ID   TI143_ARATH             Reviewed;         112 AA.
AC   Q9LYY2;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit TIM14-3;
DE   AltName: Full=Chaperone DnaJ-domain containing protein 3;
GN   Name=TIM14-3; OrderedLocusNames=At5g03030; ORFNames=F15A17.60;
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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].
RA   Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
RP   SUBCELLULAR LOCATION.
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   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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: Component of the PAM complex, a complex required for the
CC       translocation of transit peptide-containing proteins from the inner
CC       membrane into the mitochondrial matrix in an ATP-dependent manner.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Probable component of the PAM complex at least composed of a
CC       mitochondrial HSP70 protein, TIMM44 and TIMM14. The complex interacts
CC       with the TIMM23 component of the TIM17:23 complex (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:17098851}.
CC       Mitochondrion inner membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TIM14 family. {ECO:0000305}.
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DR   EMBL; AL163002; CAB86070.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90547.1; -; Genomic_DNA.
DR   EMBL; AY085893; AAM63105.1; -; mRNA.
DR   EMBL; BT025587; ABF59005.1; -; mRNA.
DR   PIR; T48324; T48324.
DR   RefSeq; NP_195923.1; NM_120381.3.
DR   AlphaFoldDB; Q9LYY2; -.
DR   SMR; Q9LYY2; -.
DR   STRING; 3702.AT5G03030.1; -.
DR   iPTMnet; Q9LYY2; -.
DR   PaxDb; Q9LYY2; -.
DR   PRIDE; Q9LYY2; -.
DR   ProteomicsDB; 234329; -.
DR   EnsemblPlants; AT5G03030.1; AT5G03030.1; AT5G03030.
DR   GeneID; 831703; -.
DR   Gramene; AT5G03030.1; AT5G03030.1; AT5G03030.
DR   KEGG; ath:AT5G03030; -.
DR   Araport; AT5G03030; -.
DR   TAIR; locus:2143488; AT5G03030.
DR   eggNOG; KOG0723; Eukaryota.
DR   HOGENOM; CLU_017633_13_2_1; -.
DR   InParanoid; Q9LYY2; -.
DR   OMA; MTKWEAA; -.
DR   PhylomeDB; Q9LYY2; -.
DR   PRO; PR:Q9LYY2; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LYY2; baseline and differential.
DR   Genevisible; Q9LYY2; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0001405; C:PAM complex, Tim23 associated import motor; IBA:GO_Central.
DR   GO; GO:0001671; F:ATPase activator activity; IBA:GO_Central.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR   Gene3D; 1.10.287.110; -; 1.
DR   InterPro; IPR036869; J_dom_sf.
DR   SUPFAM; SSF46565; SSF46565; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..112
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit TIM14-3"
FT                   /id="PRO_0000420927"
FT   TRANSMEM        6..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          53..112
FT                   /note="J"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   112 AA;  12064 MW;  9FFF91D9A28F8172 CRC64;
     MATPMIAGAA VAAAAVAGRY GILAWQAFKA RPRVPRMRRF YEGGFQSSMT RREAALILGV
     RESVVADKVK EAHRRVMVAN HPDAGGSHYL ASKINEAKDM MLGKSNNSGS AF