TI222_ARATH
ID TI222_ARATH Reviewed; 210 AA.
AC Q94EH2; Q9SZ09;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Chloroplastic import inner membrane translocase subunit TIM22-2;
DE AltName: Full=Hypothetical outer plastid envelope protein of 20 kDa {ECO:0000303|PubMed:24248378};
DE Short=Hypothetical protein 20 {ECO:0000303|PubMed:24248378};
GN Name=TIM22-2; Synonyms=HP20 {ECO:0000303|PubMed:24248378};
GN OrderedLocusNames=At4g26670; ORFNames=F10M23.10;
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 [MRNA].
RX PubMed=17098851; DOI=10.1104/pp.106.090688;
RA Murcha M.W., Elhafez D., Lister R., Tonti-Filippini J., Baumgartner M.,
RA Philippar K., Carrie C., Mokranjac D., Soll J., Whelan J.;
RT "Characterization of the preprotein and amino acid transporter gene family
RT in Arabidopsis.";
RL Plant Physiol. 143:199-212(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12692332; DOI=10.1104/pp.102.016808;
RA Murcha M.W., Lister R., Ho A.Y., Whelan J.;
RT "Identification, expression, and import of components 17 and 23 of the
RT inner mitochondrial membrane translocase from Arabidopsis.";
RL Plant Physiol. 131:1737-1747(2003).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=14730085; DOI=10.1104/pp.103.033910;
RA Lister R., Chew O., Lee M.N., Heazlewood J.L., Clifton R., Parker K.L.,
RA Millar A.H., Whelan J.;
RT "A transcriptomic and proteomic characterization of the Arabidopsis
RT mitochondrial protein import apparatus and its response to mitochondrial
RT dysfunction.";
RL Plant Physiol. 134:777-789(2004).
RN [8]
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 [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, SUBUNIT, AND
RP INTERACTION WITH CEQORH.
RC STRAIN=cv. Columbia;
RX PubMed=24248378; DOI=10.1073/pnas.1319648110;
RA Rossig C., Reinbothe C., Gray J., Valdes O., von Wettstein D.,
RA Reinbothe S.;
RT "Three proteins mediate import of transit sequence-less precursors into the
RT inner envelope of chloroplasts in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19962-19967(2013).
CC -!- FUNCTION: Together with HP30-1 and HP30-2, triggers the import and
CC insertion of transit sequence-less multi-pass transmembrane proteins
CC (e.g. CEQORH) into the chloroplastic inner membrane.
CC {ECO:0000269|PubMed:24248378}.
CC -!- SUBUNIT: Homodimer. Probable component of a protein-conducting channel
CC made of HP30-1, HP30-2 and HP20 that mediates the import of transit
CC sequence-less proteins into the chloroplastic inner membrane. Interacts
CC with CEQORH. {ECO:0000269|PubMed:24248378}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000269|PubMed:24248378}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in young cotyledons, roots, leaves and
CC flowers. {ECO:0000269|PubMed:12692332, ECO:0000269|PubMed:14730085}.
CC -!- DEVELOPMENTAL STAGE: Peak of expression during cotyledon development.
CC {ECO:0000269|PubMed:12692332}.
CC -!- DISRUPTION PHENOTYPE: Impaired import of CEQORH in chloroplast inner
CC membranes. {ECO:0000269|PubMed:24248378}.
CC -!- SIMILARITY: Belongs to the Tim17/Tim22/Tim23 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB36513.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79522.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF410323; AAK95309.1; -; mRNA.
DR EMBL; AL035440; CAB36513.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161565; CAB79522.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85235.1; -; Genomic_DNA.
DR EMBL; AY102132; AAM26699.1; -; mRNA.
DR EMBL; AY088301; AAM65840.1; -; mRNA.
DR EMBL; DQ405270; ABD64059.1; -; mRNA.
DR PIR; T04790; T04790.
DR RefSeq; NP_567754.1; NM_118801.4.
DR AlphaFoldDB; Q94EH2; -.
DR SMR; Q94EH2; -.
DR STRING; 3702.AT4G26670.1; -.
DR TCDB; 3.A.8.1.4; the mitochondrial protein translocase (mpt) family.
DR iPTMnet; Q94EH2; -.
DR PaxDb; Q94EH2; -.
DR PRIDE; Q94EH2; -.
DR ProteomicsDB; 234297; -.
DR DNASU; 828774; -.
DR EnsemblPlants; AT4G26670.1; AT4G26670.1; AT4G26670.
DR GeneID; 828774; -.
DR Gramene; AT4G26670.1; AT4G26670.1; AT4G26670.
DR KEGG; ath:AT4G26670; -.
DR Araport; AT4G26670; -.
DR TAIR; locus:2116367; AT4G26670.
DR eggNOG; KOG1652; Eukaryota.
DR HOGENOM; CLU_083527_0_0_1; -.
DR InParanoid; Q94EH2; -.
DR OMA; PAVCLFR; -.
DR OrthoDB; 1456214at2759; -.
DR PhylomeDB; Q94EH2; -.
DR PRO; PR:Q94EH2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94EH2; baseline and differential.
DR Genevisible; Q94EH2; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009707; C:chloroplast outer membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IEA:InterPro.
DR GO; GO:0045036; P:protein targeting to chloroplast; IMP:UniProtKB.
DR InterPro; IPR039175; TIM22.
DR PANTHER; PTHR14110; PTHR14110; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Membrane; Plastid; Plastid outer membrane; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..210
FT /note="Chloroplastic import inner membrane translocase
FT subunit TIM22-2"
FT /id="PRO_0000420935"
FT TRANSMEM 37..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 210 AA; 21811 MW; F0300E3B7451053C CRC64;
MAANDSSNAI DIDGNLDSDS NLNTDGDEAT DNDSSKALVT IPAPAVCLFR FAGDAAGGAV
MGSIFGYGSG LFKKKGFKGS FADAGQSAKT FAVLSGVHSL VVCLLKQIRG KDDAINVGVA
GCCTGLALSF PGAPQALLQS CLTFGAFSFI LEGLNKRQTA LAHSVSLRHQ TGLFQDHHRA
LPLSLALPIP EEIKGAFSSF CKSLAKPRKF
