ID TTC19_HUMAN Reviewed; 380 AA.
AC Q6DKK2; A8MZ52; B3KP62; B4DN65; Q2M248; Q7L3U8; Q9H6G3; Q9NXB2;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 4.
DT 27-MAR-2024, entry version 160.
DE RecName: Full=Tetratricopeptide repeat protein 19, mitochondrial;
DE Short=TPR repeat protein 19;
DE Flags: Precursor;
GN Name=TTC19;
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=Chondrocyte, and Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Muscle;
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 [5]
RP INTERACTION WITH ZFYVE26 AND CHMP4B, AND CAUTION.
RX PubMed=20208530; DOI=10.1038/ncb2036;
RA Sagona A.P., Nezis I.P., Pedersen N.M., Liestol K., Poulton J.,
RA Rusten T.E., Skotheim R.I., Raiborg C., Stenmark H.;
RT "PtdIns(3)P controls cytokinesis through KIF13A-mediated recruitment of
RT FYVE-CENT to the midbody.";
RL Nat. Cell Biol. 12:362-371(2010).
RN [6]
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 [7]
RP INVOLVEMENT IN MC3DN2, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=21278747; DOI=10.1038/ng.761;
RA Ghezzi D., Arzuffi P., Zordan M., Da Re C., Lamperti C., Benna C.,
RA D'Adamo P., Diodato D., Costa R., Mariotti C., Uziel G., Smiderle C.,
RA Zeviani M.;
RT "Mutations in TTC19 cause mitochondrial complex III deficiency and
RT neurological impairment in humans and flies.";
RL Nat. Genet. 43:259-263(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH COMPLEX III.
RX PubMed=28673544; DOI=10.1016/j.molcel.2017.06.001;
RA Bottani E., Cerutti R., Harbour M.E., Ravaglia S., Dogan S.A., Giordano C.,
RA Fearnley I.M., D'Amati G., Viscomi C., Fernandez-Vizarra E., Zeviani M.;
RT "TTC19 plays a husbandry role on UQCRFS1 turnover in the biogenesis of
RT mitochondrial respiratory complex III.";
RL Mol. Cell 67:96-105(2017).
RN [10]
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=28288130; DOI=10.1038/ncb3488;
RA Saita S., Nolte H., Fiedler K.U., Kashkar H., Venne A.S., Zahedi R.P.,
RA Krueger M., Langer T.;
RT "PARL mediates Smac proteolytic maturation in mitochondria to promote
RT apoptosis.";
RL Nat. Cell Biol. 19:318-328(2017).
CC -!- FUNCTION: Required for the preservation of the structural and
CC functional integrity of mitochondrial respiratory complex III by
CC allowing the physiological turnover of the Rieske protein UQCRFS1
CC (PubMed:21278747, PubMed:28673544). Involved in the clearance of
CC UQCRFS1 N-terminal fragments, which are produced upon incorporation of
CC UQCRFS1 into the complex III and whose presence is detrimental for its
CC catalytic activity (PubMed:28673544). {ECO:0000269|PubMed:21278747,
CC ECO:0000269|PubMed:28673544}.
CC -!- SUBUNIT: Binds to the mature mitochondrial complex III dimer, after the
CC incorporation of the Rieske protein UQCRFS1 (PubMed:28673544).
CC Interacts with UQCRC1 and UQCRFS1 (By similarity). Interacts with
CC ZFYVE26 and CHMP4B (PubMed:20208530). {ECO:0000250|UniProtKB:Q8CC21,
CC ECO:0000269|PubMed:20208530, ECO:0000269|PubMed:28673544}.
CC -!- INTERACTION:
CC Q6DKK2; P21549: AGXT; NbExp=3; IntAct=EBI-948354, EBI-727098;
CC Q6DKK2; P07741: APRT; NbExp=3; IntAct=EBI-948354, EBI-1047565;
CC Q6DKK2; P54253: ATXN1; NbExp=7; IntAct=EBI-948354, EBI-930964;
CC Q6DKK2; Q9H1P6: CIMIP1; NbExp=3; IntAct=EBI-948354, EBI-12155483;
CC Q6DKK2; Q5JTJ3: COA6; NbExp=3; IntAct=EBI-948354, EBI-2874677;
CC Q6DKK2; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-948354, EBI-9679045;
CC Q6DKK2; Q9NRA8: EIF4ENIF1; NbExp=3; IntAct=EBI-948354, EBI-301024;
CC Q6DKK2; Q96C01: FAM136A; NbExp=3; IntAct=EBI-948354, EBI-373319;
CC Q6DKK2; Q9NTX9: FAM217B; NbExp=3; IntAct=EBI-948354, EBI-19153639;
CC Q6DKK2; P07954: FH; NbExp=3; IntAct=EBI-948354, EBI-1050358;
CC Q6DKK2; Q9C0B1-2: FTO; NbExp=3; IntAct=EBI-948354, EBI-18138793;
CC Q6DKK2; Q9H8Y8: GORASP2; NbExp=5; IntAct=EBI-948354, EBI-739467;
CC Q6DKK2; O95872: GPANK1; NbExp=4; IntAct=EBI-948354, EBI-751540;
CC Q6DKK2; P35452-2: HOXD12; NbExp=3; IntAct=EBI-948354, EBI-17244356;
CC Q6DKK2; O43464: HTRA2; NbExp=4; IntAct=EBI-948354, EBI-517086;
CC Q6DKK2; P42858: HTT; NbExp=3; IntAct=EBI-948354, EBI-466029;
CC Q6DKK2; Q8IYA8: IHO1; NbExp=6; IntAct=EBI-948354, EBI-8638439;
CC Q6DKK2; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-948354, EBI-1055254;
CC Q6DKK2; Q96JM7: L3MBTL3; NbExp=3; IntAct=EBI-948354, EBI-2686809;
CC Q6DKK2; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-948354, EBI-11985629;
CC Q6DKK2; O43679: LDB2; NbExp=3; IntAct=EBI-948354, EBI-2865580;
CC Q6DKK2; P12872: MLN; NbExp=3; IntAct=EBI-948354, EBI-18053274;
CC Q6DKK2; Q9BRK3: MXRA8; NbExp=3; IntAct=EBI-948354, EBI-11721798;
CC Q6DKK2; Q15742: NAB2; NbExp=3; IntAct=EBI-948354, EBI-8641936;
CC Q6DKK2; O00746: NME4; NbExp=3; IntAct=EBI-948354, EBI-744871;
CC Q6DKK2; P78424: POU6F2; NbExp=3; IntAct=EBI-948354, EBI-12029004;
CC Q6DKK2; P0CG20: PRR35; NbExp=3; IntAct=EBI-948354, EBI-11986293;
CC Q6DKK2; P09455: RBP1; NbExp=3; IntAct=EBI-948354, EBI-2623483;
CC Q6DKK2; Q04864: REL; NbExp=3; IntAct=EBI-948354, EBI-307352;
CC Q6DKK2; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-948354, EBI-6257312;
CC Q6DKK2; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-948354, EBI-747035;
CC Q6DKK2; Q6ZSJ9: SHISA6; NbExp=3; IntAct=EBI-948354, EBI-12037847;
CC Q6DKK2; Q8N1D0-2: SLC22A18AS; NbExp=5; IntAct=EBI-948354, EBI-12829638;
CC Q6DKK2; Q9H0W8: SMG9; NbExp=3; IntAct=EBI-948354, EBI-2872322;
CC Q6DKK2; Q13207: TBX2; NbExp=3; IntAct=EBI-948354, EBI-2853051;
CC Q6DKK2; O15273: TCAP; NbExp=4; IntAct=EBI-948354, EBI-954089;
CC Q6DKK2; A0A024R8A9: USP20; NbExp=3; IntAct=EBI-948354, EBI-14096082;
CC Q6DKK2; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-948354, EBI-11975223;
CC Q6DKK2; P0C7X2: ZNF688; NbExp=3; IntAct=EBI-948354, EBI-4395732;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:21278747}.
CC -!- PTM: Proteolytically cleaved by PARL. {ECO:0000269|PubMed:28288130}.
CC -!- DISEASE: Mitochondrial complex III deficiency, nuclear type 2 (MC3DN2)
CC [MIM:615157]: A disorder of the mitochondrial respiratory chain
CC resulting in a highly variable phenotype depending on which tissues are
CC affected. Clinical features include mitochondrial encephalopathy,
CC psychomotor retardation, ataxia, severe failure to thrive, liver
CC dysfunction, renal tubulopathy, muscle weakness and exercise
CC intolerance. {ECO:0000269|PubMed:21278747}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TTC19 family. {ECO:0000305}.
CC -!- CAUTION: Was reported to be required for the abcission step in
CC cytokinesis, possibly regulating the ESCRT-III complex via its
CC interaction with CHMP4B (PubMed:20208530). According to the same
CC authors, localizes to the centrosome during all stages of the cell
CC cycle and is recruited to the midbody during cytokinesis
CC (PubMed:20208530). However, the midbody localization could not be
CC confirmed by others (PubMed:21278747). {ECO:0000269|PubMed:20208530,
CC ECO:0000269|PubMed:21278747}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH11698.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH73796.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI05129.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI12108.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91103.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15296.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG51574.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG51820.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK000350; BAA91103.1; ALT_INIT; mRNA.
DR EMBL; AK025958; BAB15296.1; ALT_INIT; mRNA.
DR EMBL; AK055780; BAG51574.1; ALT_INIT; mRNA.
DR EMBL; AK056878; BAG51820.1; ALT_INIT; mRNA.
DR EMBL; AK297783; BAG60127.1; -; mRNA.
DR EMBL; AC006251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC002553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471222; EAX04490.1; -; Genomic_DNA.
DR EMBL; BC011698; AAH11698.2; ALT_INIT; mRNA.
DR EMBL; BC073796; AAH73796.1; ALT_INIT; mRNA.
DR EMBL; BC105128; AAI05129.1; ALT_INIT; mRNA.
DR EMBL; BC112107; AAI12108.1; ALT_INIT; mRNA.
DR CCDS; CCDS11174.2; -.
DR RefSeq; NP_001258349.1; NM_001271420.1.
DR RefSeq; NP_060245.3; NM_017775.3.
DR AlphaFoldDB; Q6DKK2; -.
DR SMR; Q6DKK2; -.
DR BioGRID; 120248; 122.
DR IntAct; Q6DKK2; 84.
DR MINT; Q6DKK2; -.
DR STRING; 9606.ENSP00000261647; -.
DR iPTMnet; Q6DKK2; -.
DR MetOSite; Q6DKK2; -.
DR PhosphoSitePlus; Q6DKK2; -.
DR BioMuta; TTC19; -.
DR DMDM; 332278244; -.
DR EPD; Q6DKK2; -.
DR jPOST; Q6DKK2; -.
DR MassIVE; Q6DKK2; -.
DR MaxQB; Q6DKK2; -.
DR PaxDb; 9606-ENSP00000261647; -.
DR PeptideAtlas; Q6DKK2; -.
DR ProteomicsDB; 66236; -.
DR Pumba; Q6DKK2; -.
DR Antibodypedia; 13179; 85 antibodies from 21 providers.
DR DNASU; 54902; -.
DR Ensembl; ENST00000261647.10; ENSP00000261647.5; ENSG00000011295.16.
DR GeneID; 54902; -.
DR KEGG; hsa:54902; -.
DR MANE-Select; ENST00000261647.10; ENSP00000261647.5; NM_017775.4; NP_060245.3.
DR UCSC; uc002gph.4; human.
DR AGR; HGNC:26006; -.
DR CTD; 54902; -.
DR DisGeNET; 54902; -.
DR GeneCards; TTC19; -.
DR HGNC; HGNC:26006; TTC19.
DR HPA; ENSG00000011295; Low tissue specificity.
DR MalaCards; TTC19; -.
DR MIM; 613814; gene.
DR MIM; 615157; phenotype.
DR neXtProt; NX_Q6DKK2; -.
DR OpenTargets; ENSG00000011295; -.
DR Orphanet; 1460; Isolated complex III deficiency.
DR PharmGKB; PA134922384; -.
DR VEuPathDB; HostDB:ENSG00000011295; -.
DR eggNOG; KOG1840; Eukaryota.
DR GeneTree; ENSGT00390000009194; -.
DR HOGENOM; CLU_057135_1_0_1; -.
DR InParanoid; Q6DKK2; -.
DR OMA; MKQGKYL; -.
DR OrthoDB; 3667607at2759; -.
DR TreeFam; TF314010; -.
DR PathwayCommons; Q6DKK2; -.
DR SignaLink; Q6DKK2; -.
DR SIGNOR; Q6DKK2; -.
DR BioGRID-ORCS; 54902; 78 hits in 1162 CRISPR screens.
DR ChiTaRS; TTC19; human.
DR GenomeRNAi; 54902; -.
DR Pharos; Q6DKK2; Tbio.
DR PRO; PR:Q6DKK2; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q6DKK2; Protein.
DR Bgee; ENSG00000011295; Expressed in jejunal mucosa and 201 other cell types or tissues.
DR ExpressionAtlas; Q6DKK2; baseline and differential.
DR Genevisible; Q6DKK2; HS.
DR GO; GO:0005813; C:centrosome; TAS:UniProtKB.
DR GO; GO:0030496; C:midbody; TAS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0034551; P:mitochondrial respiratory chain complex III assembly; IMP:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; TAS:UniProtKB.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR040395; TTC19.
DR PANTHER; PTHR13143; TETRATRICOPEPTIDE REPEAT PROTEIN 19; 1.
DR PANTHER; PTHR13143:SF6; TETRATRICOPEPTIDE REPEAT PROTEIN 19, MITOCHONDRIAL; 1.
DR Pfam; PF13374; TPR_10; 1.
DR Pfam; PF13424; TPR_12; 1.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Primary mitochondrial disease;
KW Reference proteome; Repeat; Respiratory chain; TPR repeat; Transit peptide;
KW Transport.
FT TRANSIT 1..70
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 71..380
FT /note="Tetratricopeptide repeat protein 19, mitochondrial"
FT /id="PRO_0000106407"
FT REPEAT 136..169
FT /note="TPR 1"
FT REPEAT 179..212
FT /note="TPR 2"
FT REPEAT 237..270
FT /note="TPR 3"
FT REPEAT 279..312
FT /note="TPR 4"
FT REPEAT 318..351
FT /note="TPR 5"
FT SITE 71..72
FT /note="Cleavage; by PARL"
FT /evidence="ECO:0000269|PubMed:28288130"
FT CONFLICT 282
FT /note="M -> V (in Ref. 1; BAG51574)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="E -> K (in Ref. 1; BAB15296)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 42457 MW; AA082C9F6F8EE429 CRC64;
MFRLLSWSLG RGFLRAAGRR CRGCSARLLP GLAGGPGPEV QVPPSRVAPH GRGPGLLPLL
AALAWFSRPA AAEEEEQQGA DGAAAEDGAD EAEAEIIQLL KRAKLSIMKD EPEEAELILH
DALRLAYQTD NKKAITYTYD LMANLAFIRG QLENAEQLFK ATMSYLLGGG MKQEDNAIIE
ISLKLASIYA AQNRQEFAVA GYEFCISTLE EKIEREKELA EDIMSVEEKA NTHLLLGMCL
DACARYLLFS KQPSQAQRMY EKALQISEEI QGERHPQTIV LMSDLATTLD AQGRFDEAYI
YMQRASDLAR QINHPELHMV LSNLAAVLMH RERYTQAKEI YQEALKQAKL KKDEISVQHI
REELAELSKK SRPLTNSVKL
//
