TIM21_HUMAN
ID TIM21_HUMAN Reviewed; 248 AA.
AC Q9BVV7; Q9P010;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim21;
DE AltName: Full=TIM21-like protein, mitochondrial;
DE Flags: Precursor;
GN Name=TIMM21; Synonyms=C18orf55, TIM21; ORFNames=HSPC154;
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 MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix carcinoma;
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 FUNCTION, IDENTIFICATION IN THE TIM23 COMPLEX, AND IDENTIFICATION IN MITRAC
RP COMPLEX.
RX PubMed=23260140; DOI=10.1016/j.cell.2012.11.053;
RA Mick D.U., Dennerlein S., Wiese H., Reinhold R., Pacheu-Grau D.,
RA Lorenzi I., Sasarman F., Weraarpachai W., Shoubridge E.A., Warscheid B.,
RA Rehling P.;
RT "MITRAC links mitochondrial protein translocation to respiratory-chain
RT assembly and translational regulation.";
RL Cell 151:1528-1541(2012).
RN [5]
RP INTERACTION WITH COA3 AND MT-CO1.
RX PubMed=26321642; DOI=10.1016/j.celrep.2015.08.009;
RA Dennerlein S., Oeljeklaus S., Jans D., Hellwig C., Bareth B., Jakobs S.,
RA Deckers M., Warscheid B., Rehling P.;
RT "MITRAC7 acts as a COX1-specific chaperone and reveals a checkpoint during
RT cytochrome c oxidase assembly.";
RL Cell Rep. 12:1644-1655(2015).
RN [6]
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).
CC -!- FUNCTION: Participates in the translocation of transit peptide-
CC containing proteins across the mitochondrial inner membrane. Also
CC required for assembly of mitochondrial respiratory chain complex I and
CC complex IV as component of the MITRAC (mitochondrial translation
CC regulation assembly intermediate of cytochrome c oxidase complex)
CC complex. Probably shuttles between the presequence translocase and
CC respiratory-chain assembly intermediates in a process that promotes
CC incorporation of early nuclear-encoded subunits into these complexes.
CC {ECO:0000269|PubMed:23260140}.
CC -!- SUBUNIT: Component of the TIM23 complex. Component of the MITRAC
CC (mitochondrial translation regulation assembly intermediate of
CC cytochrome c oxidase complex) complex, the core components of this
CC complex being COA3/MITRAC12 and COX14 (Probable) (PubMed:23260140).
CC Interacts with COA3 AND MT-CO1/COX1 (PubMed:26321642).
CC {ECO:0000269|PubMed:23260140, ECO:0000269|PubMed:26321642,
CC ECO:0000305|PubMed:26321642}.
CC -!- INTERACTION:
CC Q9BVV7; P00395: MT-CO1; NbExp=3; IntAct=EBI-6570759, EBI-2117234;
CC Q9BVV7; O14925: TIMM23; NbExp=3; IntAct=EBI-6570759, EBI-1047996;
CC Q9BVV7; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-6570759, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TIM21 family. {ECO:0000305}.
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DR EMBL; AF161503; AAF29118.1; -; mRNA.
DR EMBL; BC000892; AAH00892.1; -; mRNA.
DR CCDS; CCDS12003.1; -.
DR RefSeq; NP_054896.2; NM_014177.2.
DR AlphaFoldDB; Q9BVV7; -.
DR SMR; Q9BVV7; -.
DR BioGRID; 118859; 38.
DR ComplexPortal; CPX-6129; TIM23 mitochondrial inner membrane pre-sequence translocase complex, TIM17A variant.
DR ComplexPortal; CPX-6130; TIM23 mitochondrial inner membrane pre-sequence translocase complex, TIM17B variant.
DR CORUM; Q9BVV7; -.
DR IntAct; Q9BVV7; 25.
DR MINT; Q9BVV7; -.
DR STRING; 9606.ENSP00000169551; -.
DR GlyGen; Q9BVV7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BVV7; -.
DR PhosphoSitePlus; Q9BVV7; -.
DR SwissPalm; Q9BVV7; -.
DR BioMuta; TIMM21; -.
DR DMDM; 73918912; -.
DR EPD; Q9BVV7; -.
DR jPOST; Q9BVV7; -.
DR MassIVE; Q9BVV7; -.
DR MaxQB; Q9BVV7; -.
DR PaxDb; Q9BVV7; -.
DR PeptideAtlas; Q9BVV7; -.
DR PRIDE; Q9BVV7; -.
DR ProteomicsDB; 79238; -.
DR TopDownProteomics; Q9BVV7; -.
DR Antibodypedia; 2242; 49 antibodies from 18 providers.
DR DNASU; 29090; -.
DR Ensembl; ENST00000169551.11; ENSP00000169551.6; ENSG00000075336.12.
DR GeneID; 29090; -.
DR KEGG; hsa:29090; -.
DR MANE-Select; ENST00000169551.11; ENSP00000169551.6; NM_014177.3; NP_054896.2.
DR UCSC; uc010dqr.2; human.
DR CTD; 29090; -.
DR GeneCards; TIMM21; -.
DR HGNC; HGNC:25010; TIMM21.
DR HPA; ENSG00000075336; Low tissue specificity.
DR MIM; 615180; gene.
DR neXtProt; NX_Q9BVV7; -.
DR OpenTargets; ENSG00000075336; -.
DR PharmGKB; PA134897360; -.
DR VEuPathDB; HostDB:ENSG00000075336; -.
DR eggNOG; KOG4836; Eukaryota.
DR GeneTree; ENSGT00390000011552; -.
DR HOGENOM; CLU_099476_0_0_1; -.
DR InParanoid; Q9BVV7; -.
DR OMA; FRYVFVE; -.
DR OrthoDB; 1330321at2759; -.
DR PhylomeDB; Q9BVV7; -.
DR TreeFam; TF315067; -.
DR PathwayCommons; Q9BVV7; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR SignaLink; Q9BVV7; -.
DR SIGNOR; Q9BVV7; -.
DR BioGRID-ORCS; 29090; 11 hits in 1085 CRISPR screens.
DR ChiTaRS; TIMM21; human.
DR GenomeRNAi; 29090; -.
DR Pharos; Q9BVV7; Tbio.
DR PRO; PR:Q9BVV7; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q9BVV7; protein.
DR Bgee; ENSG00000075336; Expressed in left ventricle myocardium and 186 other tissues.
DR ExpressionAtlas; Q9BVV7; baseline and differential.
DR Genevisible; Q9BVV7; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IC:ComplexPortal.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IMP:UniProtKB.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:UniProtKB.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IMP:UniProtKB.
DR Gene3D; 3.10.450.320; -; 1.
DR InterPro; IPR013261; Tim21.
DR InterPro; IPR038552; Tim21_IMS_sf.
DR PANTHER; PTHR13032; PTHR13032; 1.
DR Pfam; PF08294; TIM21; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Protein transport; Reference proteome;
KW Transit peptide; Translocation; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..18
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 19..248
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim21"
FT /id="PRO_0000043228"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 67..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 79
FT /note="G -> S (in dbSNP:rs3737512)"
FT /id="VAR_052306"
FT CONFLICT 34
FT /note="C -> Y (in Ref. 1; AAF29118)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 28202 MW; 7BA2694A9DCD9024 CRC64;
MICTFLRAVQ YTEKLHRSSA KRLLLPYIVL NKACLKTEPS LRCGLQYQKK TLRPRCILGV
TQKTIWTQGP SPRKAKEDGS KQVSVHRSQR GGTAVPTSQK VKEAGRDFTY LIVVLFGISI
TGGLFYTIFK ELFSSSSPSK IYGRALEKCR SHPEVIGVFG ESVKGYGEVT RRGRRQHVRF
TEYVKDGLKH TCVKFYIEGS EPGKQGTVYA QVKENPGSGE YDFRYIFVEI ESYPRRTIII
EDNRSQDD
