TI110_ARATH
ID TI110_ARATH Reviewed; 1016 AA.
AC Q8LPR9; Q0WMF8; Q8LPG5; Q9LMI9; Q9M9Z7;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Protein TIC110, chloroplastic;
DE AltName: Full=Translocon at the inner envelope membrane of chloroplasts 110;
DE Short=AtTIC110;
DE Flags: Precursor;
GN Name=TIC110; OrderedLocusNames=At1g06950; ORFNames=F10K1.33, F4H5.1;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 823-1016.
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 [5]
RP TOPOLOGY.
RX PubMed=9632730; DOI=10.1074/jbc.273.26.16583;
RA Jackson D.T., Froehlich J.E., Keegstra K.;
RT "The hydrophilic domain of Tic110, an inner envelope membrane component of
RT the chloroplastic protein translocation apparatus, faces the stromal
RT compartment.";
RL J. Biol. Chem. 273:16583-16588(1998).
RN [6]
RP FUNCTION.
RX PubMed=12032074; DOI=10.1093/emboj/21.11.2616;
RA Heins L., Mehrle A., Hemmler R., Wagner R., Kuechler M., Hoermann F.,
RA Sveshnikov D., Soll J.;
RT "The preprotein conducting channel at the inner envelope membrane of
RT plastids.";
RL EMBO J. 21:2616-2625(2002).
RN [7]
RP FUNCTION, AND TOPOLOGY.
RX PubMed=12874276; DOI=10.1074/jbc.m306367200;
RA Inaba T., Li M., Alvarez-Huerta M., Kessler F., Schnell D.J.;
RT "atTic110 functions as a scaffold for coordinating the stromal events of
RT protein import into chloroplasts.";
RL J. Biol. Chem. 278:38617-38627(2003).
RN [8]
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 [9]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP HSP93; TIC40 AND TOC COMPLEX.
RX PubMed=15829604; DOI=10.1105/tpc.105.030700;
RA Inaba T., Alvarez-Huerta M., Li M., Bauer J., Ewers C., Kessler F.,
RA Schnell D.J.;
RT "Arabidopsis tic110 is essential for the assembly and function of the
RT protein import machinery of plastids.";
RL Plant Cell 17:1482-1496(2005).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15659100; DOI=10.1111/j.1365-313x.2004.02307.x;
RA Kovacheva S., Bedard J., Patel R., Dudley P., Twell D., Rios G., Koncz C.,
RA Jarvis P.;
RT "In vivo studies on the roles of Tic110, Tic40 and Hsp93 during chloroplast
RT protein import.";
RL Plant J. 41:412-428(2005).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=17060496; DOI=10.1083/jcb.200605162;
RA Li M., Schnell D.J.;
RT "Reconstitution of protein targeting to the inner envelope membrane of
RT chloroplasts.";
RL J. Cell Biol. 175:249-259(2006).
RN [12]
RP IDENTIFICATION IN TIC/TOC SUPERCOMPLEX.
RX PubMed=17144891; DOI=10.1111/j.1365-313x.2006.02944.x;
RA Chen K.Y., Li H.M.;
RT "Precursor binding to an 880-kDa Toc complex as an early step during active
RT import of protein into chloroplasts.";
RL Plant J. 49:149-158(2007).
RN [13]
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 [14]
RP INTERACTION WITH HSP70.
RX PubMed=20484004; DOI=10.1105/tpc.109.071415;
RA Su P.H., Li H.M.;
RT "Stromal Hsp70 is important for protein translocation into pea and
RT Arabidopsis chloroplasts.";
RL Plant Cell 22:1516-1531(2010).
RN [15]
RP INTERACTION WITH LTD.
RX PubMed=21505433; DOI=10.1038/ncomms1278;
RA Ouyang M., Li X., Ma J., Chi W., Xiao J., Zou M., Chen F., Lu C., Zhang L.;
RT "LTD is a protein required for sorting light-harvesting chlorophyll-binding
RT proteins to the chloroplast SRP pathway.";
RL Nat. Commun. 2:277-277(2011).
RN [16]
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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-52, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER SER-51, 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. Forms
CC a voltage-dependent cation-selective channel at the inner envelope of
CC chloroplasts, which specifically responds to a transit peptide.
CC Associates with both the precursor and mature forms of the preprotein.
CC {ECO:0000269|PubMed:12032074, ECO:0000269|PubMed:12874276,
CC ECO:0000269|PubMed:15659100, ECO:0000269|PubMed:15829604}.
CC -!- SUBUNIT: Part of the Tic complex. Interacts with HSP70, HSP93 and
CC TIC40. Interacts with the Toc complex components TOC33, TOC75 and
CC TOC159. Interacts with LTD. {ECO:0000269|PubMed:15829604,
CC ECO:0000269|PubMed:17144891, ECO:0000269|PubMed:20484004,
CC ECO:0000269|PubMed:21505433}.
CC -!- INTERACTION:
CC Q8LPR9; Q9FI56: CLPC1; NbExp=4; IntAct=EBI-639092, EBI-2297694;
CC Q8LPR9; Q9FMD5: TIC40; NbExp=3; IntAct=EBI-639092, EBI-639157;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, flowers, leaves, stems and
CC roots. {ECO:0000269|PubMed:15033972, ECO:0000269|PubMed:15659100,
CC ECO:0000269|PubMed:15829604}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC {ECO:0000269|PubMed:15659100}.
CC -!- DOMAIN: An internal domain (143-652) is sufficient for assembly into
CC supercomplex with Toc complex.
CC -!- DOMAIN: Residues 235-420 contain a binding site for preprotein transit
CC peptides.
CC -!- DISRUPTION PHENOTYPE: Embryo lethal. {ECO:0000269|PubMed:15659100,
CC ECO:0000269|PubMed:15829604}.
CC -!- MISCELLANEOUS: The region 143-1016 is indicated to be located in the
CC stroma (PubMed:12874276, PubMed:9632730) while the homologous region in
CC pea TIC110 contains probably 4 trans-membrane domains resulting in 2
CC regions in the intermembrane space localized to form supercomplexes
CC with the TOC machinery and to receive the transit peptide of
CC preproteins. {ECO:0000305|PubMed:12874276, ECO:0000305|PubMed:9632730}.
CC -!- MISCELLANEOUS: Inserts into the inner envelope membrane from the stroma
CC after import from the cytoplasm.
CC -!- SIMILARITY: Belongs to the chloroplast envelope anion channel-forming
CC Tic110 (TC 1.A.18) family. {ECO:0000305}.
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DR EMBL; AC011001; AAF63131.1; -; Genomic_DNA.
DR EMBL; AC067971; AAF82224.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28057.1; -; Genomic_DNA.
DR EMBL; AY094426; AAM19799.1; -; mRNA.
DR EMBL; AY099850; AAM20701.1; -; mRNA.
DR EMBL; AK229869; BAF01698.1; -; mRNA.
DR PIR; B86204; B86204.
DR RefSeq; NP_172176.1; NM_100568.4.
DR AlphaFoldDB; Q8LPR9; -.
DR BioGRID; 22446; 9.
DR IntAct; Q8LPR9; 9.
DR MINT; Q8LPR9; -.
DR STRING; 3702.AT1G06950.1; -.
DR TCDB; 3.A.9.1.2; the chloroplast envelope protein translocase (cept or tic-toc) family.
DR iPTMnet; Q8LPR9; -.
DR SwissPalm; Q8LPR9; -.
DR PaxDb; Q8LPR9; -.
DR PRIDE; Q8LPR9; -.
DR ProMEX; Q8LPR9; -.
DR ProteomicsDB; 232456; -.
DR EnsemblPlants; AT1G06950.1; AT1G06950.1; AT1G06950.
DR GeneID; 837205; -.
DR Gramene; AT1G06950.1; AT1G06950.1; AT1G06950.
DR KEGG; ath:AT1G06950; -.
DR Araport; AT1G06950; -.
DR TAIR; locus:2007437; AT1G06950.
DR eggNOG; ENOG502QS6A; Eukaryota.
DR HOGENOM; CLU_006871_0_0_1; -.
DR InParanoid; Q8LPR9; -.
DR OMA; PTEYAQK; -.
DR OrthoDB; 172216at2759; -.
DR PhylomeDB; Q8LPR9; -.
DR PRO; PR:Q8LPR9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LPR9; baseline and differential.
DR Genevisible; Q8LPR9; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0031897; C:Tic complex; TAS:TAIR.
DR GO; GO:0061927; C:TOC-TIC supercomplex I; IDA:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0045037; P:protein import into chloroplast stroma; IMP:TAIR.
DR InterPro; IPR031610; TIC110.
DR PANTHER; PTHR34935; PTHR34935; 1.
DR Pfam; PF16940; Tic110; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chloroplast; Membrane; Plastid; Plastid inner membrane;
KW Protein transport; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 52..1016
FT /note="Protein TIC110, chloroplastic"
FT /id="PRO_0000413668"
FT TOPO_DOM 52..95
FT /note="Stromal"
FT /evidence="ECO:0000250"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..118
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000250"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..259
FT /note="Stromal"
FT /evidence="ECO:0000250"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..368
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000250"
FT TRANSMEM 369..386
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 387..632
FT /note="Stromal"
FT /evidence="ECO:0000250"
FT TRANSMEM 633..650
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 651..719
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000250"
FT TRANSMEM 720..736
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 737..1016
FT /note="Stromal"
FT /evidence="ECO:0000250"
FT REGION 654..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 220
FT /note="K -> N (in Ref. 3; AAM20701)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1016 AA; 112121 MW; 814CCDE07EB5D0EA CRC64;
MNPSLVTAIN APISPSPRSP LLSHFLPTLP HRFSKSECLS RRRYRVSFPR SSAASSDQLS
VSTQAKNPGI HGNKKELTGL QPIVEKMTPP VRLATSAVVL AASLATGYGL GLRLAGSRNI
AFGGAAVAGA AGGAVVYALN SAVPEVAAIS LHNYVAEFED PASVTKDDVE KIADRYGVNK
GDEAFQAEIC DIYCRYVTSV LPTEGQSLKG DEVAKIVKFK NALGIDEPDA AAMHMEIGRR
IFRQRLETGE REGDAEQRRA FMRLVYVSAL VFGDASSFLL PWKRVLKVTD AQVEIAIREN
AKQLYAERLK LVGRDINVEN LVDLRKSQLS FKLSDELAED LFREHTRKVV VENISSALSI
LKSRTRAAKS LASVVEELEK VLEFNNLLVS LKSHSEADQF ARGVGPISLI GDESDFERRM
DDLKLLYRAY VTDALSGGRL EENKLVAMSQ LRNILGLGKR EAEAISVDVT SKSYRKRLAN
AVSSGDLEAQ DSKAKYLQKL CEELHFDAQK AGAIHEEIYR QKLQQCVTDG ELSDDNVAAL
LRLRVMLCIP QQTVDTAHAE ICGTIFEKVV RDAISSGVDG YDAETRKSVR KAAHGLRLSR
ETAMSIASKA VRRVFTNYIR RARAAENRTD SAKELKKMIA FNTLVVTEMV ADIKGESSDK
APEEDPVQEK EEDDEDEEWG SLESLRKTRP DKELAEKMGK PGQTEITLKD DLPDRDRIDL
YKTYLLYCVT GEVTRIPFGA QITTKRDDSE YLLLNQLGGI LGLSSKEIVN IHVGLAEQAF
RQQAEVILAD GQLTKARVEQ LDELQKQVGL PQPQAEKVIK NITTTKMANA IETAVNQGRL
NIKQIRELKE ANVSLDSMIA VSLREKLFKK TVSDIFSSGT GEFDETEVYQ TIPSDLSIDV
EKAKRVVHDL AQSRLSNSLV QAVALLRQRN SKGVVLSLND LLACDKAVPA EPMSWEVSEE
LSDLYAIYSK SDPKPAPEKV LRLQYLLGID DSTATALREM EDGALSSAAE EGNFVF
