MTRFR_HUMAN
ID MTRFR_HUMAN Reviewed; 166 AA.
AC Q9H3J6; Q8WUC6;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Mitochondrial translation release factor in rescue {ECO:0000305};
DE Flags: Precursor;
GN Name=MTRFR {ECO:0000312|HGNC:HGNC:26784}; ORFNames=C12orf65, My030;
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] (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Mao Y.M., Xie Y., Ying K.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [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] (ISOFORMS 1 AND 2).
RC TISSUE=Blood, Colon, and Testis;
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 SUBCELLULAR LOCATION.
RX PubMed=20186120; DOI=10.1038/emboj.2010.14;
RA Richter R., Rorbach J., Pajak A., Smith P.M., Wessels H.J., Huynen M.A.,
RA Smeitink J.A., Lightowlers R.N., Chrzanowska-Lightowlers Z.M.;
RT "A functional peptidyl-tRNA hydrolase, ICT1, has been recruited into the
RT human mitochondrial ribosome.";
RL EMBO J. 29:1116-1125(2010).
RN [6]
RP DOMAIN.
RX PubMed=22821833; DOI=10.1002/prot.24152;
RA Kogure H., Hikawa Y., Hagihara M., Tochio N., Koshiba S., Inoue Y.,
RA Guntert P., Kigawa T., Yokoyama S., Nameki N.;
RT "Solution structure and siRNA-mediated knockdown analysis of the
RT mitochondrial disease-related protein C12orf65.";
RL Proteins 80:2629-2642(2012).
RN [7]
RP INTERACTION WITH MTRES1.
RX PubMed=31396629; DOI=10.1093/nar/gkz684;
RA Gopalakrishna S., Pearce S.F., Dinan A.M., Schober F.A., Cipullo M.,
RA Spaahr H., Khawaja A., Maffezzini C., Freyer C., Wredenberg A.,
RA Atanassov I., Firth A.E., Rorbach J.;
RT "C6orf203 is an RNA-binding protein involved in mitochondrial protein
RT synthesis.";
RL Nucleic Acids Res. 47:9386-9399(2019).
RN [8] {ECO:0000312|PDB:7A5H}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.3 ANGSTROMS) OF 1-166 IN COMPLEX WITH
RP MTRES1; PEPTIDYL TRNA AND MITORIBOSOMAL LARGE SUBUNIT, FUNCTION,
RP INTERACTION WITH MTRES1, AND RNA-BINDING.
RX PubMed=33243891; DOI=10.1126/science.abc7782;
RA Desai N., Yang H., Chandrasekaran V., Kazi R., Minczuk M., Ramakrishnan V.;
RT "Elongational stalling activates mitoribosome-associated quality control.";
RL Science 370:1105-1110(2020).
RN [9]
RP INVOLVEMENT IN COXPD7, SUBCELLULAR LOCATION, VARIANT COXPD7 83-VAL--HIS-166
RP DELINS GLY, CHARACTERIZATION OF VARIANT COXPD7 83-VAL--HIS-166 DELINS GLY,
RP AND RNA-BINDING.
RX PubMed=20598281; DOI=10.1016/j.ajhg.2010.06.004;
RA Antonicka H., Ostergaard E., Sasarman F., Weraarpachai W., Wibrand F.,
RA Pedersen A.M., Rodenburg R.J., van der Knaap M.S., Smeitink J.A.,
RA Chrzanowska-Lightowlers Z.M., Shoubridge E.A.;
RT "Mutations in C12orf65 in patients with encephalomyopathy and a
RT mitochondrial translation defect.";
RL Am. J. Hum. Genet. 87:115-122(2010).
RN [10]
RP INVOLVEMENT IN SPG55, AND VARIANT SPG55 132-ARG--HIS-166 DEL.
RX PubMed=23188110; DOI=10.1136/jmedgenet-2012-101212;
RG Japan Spastic Paraplegia Research Consortium (JASPAC);
RA Shimazaki H., Takiyama Y., Ishiura H., Sakai C., Matsushima Y.,
RA Hatakeyama H., Honda J., Sakoe K., Naoi T., Namekawa M., Fukuda Y.,
RA Takahashi Y., Goto J., Tsuji S., Goto Y., Nakano I.;
RT "A homozygous mutation of C12orf65 causes spastic paraplegia with optic
RT atrophy and neuropathy (SPG55).";
RL J. Med. Genet. 49:777-784(2012).
RN [11]
RP INVOLVEMENT IN SPG55, AND VARIANT SPG55 139-GLN--HIS-166 DEL.
RX PubMed=24080142; DOI=10.1016/j.ejmg.2013.09.010;
RA Buchert R., Uebe S., Radwan F., Tawamie H., Issa S., Shimazaki H.,
RA Henneke M., Ekici A.B., Reis A., Abou Jamra R.;
RT "Mutations in the mitochondrial gene C12ORF65 lead to syndromic autosomal
RT recessive intellectual disability and show genotype phenotype
RT correlation.";
RL Eur. J. Med. Genet. 56:599-602(2013).
RN [12]
RP INVOLVEMENT IN SPG55, VARIANT SPG55 116-VAL--HIS-166 DEL, CHARACTERIZATION
RP OF VARIANT SPG55 116-VAL--HIS-166 DEL, AND TISSUE SPECIFICITY.
RX PubMed=24198383; DOI=10.1136/jnnp-2013-306387;
RG UKBEC;
RA Tucci A., Liu Y.T., Preza E., Pitceathly R.D., Chalasani A., Plagnol V.,
RA Land J.M., Trabzuni D., Ryten M., Jaunmuktane Z., Reilly M.M., Brandner S.,
RA Hargreaves I., Hardy J., Singleton A.B., Abramov A.Y., Houlden H.;
RT "Novel C12orf65 mutations in patients with axonal neuropathy and optic
RT atrophy.";
RL J. Neurol. Neurosurg. Psych. 85:486-492(2014).
RN [13]
RP INVOLVEMENT IN SPG55.
RX PubMed=26380172; DOI=10.3233/jnd-140003;
RA Pyle A., Ramesh V., Bartsakoulia M., Boczonadi V., Gomez-Duran A.,
RA Herczegfalvi A., Blakely E.L., Smertenko T., Duff J., Eglon G., Moore D.,
RA Yu-Wai-Man P., Douroudis K., Santibanez-Koref M., Griffin H.,
RA Lochmueller H., Karcagi V., Taylor R.W., Chinnery P.F., Horvath R.;
RT "Behr's Syndrome is Typically Associated with Disturbed Mitochondrial
RT Translation and Mutations in the C12orf65 Gene.";
RL J. Neuromuscul. Dis. 1:55-63(2014).
RN [14]
RP INVOLVEMENT IN COXPD7, AND VARIANT COXPD7 116-VAL--HIS-166 DEL.
RX PubMed=25995486; DOI=10.1136/jnnp-2014-310084;
RA Imagawa E., Fattal-Valevski A., Eyal O., Miyatake S., Saada A.,
RA Nakashima M., Tsurusaki Y., Saitsu H., Miyake N., Matsumoto N.;
RT "Homozygous p.V116* mutation in C12orf65 results in Leigh syndrome.";
RL J. Neurol. Neurosurg. Psych. 87:212-216(2016).
RN [15]
RP INVOLVEMENT IN COXPD7.
RX PubMed=32478789; DOI=10.1590/1678-4685-gmb-2018-0271;
RA Perrone E., Cavole T.R., Oliveira M.G., Virmond L.D.A., Silva M.F.B.,
RA Soares M.F.F., Iglesias S.B.O., Falconi A., Silva J.S., Nakano V.,
RA Milanezi M.F., Mendes C.S.C., Curiati M.A., Micheletti C.;
RT "Leigh syndrome in a patient with a novel C12orf65 pathogenic variant: case
RT report and literature review.";
RL Genet. Mol. Biol. 43:e20180271-e20180271(2020).
RN [16]
RP INVOLVEMENT IN COXPD7.
RX PubMed=32808965; DOI=10.1590/1678-4685-gmb-2020-0177;
RA Finsterer J.;
RT "The Leigh phenotype resulting from C12orf65 variants.";
RL Genet. Mol. Biol. 43:e20200177-e20200177(2020).
CC -!- FUNCTION: Part of a mitoribosome-associated quality control pathway
CC that prevents aberrant translation by responding to interruptions
CC during elongation (PubMed:33243891). As heterodimer with MTRES1, ejects
CC the unfinished nascent chain and peptidyl transfer RNA (tRNA),
CC respectively, from stalled ribosomes. Recruitment of mitoribosome
CC biogenesis factors to these quality control intermediates suggests
CC additional roles for MTRES1 and MTRF during mitoribosome rescue
CC (PubMed:33243891). {ECO:0000269|PubMed:33243891}.
CC -!- SUBUNIT: Interacts (via C-terminus) with MTRES1 (via S4 domain)
CC (PubMed:33243891). Associates with mitoribosomal S39 large subunit,
CC peptidyl tRNA and nascent chain (PubMed:33243891).
CC {ECO:0000269|PubMed:33243891}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20186120,
CC ECO:0000269|PubMed:20598281}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H3J6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H3J6-2; Sequence=VSP_029602, VSP_029603;
CC -!- TISSUE SPECIFICITY: Expressed in all areas of the brain tested.
CC {ECO:0000269|PubMed:24198383}.
CC -!- DOMAIN: The GGQ domain interacts with the peptidyltransferase center
CC (PTC) of the large ribosomal subunit to trigger nascent chain
CC hydrolysis. {ECO:0000269|PubMed:22821833, ECO:0000269|PubMed:33243891}.
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 7 (COXPD7)
CC [MIM:613559]: A mitochondrial disease resulting in encephalomyopathy.
CC Clinical manifestations include psychomotor delay and regression,
CC ataxia, optic atrophy, nystagmus and muscle atrophy and weakness.
CC {ECO:0000269|PubMed:20598281, ECO:0000269|PubMed:25995486,
CC ECO:0000269|PubMed:32478789, ECO:0000269|PubMed:32808965}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Spastic paraplegia 55, autosomal recessive (SPG55)
CC [MIM:615035]: A form of spastic paraplegia, a neurodegenerative
CC disorder characterized by a slow, gradual, progressive weakness and
CC spasticity of the lower limbs. Rate of progression and the severity of
CC symptoms are quite variable. Initial symptoms may include difficulty
CC with balance, weakness and stiffness in the legs, muscle spasms, and
CC dragging the toes when walking. Complicated forms are recognized by
CC additional variable features including spastic quadriparesis, seizures,
CC dementia, amyotrophy, extrapyramidal disturbance, cerebral or
CC cerebellar atrophy, optic atrophy, and peripheral neuropathy, as well
CC as by extra neurological manifestations. {ECO:0000269|PubMed:23188110,
CC ECO:0000269|PubMed:24080142, ECO:0000269|PubMed:24198383,
CC ECO:0000269|PubMed:26380172}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000305}.
CC -!- CAUTION: In contrast to other members of the family, lacks the regions
CC that come into close contact with the mRNA in the ribosomal A-site and
CC determine the STOP codon specificity, suggesting a loss of codon
CC specificity for translation release factor activity. {ECO:0000305}.
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DR EMBL; AF061733; AAG43144.1; -; mRNA.
DR EMBL; AK095982; BAC04665.1; -; mRNA.
DR EMBL; CH471054; EAW98395.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW98396.1; -; Genomic_DNA.
DR EMBL; BC018145; AAH18145.1; -; mRNA.
DR EMBL; BC020885; AAH20885.1; -; mRNA.
DR EMBL; BC062329; AAH62329.1; -; mRNA.
DR CCDS; CCDS9244.1; -. [Q9H3J6-1]
DR RefSeq; NP_001137377.1; NM_001143905.2. [Q9H3J6-1]
DR RefSeq; NP_001181924.1; NM_001194995.1. [Q9H3J6-1]
DR RefSeq; NP_689482.1; NM_152269.4. [Q9H3J6-1]
DR RefSeq; XP_005253687.1; XM_005253630.4. [Q9H3J6-1]
DR RefSeq; XP_011537282.1; XM_011538980.2. [Q9H3J6-1]
DR PDB; 7A5H; EM; 3.30 A; C=1-166.
DR PDBsum; 7A5H; -.
DR AlphaFoldDB; Q9H3J6; -.
DR SMR; Q9H3J6; -.
DR BioGRID; 124847; 227.
DR IntAct; Q9H3J6; 3.
DR STRING; 9606.ENSP00000253233; -.
DR iPTMnet; Q9H3J6; -.
DR PhosphoSitePlus; Q9H3J6; -.
DR BioMuta; C12orf65; -.
DR DMDM; 74733574; -.
DR EPD; Q9H3J6; -.
DR MassIVE; Q9H3J6; -.
DR MaxQB; Q9H3J6; -.
DR PaxDb; Q9H3J6; -.
DR PeptideAtlas; Q9H3J6; -.
DR PRIDE; Q9H3J6; -.
DR ProteomicsDB; 80723; -. [Q9H3J6-1]
DR ProteomicsDB; 80724; -. [Q9H3J6-2]
DR TopDownProteomics; Q9H3J6-1; -. [Q9H3J6-1]
DR Antibodypedia; 31771; 58 antibodies from 16 providers.
DR DNASU; 91574; -.
DR Ensembl; ENST00000253233.6; ENSP00000253233.1; ENSG00000130921.9. [Q9H3J6-1]
DR Ensembl; ENST00000366329.7; ENSP00000390647.1; ENSG00000130921.9. [Q9H3J6-1]
DR Ensembl; ENST00000425637.3; ENSP00000506680.1; ENSG00000130921.9. [Q9H3J6-2]
DR Ensembl; ENST00000429587.2; ENSP00000391513.2; ENSG00000130921.9. [Q9H3J6-1]
DR Ensembl; ENST00000536130.2; ENSP00000443072.2; ENSG00000130921.9. [Q9H3J6-1]
DR Ensembl; ENST00000538888.6; ENSP00000505059.1; ENSG00000130921.9. [Q9H3J6-2]
DR Ensembl; ENST00000543139.2; ENSP00000444843.2; ENSG00000130921.9. [Q9H3J6-1]
DR Ensembl; ENST00000546132.2; ENSP00000441796.2; ENSG00000130921.9. [Q9H3J6-2]
DR Ensembl; ENST00000679849.1; ENSP00000505808.1; ENSG00000130921.9. [Q9H3J6-1]
DR Ensembl; ENST00000680325.1; ENSP00000505277.1; ENSG00000130921.9. [Q9H3J6-2]
DR GeneID; 91574; -.
DR KEGG; hsa:91574; -.
DR MANE-Select; ENST00000253233.6; ENSP00000253233.1; NM_152269.5; NP_689482.1.
DR UCSC; uc001uen.4; human. [Q9H3J6-1]
DR CTD; 91574; -.
DR DisGeNET; 91574; -.
DR GeneCards; MTRFR; -.
DR HGNC; HGNC:26784; MTRFR.
DR HPA; ENSG00000130921; Tissue enhanced (lymphoid).
DR MalaCards; MTRFR; -.
DR MIM; 613541; gene.
DR MIM; 613559; phenotype.
DR MIM; 615035; phenotype.
DR neXtProt; NX_Q9H3J6; -.
DR OpenTargets; ENSG00000130921; -.
DR Orphanet; 320375; Autosomal recessive spastic paraplegia type 55.
DR Orphanet; 254930; Combined oxidative phosphorylation defect type 7.
DR VEuPathDB; HostDB:ENSG00000130921; -.
DR eggNOG; KOG2726; Eukaryota.
DR GeneTree; ENSGT00390000012759; -.
DR InParanoid; Q9H3J6; -.
DR OMA; WESSKNI; -.
DR OrthoDB; 1415962at2759; -.
DR PhylomeDB; Q9H3J6; -.
DR TreeFam; TF323274; -.
DR PathwayCommons; Q9H3J6; -.
DR SignaLink; Q9H3J6; -.
DR BioGRID-ORCS; 91574; 60 hits in 1073 CRISPR screens.
DR ChiTaRS; C12orf65; human.
DR GenomeRNAi; 91574; -.
DR Pharos; Q9H3J6; Tbio.
DR PRO; PR:Q9H3J6; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9H3J6; protein.
DR Bgee; ENSG00000130921; Expressed in thymus and 185 other tissues.
DR ExpressionAtlas; Q9H3J6; baseline and differential.
DR Genevisible; Q9H3J6; HS.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0043023; F:ribosomal large subunit binding; IDA:UniProtKB.
DR GO; GO:0003747; F:translation release factor activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
DR GO; GO:0072344; P:rescue of stalled ribosome; IDA:UniProtKB.
DR InterPro; IPR000352; Pep_chain_release_fac_I.
DR InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR Pfam; PF00472; RF-1; 1.
DR SUPFAM; SSF75620; SSF75620; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Disease variant;
KW Hereditary spastic paraplegia; Mitochondrion; Neurodegeneration;
KW Primary mitochondrial disease; Protein biosynthesis; Reference proteome;
KW RNA-binding; Transit peptide.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..166
FT /note="Mitochondrial translation release factor in rescue"
FT /id="PRO_0000311835"
FT REGION 57..121
FT /note="GGQ domain"
FT /evidence="ECO:0000250|UniProtKB:Q80VP5"
FT REGION 122..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 127..160
FT /evidence="ECO:0000255"
FT MOTIF 71..73
FT /note="GGQ"
FT /evidence="ECO:0000269|PubMed:24198383"
FT VAR_SEQ 95..119
FT /note="CHQTRSVDQNRKLARKILQEKVDVF -> VDHRRPLRGEAPPKGSTASRDFS
FT QV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029602"
FT VAR_SEQ 120..166
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029603"
FT VARIANT 83..166
FT /note="VLKHIPSGIVVKCHQTRSVDQNRKLARKILQEKVDVFYNGENSPVHKEKREA
FT AKKKQERKKRAKETLEKKKLLKELWESSKKVH -> G (in COXPD7; decreased
FT cytochrome c oxidase activity in fibroblasts; severe
FT assembly defects in mitochondrial complexes I, IV and V
FT with a milder defect in the assembly of complex III; no
FT effect on mitochondrial transcripts, rRNAs and tRNAs
FT levels)"
FT /evidence="ECO:0000269|PubMed:20598281"
FT /id="VAR_084490"
FT VARIANT 116..166
FT /note="Missing (in SPG55 and COXPD7; decreased activity of
FT mitochondrial respiratory chain; no effect on mitochondrial
FT morphology)"
FT /evidence="ECO:0000269|PubMed:24198383,
FT ECO:0000269|PubMed:25995486"
FT /id="VAR_084491"
FT VARIANT 132..166
FT /note="Missing (in SPG55)"
FT /evidence="ECO:0000269|PubMed:23188110"
FT /id="VAR_084492"
FT VARIANT 134
FT /note="A -> T (in dbSNP:rs1045496)"
FT /id="VAR_037325"
FT VARIANT 139..166
FT /note="Missing (in SPG55)"
FT /evidence="ECO:0000269|PubMed:24080142"
FT /id="VAR_084493"
SQ SEQUENCE 166 AA; 18828 MW; CB9B74E0CC7E920C CRC64;
MSTVGLFHFP TPLTRICPAP WGLRLWEKLT LLSPGIAVTP VQMAGKKDYP ALLSLDENEL
EEQFVKGHGP GGQATNKTSN CVVLKHIPSG IVVKCHQTRS VDQNRKLARK ILQEKVDVFY
NGENSPVHKE KREAAKKKQE RKKRAKETLE KKKLLKELWE SSKKVH
