., He Y., Ding X.,
RA Grabsztunowicz M., Mulo P., Chen T., Liu Y., Wu Z., Wu Y., Mao C., Wu P.,
RA Mo X.;
RT "LIGHT-INDUCED RICE1 regulates light-dependent attachment of LEAF-TYPE
RT FERREDOXIN-NADP+ OXIDOREDUCTASE to the thylakoid membrane in rice and
RT Arabidopsis.";
RL Plant Cell 28:712-728(2016).
CC -!- FUNCTION: Involved in protein precursor import into chloroplasts. Part
CC of the redox regulon consisting of TIC32, TIC 55 and TIC62
CC (PubMed:12426385). Acts as a membrane anchor of LFNR1 and LFNR2. Has a
CC NADPH-dependent dehydrogenase activity, but only after preincubation
CC with lipids (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:12426385}.
CC -!- SUBUNIT: Part of the Tic complex. Interacts with TIC110 and TIC55.
CC Interacts with LFNR1 and LFNR2. Component of high molecular weight
CC thylakoid LFNRs-containing protein complexes containing LIR1, LFNR1,
CC LFNR2, TIC62 and TROL proteins. {ECO:0000269|PubMed:20040542,
CC ECO:0000269|PubMed:20934402}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:20040542}; Peripheral membrane protein
CC {ECO:0000269|PubMed:20040542}. Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:20040542}. Plastid, chloroplast thylakoid
CC {ECO:0000269|PubMed:20040542}. Note=Shuttles between the membranes and
CC the stroma, depending on the redox state of the plastidic NADP(+)/NADPH
CC pool.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons and leaves, but not in
CC roots. {ECO:0000269|PubMed:15033972, ECO:0000269|PubMed:20040542}.
CC -!- DEVELOPMENTAL STAGE: Expressed from day 3 of seedling development and
CC continues throughout the development of photosynthetic tissues.
CC {ECO:0000269|PubMed:20040542}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but loss of membrane-bound
CC LFNR1 or LFNR2. {ECO:0000269|PubMed:20040542,
CC ECO:0000269|PubMed:26941088}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB03098.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP002039; BAB03098.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76164.1; -; Genomic_DNA.
DR EMBL; BT002039; AAN72050.1; -; mRNA.
DR EMBL; BT008403; AAP37762.1; -; mRNA.
DR RefSeq; NP_188519.2; NM_112775.4.
DR AlphaFoldDB; Q8H0U5; -.
DR SMR; Q8H0U5; -.
DR BioGRID; 6755; 2.
DR STRING; 3702.AT3G18890.1; -.
DR iPTMnet; Q8H0U5; -.
DR PaxDb; Q8H0U5; -.
DR PRIDE; Q8H0U5; -.
DR ProteomicsDB; 246466; -.
DR EnsemblPlants; AT3G18890.1; AT3G18890.1; AT3G18890.
DR GeneID; 821422; -.
DR Gramene; AT3G18890.1; AT3G18890.1; AT3G18890.
DR KEGG; ath:AT3G18890; -.
DR Araport; AT3G18890; -.
DR TAIR; locus:2087901; AT3G18890.
DR eggNOG; KOG1203; Eukaryota.
DR HOGENOM; CLU_025711_7_1_1; -.
DR InParanoid; Q8H0U5; -.
DR OMA; KLKIVEC; -.
DR OrthoDB; 1166292at2759; -.
DR PhylomeDB; Q8H0U5; -.
DR PRO; PR:Q8H0U5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8H0U5; baseline and differential.
DR Genevisible; Q8H0U5; 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; IEA:UniProtKB-SubCell.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0098807; C:chloroplast thylakoid membrane protein complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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; 1.
DR Pfam; PF13460; NAD_binding_10; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chloroplast; Membrane; NAD; Plastid; Plastid inner membrane;
KW Protein transport; Reference proteome; Repeat; Thylakoid; Transit peptide;
KW Transport.
FT TRANSIT 1..63
FT /note="Chloroplast"
FT /evidence="ECO:0000255, ECO:0007744|PubMed:22223895"
FT CHAIN 64..641
FT /note="Protein TIC 62, chloroplastic"
FT /id="PRO_0000413675"
FT REPEAT 376..397
FT /note="1"
FT REPEAT 444..465
FT /note="2"
FT REPEAT 532..553
FT /note="3"
FT REPEAT 617..638
FT /note="4"
FT REGION 328..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..638
FT /note="4 X 22 AA approximate repeats"
FT COMPBIAS 357..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 84..113
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT MOD_RES 64
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 641 AA; 68342 MW; D99F4FB95A79833A CRC64;
MEGTCFLRGQ PLTTIPSLPS RKGFLLQRWK TNRIVRFSGF KNHSVSGKSR SFDLSLRASG
PIRASSVVTE ASPTNLNSKE EDLVFVAGAT GKVGSRTVRE LLKLGFRVRA GVRSAQRAGS
LVQSVKEMKL QNTDEGTQPV EKLEIVECDL EKKDSIQPAL GNASVIICCI GASEKEISDI
TGPYRIDYLA TKNLVDAATS AKVNNFILVT SLGTNKFGFP AAILNLFWGV LCWKRKAEEA
LIESGLNYAI VRPGGMERPT DAYKETHNLT LALDDTLFGG QVSNLQVAEL LACMAKNPQL
SFSKIVEVVA ETTAPLTPIE KLLEKIPSKR PYVPPPKASV ATKEVKPVPT KPVTQEPTAP
KEDEAPPKEK NVKPRPLSPY ASYEDLKPPT SPIPNSTTSV SPAKSKEVDA TQVPVEANVV
PVPDSTSNVP VVEVKQVEEK KERPLSPYAR YENLKPPSSP SPTASSTRKS DSLSPGPTDS
DTDKSSTVAK TVTETAVATS VTETSVATSV PETAVATSVT ETAAPATSKM RPLSPYAIYA
DLKPPTSPTP ASTGPKEAAS VEDNSELPGG NNDVLKTVDG NLNTIPPSTP EAVPVVSSAI
DTSLASGDNT AQPKPRPLSP YTMYADMKPP TSPLPSPVTN H
