TI100_ARATH
ID TI100_ARATH Reviewed; 871 AA.
AC Q8LPR8; Q9FNJ7;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Protein TIC 100 {ECO:0000303|PubMed:23372012};
DE AltName: Full=Protein EMBRYO DEFECTIVE 1211 {ECO:0000303|PubMed:15266054};
DE AltName: Full=Translocon at the inner envelope membrane of chloroplasts 100 {ECO:0000303|PubMed:23372012};
DE Short=AtTIC100 {ECO:0000303|PubMed:23372012};
GN Name=TIC100 {ECO:0000303|PubMed:23372012};
GN Synonyms=EMB1211 {ECO:0000303|PubMed:15266054};
GN OrderedLocusNames=At5g22640 {ECO:0000312|Araport:AT5G22640};
GN ORFNames=MDJ22.6 {ECO:0000312|EMBL:BAB11670.1};
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 IDENTIFICATION.
RX PubMed=15266054; DOI=10.1104/pp.104.045179;
RA Tzafrir I., Pena-Muralla R., Dickerman A., Berg M., Rogers R., Hutchens S.,
RA Sweeney T.C., McElver J., Aux G., Patton D., Meinke D.;
RT "Identification of genes required for embryo development in Arabidopsis.";
RL Plant Physiol. 135:1206-1220(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-649, AND IDENTIFICATION BY
RP 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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=20738804; DOI=10.1111/j.1399-3054.2010.01407.x;
RA Liang Q., Lu X., Jiang L., Wang C., Fan Y., Zhang C.;
RT "EMB1211 is required for normal embryo development and influences
RT chloroplast biogenesis in Arabidopsis.";
RL Physiol. Plantarum 140:380-394(2010).
RN [7]
RP FUNCTION, COMPONENT OF THE 1-MD COMPLEX, SUBUNIT, IDENTIFICATION BY MASS
RP SPECTROMETRY, DEAMIDATION AT ASN-238, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23372012; DOI=10.1126/science.1229262;
RA Kikuchi S., Bedard J., Hirano M., Hirabayashi Y., Oishi M., Imai M.,
RA Takase M., Ide T., Nakai M.;
RT "Uncovering the protein translocon at the chloroplast inner envelope
RT membrane.";
RL Science 339:571-574(2013).
CC -!- FUNCTION: Involved in protein precursor import into chloroplasts. May
CC be part of an intermediate translocation complex acting as a protein-
CC conducting channel at the inner envelope (PubMed:23372012). Plays an
CC important role during embryogenesis and chloroplast biogenesis
CC (PubMed:20738804). {ECO:0000269|PubMed:20738804,
CC ECO:0000269|PubMed:23372012}.
CC -!- SUBUNIT: Part of the Tic complex. Component of the 1-MD complex,
CC composed of TIC20-I, TIC214, TIC100 and TIC56. Interacts with the
CC translocating preproteins. Hydrolysis of ATP is essential for the
CC formation of this complex (PubMed:23372012). The 1-MD complex interacts
CC with TIC21 (By similarity). {ECO:0000250|UniProtKB:Q8GZ79,
CC ECO:0000269|PubMed:23372012}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:23372012}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8LPR8-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in ovules, and moderately
CC expressed in leaves and siliques. {ECO:0000269|PubMed:20738804}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing embryo.
CC {ECO:0000269|PubMed:20738804}.
CC -!- DISRUPTION PHENOTYPE: Severe defects during embryogenesis, producing
CC abnormal embryos and thereby leading to a lethality of young seedlings.
CC {ECO:0000269|PubMed:20738804, ECO:0000269|PubMed:23372012}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11670.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB006699; BAB11670.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93056.1; -; Genomic_DNA.
DR EMBL; AY094427; AAM19800.1; -; mRNA.
DR RefSeq; NP_197656.2; NM_122170.3. [Q8LPR8-1]
DR AlphaFoldDB; Q8LPR8; -.
DR STRING; 3702.AT5G22640.1; -.
DR TCDB; 3.A.9.1.2; the chloroplast envelope protein translocase (cept or tic-toc) family.
DR iPTMnet; Q8LPR8; -.
DR PaxDb; Q8LPR8; -.
DR PRIDE; Q8LPR8; -.
DR ProMEX; Q8LPR8; -.
DR EnsemblPlants; AT5G22640.1; AT5G22640.1; AT5G22640. [Q8LPR8-1]
DR GeneID; 832327; -.
DR Gramene; AT5G22640.1; AT5G22640.1; AT5G22640. [Q8LPR8-1]
DR KEGG; ath:AT5G22640; -.
DR Araport; AT5G22640; -.
DR TAIR; locus:2162469; AT5G22640.
DR eggNOG; ENOG502QVAX; Eukaryota.
DR InParanoid; Q8LPR8; -.
DR OMA; WADEEEW; -.
DR OrthoDB; 304871at2759; -.
DR PhylomeDB; Q8LPR8; -.
DR PRO; PR:Q8LPR8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LPR8; baseline and differential.
DR Genevisible; Q8LPR8; 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; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0045037; P:protein import into chloroplast stroma; IDA:TAIR.
DR InterPro; IPR003409; MORN.
DR Pfam; PF02493; MORN; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Coiled coil; Membrane; Phosphoprotein;
KW Plastid; Plastid inner membrane; Protein transport; Reference proteome;
KW Repeat; Transport.
FT CHAIN 1..871
FT /note="Protein TIC 100"
FT /id="PRO_0000431667"
FT REPEAT 219..239
FT /note="MORN 1"
FT /evidence="ECO:0000255"
FT REPEAT 243..257
FT /note="MORN 2"
FT /evidence="ECO:0000255"
FT REPEAT 337..352
FT /note="MORN 3"
FT /evidence="ECO:0000255"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 587..647
FT /evidence="ECO:0000255"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..706
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 238
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000269|PubMed:23372012"
FT MOD_RES 649
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 871 AA; 99954 MW; 0FF5C2C0A90B70FC CRC64;
MANEELTESQ QQEDPSQQLP NADEEKGSDS DSNSDSDASS QSSGDDFYIS ESENEAEGDN
TIFNYVRPSD IPPDPNANPE TNIRRFNRVL DGKRVKRMQE EEEDKYTFYE DLFDFPRDPE
RWKEQDLREI WADGPLEMTK PGWDPAWADE DDWDVVNDEI QEGRDPGIQP FYVPYRKPYP
AIPDNHYDIE NAKGVVEELD RIEEFLQWVS YIFPDGSSYE GTVWDDLAQG KGVYIAENGL
VRYEGEWLQN DMEGHGVIDV DIPDIEPIPG SKLEAKMRAE GRIIKRDYMT PEDRKWLEMD
VEDSVALTDG NFQVPFYENE EWVTQFGEKP EKGRYRYAGQ WKHSRMHGCG VYEVNERILY
GRFYFGELLE EEHGCTVDIC ALHSGLAEVA AAKARMFVNK PDGMIREERG PYGDPQHPYF
YEEDDVWMAP GFINQFYEVP EYWETYVGEV DQEREMWLNS FYKAPLRLPM PAELEHWWEN
VEVTPEFVLL NKEPEPDPND PSKLVQKEDP VILHTPTGRI INYVEDEKHG IRLFWQPPLE
EGEEVDPSKV EFLPLGFDEF YGKEVVVKKE HPIKSFVLGI EKSVKPMLDG LEKWTEEKKK
AYEERKEMIQ QELELVEAEI CLEEAIEDMD EELKKKEQEE EKKTEMGLTE EDEDVLVPVY
KEEKVVTAKE KIQENKQEEK YKDDDDEDDD DGDDDDDDDD DDDLGPSSFG SADKGRRNSP
FSSSSLSFAS CTLFPAVQSR LESSFLAWKQ HRAEPSKVNT GIIKGADTAS ASIHFPPLSS
NNARLKMGKV ANRGCVQRSY GSSRSQSQLM SLSRLLSCNA SSSSSPPDSS SSEYLKDSGL
WETPVGDMSV VLSLQIQTKC SDLFAETPAV S
