TIM29_HUMAN
ID TIM29_HUMAN Reviewed; 260 AA.
AC Q9BSF4; Q96EY6; Q96IT8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim29 {ECO:0000303|PubMed:27554484};
DE Short=TIM29 {ECO:0000303|PubMed:27554484};
DE Flags: Precursor;
GN Name=TIMM29 {ECO:0000312|HGNC:HGNC:25152}; Synonyms=c19orf52;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [5]
RP SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH TIMM10B AND TOMM40,
RP FUNCTION, IDENTIFICATION IN THE TIM22 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=27554484; DOI=10.7554/elife.17463;
RA Kang Y., Baker M.J., Liem M., Louber J., McKenzie M., Atukorala I.,
RA Ang C.S., Keerthikumar S., Mathivanan S., Stojanovski D.;
RT "Tim29 is a novel subunit of the human TIM22 translocase and is involved in
RT complex assembly and stability.";
RL Elife 5:0-0(2016).
RN [6]
RP SUBCELLULAR LOCATION, TOPOLOGY, IDENTIFICATION IN THE TIM22 COMPLEX,
RP INTERACTION WITH TRIMM22, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP FUNCTION.
RX PubMed=27718247; DOI=10.1002/1873-3468.12450;
RA Callegari S., Richter F., Chojnacka K., Jans D.C., Lorenzi I.,
RA Pacheu-Grau D., Jakobs S., Lenz C., Urlaub H., Dudek J., Chacinska A.,
RA Rehling P.;
RT "TIM29 is a subunit of the human carrier translocase required for protein
RT transport.";
RL FEBS Lett. 590:4147-4158(2016).
RN [7]
RP IDENTIFICATION IN THE TIM22 COMPLEX.
RX PubMed=28712724; DOI=10.1016/j.molcel.2017.06.013;
RA Vukotic M., Nolte H., Koenig T., Saita S., Ananjew M., Krueger M.,
RA Tatsuta T., Langer T.;
RT "Acylglycerol kinase mutated in Sengers Syndrome is a subunit of the TIM22
RT protein translocase in mitochondria.";
RL Mol. Cell 0:0-0(2017).
RN [8]
RP IDENTIFICATION IN THE TIM22 COMPLEX.
RX PubMed=28712726; DOI=10.1016/j.molcel.2017.06.014;
RA Kang Y., Stroud D.A., Baker M.J., De Souza D.P., Frazier A.E., Liem M.,
RA Tull D., Mathivanan S., McConville M.J., Thorburn D.R., Ryan M.T.,
RA Stojanovski D.;
RT "Sengers syndrome-associated mitochondrial acylglycerol kinase is a subunit
RT of the human TIM22 protein import complex.";
RL Mol. Cell 0:0-0(2017).
CC -!- FUNCTION: Component of the TIM22 complex, a complex that mediates the
CC import and insertion of multi-pass transmembrane proteins into the
CC mitochondrial inner membrane. The TIM22 complex forms a twin-pore
CC translocase that uses the membrane potential as the external driving
CC force. Required for the stability of the TIM22 complex and functions in
CC the assembly of the TIMM22 protein into the TIM22 complex. May
CC facilitate cooperation between TIM22 and TOM complexes by interacting
CC with TOMM40. {ECO:0000269|PubMed:27554484,
CC ECO:0000269|PubMed:27718247}.
CC -!- SUBUNIT: Component of the TIM22 complex, which core is composed of
CC TIMM22, associated with TIMM10 (TIMM10A and/or TIMM10B), TIMM9, AGK and
CC TIMM29 (PubMed:27554484, PubMed:27718247, PubMed:28712724,
CC PubMed:28712726). Interacts with TIMM10B; the interaction is direct
CC (PubMed:27554484). Interacts with TOMM40; linking the TIM22 complex to
CC the TOM complex (PubMed:27554484). Interacts with TIMM22 (when
CC oxidized); the interaction is direct (PubMed:27718247).
CC {ECO:0000269|PubMed:27554484, ECO:0000269|PubMed:27718247}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:27554484, ECO:0000269|PubMed:27718247}; Single-pass
CC membrane protein {ECO:0000305}; Intermembrane side
CC {ECO:0000269|PubMed:27718247}.
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DR EMBL; AC011442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005075; AAH05075.2; -; mRNA.
DR EMBL; BC007244; AAH07244.2; -; mRNA.
DR EMBL; BC011833; AAH11833.1; -; mRNA.
DR CCDS; CCDS12252.1; -.
DR RefSeq; NP_612367.1; NM_138358.2.
DR PDB; 7CGP; EM; 3.70 A; C=1-260.
DR PDBsum; 7CGP; -.
DR AlphaFoldDB; Q9BSF4; -.
DR SMR; Q9BSF4; -.
DR BioGRID; 124736; 119.
DR ComplexPortal; CPX-6124; TIM22 mitochondrial inner membrane twin-pore carrier translocase complex.
DR IntAct; Q9BSF4; 36.
DR MINT; Q9BSF4; -.
DR STRING; 9606.ENSP00000270502; -.
DR iPTMnet; Q9BSF4; -.
DR PhosphoSitePlus; Q9BSF4; -.
DR BioMuta; TIMM29; -.
DR DMDM; 74732998; -.
DR EPD; Q9BSF4; -.
DR jPOST; Q9BSF4; -.
DR MassIVE; Q9BSF4; -.
DR MaxQB; Q9BSF4; -.
DR PaxDb; Q9BSF4; -.
DR PeptideAtlas; Q9BSF4; -.
DR PRIDE; Q9BSF4; -.
DR ProteomicsDB; 78885; -.
DR Antibodypedia; 51917; 34 antibodies from 13 providers.
DR DNASU; 90580; -.
DR Ensembl; ENST00000270502.7; ENSP00000270502.5; ENSG00000142444.7.
DR GeneID; 90580; -.
DR KEGG; hsa:90580; -.
DR MANE-Select; ENST00000270502.7; ENSP00000270502.5; NM_138358.4; NP_612367.1.
DR UCSC; uc002mqd.3; human.
DR CTD; 90580; -.
DR GeneCards; TIMM29; -.
DR HGNC; HGNC:25152; TIMM29.
DR HPA; ENSG00000142444; Low tissue specificity.
DR MIM; 617380; gene.
DR neXtProt; NX_Q9BSF4; -.
DR OpenTargets; ENSG00000142444; -.
DR PharmGKB; PA147358399; -.
DR VEuPathDB; HostDB:ENSG00000142444; -.
DR eggNOG; KOG4545; Eukaryota.
DR GeneTree; ENSGT00390000018541; -.
DR HOGENOM; CLU_102697_0_0_1; -.
DR InParanoid; Q9BSF4; -.
DR OMA; WRLKWKM; -.
DR OrthoDB; 1386679at2759; -.
DR PhylomeDB; Q9BSF4; -.
DR TreeFam; TF313304; -.
DR PathwayCommons; Q9BSF4; -.
DR SignaLink; Q9BSF4; -.
DR SIGNOR; Q9BSF4; -.
DR BioGRID-ORCS; 90580; 413 hits in 1055 CRISPR screens.
DR ChiTaRS; C19orf52; human.
DR GenomeRNAi; 90580; -.
DR Pharos; Q9BSF4; Tdark.
DR PRO; PR:Q9BSF4; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BSF4; protein.
DR Bgee; ENSG00000142444; Expressed in monocyte and 106 other tissues.
DR ExpressionAtlas; Q9BSF4; baseline and differential.
DR Genevisible; Q9BSF4; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR GO; GO:0042721; C:TIM22 mitochondrial import inner membrane insertion complex; IDA:UniProtKB.
DR GO; GO:0140318; F:protein transporter activity; IMP:FlyBase.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IDA:UniProtKB.
DR InterPro; IPR019322; TIMM29.
DR PANTHER; PTHR21435; PTHR21435; 1.
DR Pfam; PF10171; Tim29; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Protein transport; Reference proteome; Transit peptide; Translocation;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 32..260
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim29"
FT /id="PRO_0000271006"
FT TOPO_DOM 32..59
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:27554484,
FT ECO:0000305|PubMed:27718247"
FT TRANSMEM 60..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..260
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:27554484,
FT ECO:0000305|PubMed:27718247"
SQ SEQUENCE 260 AA; 29233 MW; 000324A28C9F2902 CRC64;
MAAAALRRFW SRRRAEAGDA VVAKPGVWAR LGSWARALLR DYAEACRDAS AEARARPGRA
AVYVGLLGGA AACFTLAPSE GAFEEALLEA SGTLLLLAPA TRNRESEAFV QRLLWLRGRG
RLRYVNLGLC SLVYEAPFDA QASLYQARCR YLQPRWTDFP GRVLDVGFVG RWWVLGAWMR
DCDINDDEFL HLPAHLRVVG PQQLHSETNE RLFDEKYKPV VLTDDQVDQA LWEEQVLQKE
KKDRLALSQA HSLVQAEAPR
