COA7_HUMAN
ID COA7_HUMAN Reviewed; 231 AA.
AC Q96BR5; Q0P6I7; Q9H9Z9;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Cytochrome c oxidase assembly factor 7;
DE AltName: Full=Beta-lactamase hcp-like protein;
DE AltName: Full=Respiratory chain assembly factor 1;
DE AltName: Full=Sel1 repeat-containing protein 1;
GN Name=COA7; Synonyms=C1orf163, RESA1, SELRC1;
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], AND VARIANT ARG-219.
RC TISSUE=Teratocarcinoma;
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=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-219.
RC TISSUE=Bone marrow, and Prostate;
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 [4]
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=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [5]
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24333015; DOI=10.1016/j.jmb.2013.12.001;
RA Kozjak-Pavlovic V., Prell F., Thiede B., Gotz M., Wosiek D., Ott C.,
RA Rudel T.;
RT "C1orf163/RESA1 is a novel mitochondrial intermembrane space protein
RT connected to respiratory chain assembly.";
RL J. Mol. Biol. 426:908-920(2014).
RN [7]
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 [8]
RP INVOLVEMENT IN SCAN3, AND VARIANT SCAN3 CYS-137.
RX PubMed=27683825; DOI=10.1136/jmedgenet-2016-104194;
RA Martinez Lyons A., Ardissone A., Reyes A., Robinson A.J., Moroni I.,
RA Ghezzi D., Fernandez-Vizarra E., Zeviani M.;
RT "COA7 (C1orf163/RESA1) mutations associated with mitochondrial
RT leukoencephalopathy and cytochrome c oxidase deficiency.";
RL J. Med. Genet. 53:846-849(2016).
RN [9]
RP INVOLVEMENT IN SCAN3, AND VARIANTS SCAN3 GLY-6; TRP-39 AND ILE-149.
RX PubMed=29718187; DOI=10.1093/brain/awy104;
RA Higuchi Y., Okunushi R., Hara T., Hashiguchi A., Yuan J., Yoshimura A.,
RA Murayama K., Ohtake A., Ando M., Hiramatsu Y., Ishihara S., Tanabe H.,
RA Okamoto Y., Matsuura E., Ueda T., Toda T., Yamashita S., Yamada K.,
RA Koide T., Yaguchi H., Mitsui J., Ishiura H., Yoshimura J., Doi K.,
RA Morishita S., Sato K., Nakagawa M., Yamaguchi M., Tsuji S., Takashima H.;
RT "Mutations in COA7 cause spinocerebellar ataxia with axonal neuropathy.";
RL Brain 141:1622-1636(2018).
RN [10]
RP INTERACTION WITH CHCHD4, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF
RP VARIANT SCAN3 CYS-137.
RX PubMed=30885959; DOI=10.15252/emmm.201809561;
RA Mohanraj K., Wasilewski M., Beninca C., Cysewski D., Poznanski J.,
RA Sakowska P., Bugajska Z., Deckers M., Dennerlein S., Fernandez-Vizarra E.,
RA Rehling P., Dadlez M., Zeviani M., Chacinska A.;
RT "Inhibition of proteasome rescues a pathogenic variant of respiratory chain
RT assembly factor COA7.";
RL EMBO Mol. Med. 11:0-0(2019).
CC -!- FUNCTION: Required for assembly of mitochondrial respiratory chain
CC complex I and complex IV. {ECO:0000269|PubMed:24333015}.
CC -!- SUBUNIT: Interacts with CHCHD4/MIA40 through transient intermolecular
CC disulfide bonds. {ECO:0000269|PubMed:30885959}.
CC -!- INTERACTION:
CC Q96BR5; P55212: CASP6; NbExp=3; IntAct=EBI-6269632, EBI-718729;
CC Q96BR5; P99999: CYCS; NbExp=3; IntAct=EBI-6269632, EBI-446479;
CC Q96BR5; G5E9A7: DMWD; NbExp=3; IntAct=EBI-6269632, EBI-10976677;
CC Q96BR5; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-6269632, EBI-744099;
CC Q96BR5; P22607: FGFR3; NbExp=3; IntAct=EBI-6269632, EBI-348399;
CC Q96BR5; Q9Y4H4: GPSM3; NbExp=3; IntAct=EBI-6269632, EBI-347538;
CC Q96BR5; P06396: GSN; NbExp=3; IntAct=EBI-6269632, EBI-351506;
CC Q96BR5; P30519: HMOX2; NbExp=3; IntAct=EBI-6269632, EBI-712096;
CC Q96BR5; P13473-2: LAMP2; NbExp=3; IntAct=EBI-6269632, EBI-21591415;
CC Q96BR5; D3DTS7: PMP22; NbExp=3; IntAct=EBI-6269632, EBI-25882629;
CC Q96BR5; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-6269632, EBI-5280197;
CC Q96BR5; P62826: RAN; NbExp=3; IntAct=EBI-6269632, EBI-286642;
CC Q96BR5; P14678-2: SNRPB; NbExp=3; IntAct=EBI-6269632, EBI-372475;
CC Q96BR5; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-6269632, EBI-5235340;
CC Q96BR5; P51687: SUOX; NbExp=3; IntAct=EBI-6269632, EBI-3921347;
CC Q96BR5; Q08117-2: TLE5; NbExp=3; IntAct=EBI-6269632, EBI-11741437;
CC Q96BR5; Q9Y649; NbExp=3; IntAct=EBI-6269632, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:24333015, ECO:0000269|PubMed:30885959}. Note=The
CC import in the mitochondrion intermembrane space is mediated by
CC CHCHD4/MIA40. {ECO:0000269|PubMed:30885959}.
CC -!- DISEASE: Spinocerebellar ataxia, autosomal recessive, with axonal
CC neuropathy 3 (SCAN3) [MIM:618387]: A form of spinocerebellar ataxia, a
CC clinically and genetically heterogeneous group of cerebellar disorders
CC due to degeneration of the cerebellum with variable involvement of the
CC brainstem and spinal cord. SCAN3 is an autosomal recessive disorder
CC characterized by onset in the first decade of slowly progressive distal
CC muscle weakness and atrophy and distal sensory impairment due to an
CC axonal peripheral neuropathy. Affected individuals have gait
CC disturbances and sometimes manual dexterity difficulties, as well as
CC cerebellar ataxia associated with cerebellar atrophy on brain imaging.
CC {ECO:0000269|PubMed:27683825, ECO:0000269|PubMed:29718187,
CC ECO:0000269|PubMed:30885959}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the hcp beta-lactamase family. {ECO:0000305}.
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DR EMBL; AK022501; BAB14063.1; -; mRNA.
DR EMBL; AC099784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015313; AAH15313.1; -; mRNA.
DR CCDS; CCDS570.1; -.
DR RefSeq; NP_075565.2; NM_023077.2.
DR PDB; 7MQZ; X-ray; 2.39 A; A=1-231.
DR PDBsum; 7MQZ; -.
DR AlphaFoldDB; Q96BR5; -.
DR SMR; Q96BR5; -.
DR BioGRID; 122417; 126.
DR IntAct; Q96BR5; 48.
DR MINT; Q96BR5; -.
DR STRING; 9606.ENSP00000360593; -.
DR GlyGen; Q96BR5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96BR5; -.
DR PhosphoSitePlus; Q96BR5; -.
DR BioMuta; COA7; -.
DR DMDM; 223590164; -.
DR EPD; Q96BR5; -.
DR jPOST; Q96BR5; -.
DR MassIVE; Q96BR5; -.
DR MaxQB; Q96BR5; -.
DR PaxDb; Q96BR5; -.
DR PeptideAtlas; Q96BR5; -.
DR PRIDE; Q96BR5; -.
DR ProteomicsDB; 76102; -.
DR Antibodypedia; 33027; 106 antibodies from 16 providers.
DR DNASU; 65260; -.
DR Ensembl; ENST00000371538.5; ENSP00000360593.3; ENSG00000162377.6.
DR GeneID; 65260; -.
DR KEGG; hsa:65260; -.
DR MANE-Select; ENST00000371538.5; ENSP00000360593.3; NM_023077.3; NP_075565.2.
DR UCSC; uc001cui.3; human.
DR CTD; 65260; -.
DR DisGeNET; 65260; -.
DR GeneCards; COA7; -.
DR HGNC; HGNC:25716; COA7.
DR HPA; ENSG00000162377; Low tissue specificity.
DR MalaCards; COA7; -.
DR MIM; 615623; gene.
DR MIM; 618387; phenotype.
DR neXtProt; NX_Q96BR5; -.
DR OpenTargets; ENSG00000162377; -.
DR PharmGKB; PA142672414; -.
DR VEuPathDB; HostDB:ENSG00000162377; -.
DR eggNOG; KOG4014; Eukaryota.
DR GeneTree; ENSGT00390000004835; -.
DR HOGENOM; CLU_000288_36_9_1; -.
DR InParanoid; Q96BR5; -.
DR OMA; THFEKAC; -.
DR OrthoDB; 1341787at2759; -.
DR PhylomeDB; Q96BR5; -.
DR TreeFam; TF105805; -.
DR PathwayCommons; Q96BR5; -.
DR SignaLink; Q96BR5; -.
DR BioGRID-ORCS; 65260; 338 hits in 1079 CRISPR screens.
DR ChiTaRS; COA7; human.
DR GenomeRNAi; 65260; -.
DR Pharos; Q96BR5; Tbio.
DR PRO; PR:Q96BR5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96BR5; protein.
DR Bgee; ENSG00000162377; Expressed in secondary oocyte and 199 other tissues.
DR Genevisible; Q96BR5; HS.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR040239; HcpB-like.
DR InterPro; IPR006597; Sel1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR13891; PTHR13891; 1.
DR Pfam; PF08238; Sel1; 4.
DR SMART; SM00671; SEL1; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Disease variant; Mitochondrion;
KW Neurodegeneration; Neuropathy; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..231
FT /note="Cytochrome c oxidase assembly factor 7"
FT /id="PRO_0000282364"
FT REPEAT 34..66
FT /note="Sel1-like 1"
FT REPEAT 68..104
FT /note="Sel1-like 2"
FT REPEAT 108..146
FT /note="Sel1-like 3"
FT REPEAT 147..183
FT /note="Sel1-like 4"
FT REPEAT 184..219
FT /note="Sel1-like 5"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT VARIANT 6
FT /note="D -> G (in SCAN3; dbSNP:rs780572767)"
FT /evidence="ECO:0000269|PubMed:29718187"
FT /id="VAR_082218"
FT VARIANT 39
FT /note="R -> W (in SCAN3; unknown pathological significance;
FT dbSNP:rs768084335)"
FT /evidence="ECO:0000269|PubMed:29718187"
FT /id="VAR_082219"
FT VARIANT 137
FT /note="Y -> C (in SCAN3; results in increased proteasomal
FT degradation; decreased protein levels; decreased amount of
FT protein imported in the mitochondrion intermembrane space;
FT dbSNP:rs961876891)"
FT /evidence="ECO:0000269|PubMed:27683825,
FT ECO:0000269|PubMed:30885959"
FT /id="VAR_082220"
FT VARIANT 149
FT /note="S -> I (in SCAN3; unknown pathological significance;
FT dbSNP:rs1558102448)"
FT /evidence="ECO:0000269|PubMed:29718187"
FT /id="VAR_082221"
FT VARIANT 219
FT /note="K -> R (in dbSNP:rs443751)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_031401"
FT CONFLICT 77
FT /note="Y -> H (in Ref. 1; BAB14063)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 231 AA; 25709 MW; DB7E2BEDCC0ECE8B CRC64;
MAGMVDFQDE EQVKSFLENM EVECNYHCYH EKDPDGCYRL VDYLEGIRKN FDEAAKVLKF
NCEENQHSDS CYKLGAYYVT GKGGLTQDLK AAARCFLMAC EKPGKKSIAA CHNVGLLAHD
GQVNEDGQPD LGKARDYYTR ACDGGYTSSC FNLSAMFLQG APGFPKDMDL ACKYSMKACD
LGHIWACANA SRMYKLGDGV DKDEAKAEVL KNRAQQLHKE QQKGVQPLTF G
