TIC55_ARATH
ID TIC55_ARATH Reviewed; 539 AA.
AC Q9SK50; Q56YA0;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Protein TIC 55, chloroplastic;
DE AltName: Full=Translocon at the inner envelope membrane of chloroplasts 55;
DE Short=AtTIC55;
DE AltName: Full=Translocon at the inner envelope membrane of chloroplasts 55-II;
DE Flags: Precursor;
GN Name=TIC55; Synonyms=TIC55-II; OrderedLocusNames=At2g24820;
GN ORFNames=F27C12.26;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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] OF 173-477.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION BY LIGHT, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=19995737; DOI=10.1093/mp/ssp079;
RA Boij P., Patel R., Garcia C., Jarvis P., Aronsson H.;
RT "In vivo studies on the roles of Tic55-related proteins in chloroplast
RT protein import in Arabidopsis thaliana.";
RL Mol. Plant 2:1397-1409(2009).
RN [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-51, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER SER-50, 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).
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:19995737}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00628};
CC -!- SUBUNIT: Part of the Tic complex. Interacts with TIC62 and TIC110 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:19995737}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19995737}.
CC -!- TISSUE SPECIFICITY: Highly expressed in green tissues and very low
CC levels in non-photosynthetic tissues such as roots and etiolated
CC seedlings. {ECO:0000269|PubMed:15033972, ECO:0000269|PubMed:19995737}.
CC -!- INDUCTION: Up-regulated by light. {ECO:0000269|PubMed:19995737}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:19995737}.
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DR EMBL; AC006585; AAD23030.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07632.1; -; Genomic_DNA.
DR EMBL; AK221423; BAD94416.1; -; mRNA.
DR PIR; H84640; H84640.
DR RefSeq; NP_180055.1; NM_128041.4.
DR AlphaFoldDB; Q9SK50; -.
DR SMR; Q9SK50; -.
DR BioGRID; 2371; 1.
DR STRING; 3702.AT2G24820.1; -.
DR iPTMnet; Q9SK50; -.
DR PaxDb; Q9SK50; -.
DR PRIDE; Q9SK50; -.
DR ProMEX; Q9SK50; -.
DR ProteomicsDB; 234299; -.
DR EnsemblPlants; AT2G24820.1; AT2G24820.1; AT2G24820.
DR GeneID; 817019; -.
DR Gramene; AT2G24820.1; AT2G24820.1; AT2G24820.
DR KEGG; ath:AT2G24820; -.
DR Araport; AT2G24820; -.
DR TAIR; locus:2047329; AT2G24820.
DR eggNOG; ENOG502QT2X; Eukaryota.
DR HOGENOM; CLU_003927_0_0_1; -.
DR InParanoid; Q9SK50; -.
DR OMA; VWIWMSH; -.
DR OrthoDB; 1199207at2759; -.
DR PhylomeDB; Q9SK50; -.
DR BioCyc; ARA:AT2G24820-MON; -.
DR PRO; PR:Q9SK50; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SK50; baseline and differential.
DR Genevisible; Q9SK50; 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:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010277; F:chlorophyllide a oxygenase [overall] activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0045036; P:protein targeting to chloroplast; IMP:TAIR.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR013626; PaO.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR Pfam; PF08417; PaO; 1.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Acetylation; Chloroplast; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Plastid; Plastid inner membrane; Protein transport;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 51..539
FT /note="Protein TIC 55, chloroplastic"
FT /id="PRO_0000413678"
FT TOPO_DOM 51..482
FT /note="Stromal"
FT /evidence="ECO:0000250"
FT TRANSMEM 483..500
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 501..504
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000250"
FT TRANSMEM 505..527
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 528..539
FT /note="Stromal"
FT /evidence="ECO:0000250"
FT DOMAIN 88..193
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT MOTIF 467..470
FT /note="Redox-active motif"
FT BINDING 129
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 131
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 148
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 151
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 242
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 247
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT MOD_RES 51
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 539 AA; 60608 MW; A86A38E914AE66A1 CRC64;
MAVPFLSSSL QLTPTSPILF TKVTPTPIIH NHRSTCTIPT KPRLRLLRRS AVAGTAVSDQ
TEGGGDVLLN PEEEKRVEVA DYDWTEEWYP LYLTKNVPED APLGLTVYDR QIVLYKDGEG
TLRCYEDRCP HRLAKLSEGQ LIDGRLECLY HGWQFEGEGK CVKIPQLPAS AKIPKAACVK
TYEVKDSQGV VWVWMSTKTP PNPEKLPWFE NFARPGFFDI STTHELPYDH SILLENLMDP
AHVPISHDRT DFTAKREDAQ PLVFEVTERS NRGFAGTWGR EKEGGKGSNL LRFDAPCVLQ
NNREFEGKDG VKNYFSGLFL CRPTGQGKSM LIVRFGVTKR SPLVSVLPQW FWHQNACKVF
EQDMGFLSSQ NEVLMKEKVP TKDLYLNLKS SDTWVAEYRK WMDKVGHGMP YHFGHRTISL
PKVPPVVEHA PAGLIAALSA SYPAKGGIGT MHAPNLANRY FRHIIHCRSC SNVIKSFELW
KNILSATAVA LTALAILVVS RQWKAVLLGS AALCSAAAYT CLRAINLNTN NFIRTHRRL
