COA1_HUMAN
ID COA1_HUMAN Reviewed; 146 AA.
AC Q9GZY4; A6NJU8; A8KAH8; Q9HAB7; Q9NVD2;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Cytochrome c oxidase assembly factor 1 homolog {ECO:0000305};
DE AltName: Full=Mitochondrial translation regulation assembly intermediate of cytochrome c oxidase protein of 15 kDa;
GN Name=COA1 {ECO:0000312|HGNC:HGNC:21868}; Synonyms=C7orf44, MITRAC15;
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=Embryo, and Uterus;
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=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
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=Skin;
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 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, SUBCELLULAR LOCATION, IDENTIFICATION IN MITRAC COMPLEX, AND
RP TOPOLOGY.
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 [7]
RP INTERACTION WITH COX17 AND COA6, AND SUBCELLULAR LOCATION.
RX PubMed=22356826; DOI=10.1186/gb-2012-13-2-r12;
RA Szklarczyk R., Wanschers B.F., Cuypers T.D., Esseling J.J., Riemersma M.,
RA van den Brand M.A., Gloerich J., Lasonder E., van den Heuvel L.P.,
RA Nijtmans L.G., Huynen M.A.;
RT "Iterative orthology prediction uncovers new mitochondrial proteins and
RT identifies C12orf62 as the human ortholog of COX14, a protein involved in
RT the assembly of cytochrome c oxidase.";
RL Genome Biol. 13:RESEARCH0012.1-RESEARCH0012.14(2012).
RN [8]
RP IDENTIFICATION IN THE MCIA COMPLEX, AND FUNCTION.
RX PubMed=32320651; DOI=10.1016/j.celrep.2020.107541;
RA Formosa L.E., Muellner-Wong L., Reljic B., Sharpe A.J., Jackson T.D.,
RA Beilharz T.H., Stojanovski D., Lazarou M., Stroud D.A., Ryan M.T.;
RT "Dissecting the Roles of Mitochondrial Complex I Intermediate Assembly
RT Complex Factors in the Biogenesis of Complex I.";
RL Cell Rep. 31:107541-107541(2020).
CC -!- FUNCTION: Component of the MITRAC (mitochondrial translation regulation
CC assembly intermediate of cytochrome c oxidase complex) complex, that
CC regulates cytochrome c oxidase assembly. MITRAC complexes regulate both
CC translation of mitochondrial encoded components and assembly of
CC nuclear-encoded components imported in mitochondrion. Required for
CC assembly of mitochondrial respiratory chain complex I and complex IV
CC (PubMed:23260140). As part of the MCIA complex, required for efficient
CC assembly of the mitochondrial complex I (PubMed:32320651).
CC {ECO:0000269|PubMed:23260140, ECO:0000269|PubMed:32320651}.
CC -!- SUBUNIT: Component of the MITRAC (mitochondrial translation regulation
CC assembly intermediate of cytochrome c oxidase complex) complex, the
CC core components of this complex being COA3/MITRAC12 and COX14.
CC Interacts with COX17 and COA6. Part of the mitochondrial complex I
CC assembly/MCIA complex that comprises at least the core subunits
CC TMEM126B, NDUFAF1, ECSIT and ACAD9 and complement subunits such as COA1
CC and TMEM186 (PubMed:32320651). {ECO:0000269|PubMed:22356826,
CC ECO:0000269|PubMed:23260140, ECO:0000269|PubMed:32320651}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:22356826, ECO:0000269|PubMed:23260140}; Single-pass
CC membrane protein {ECO:0000269|PubMed:22356826,
CC ECO:0000269|PubMed:23260140}.
CC -!- SIMILARITY: Belongs to the COA1 family. {ECO:0000305}.
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DR EMBL; AK001665; BAA91821.1; -; mRNA.
DR EMBL; AK021905; BAB13932.1; -; mRNA.
DR EMBL; AK023007; BAB14356.1; -; mRNA.
DR EMBL; AK023053; BAB14379.1; -; mRNA.
DR EMBL; AK293043; BAF85732.1; -; mRNA.
DR EMBL; AC005189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471073; EAW94165.1; -; Genomic_DNA.
DR EMBL; BC056884; AAH56884.1; -; mRNA.
DR CCDS; CCDS5471.1; -.
DR RefSeq; NP_001308126.1; NM_001321197.1.
DR RefSeq; NP_001308127.1; NM_001321198.1.
DR RefSeq; NP_001308128.1; NM_001321199.1.
DR RefSeq; NP_001308129.1; NM_001321200.1.
DR RefSeq; NP_060694.2; NM_018224.3.
DR RefSeq; XP_005249864.1; XM_005249807.4.
DR RefSeq; XP_006715815.1; XM_006715752.2.
DR RefSeq; XP_016867903.1; XM_017012414.1.
DR RefSeq; XP_016867904.1; XM_017012415.1.
DR RefSeq; XP_016867905.1; XM_017012416.1.
DR RefSeq; XP_016867906.1; XM_017012417.1.
DR RefSeq; XP_016867907.1; XM_017012418.1.
DR RefSeq; XP_016867908.1; XM_017012419.1.
DR RefSeq; XP_016867910.1; XM_017012421.1.
DR RefSeq; XP_016867911.1; XM_017012422.1.
DR RefSeq; XP_016867912.1; XM_017012423.1.
DR RefSeq; XP_016867913.1; XM_017012424.1.
DR RefSeq; XP_016867914.1; XM_017012425.1.
DR RefSeq; XP_016867915.1; XM_017012426.1.
DR RefSeq; XP_016867916.1; XM_017012427.1.
DR RefSeq; XP_016867917.1; XM_017012428.1.
DR RefSeq; XP_016867918.1; XM_017012429.1.
DR RefSeq; XP_016867919.1; XM_017012430.1.
DR RefSeq; XP_016867920.1; XM_017012431.1.
DR RefSeq; XP_016867921.1; XM_017012432.1.
DR AlphaFoldDB; Q9GZY4; -.
DR SMR; Q9GZY4; -.
DR BioGRID; 120862; 29.
DR ComplexPortal; CPX-6322; Mitochondrial complex I intermediate assembly (MCIA) complex.
DR CORUM; Q9GZY4; -.
DR IntAct; Q9GZY4; 16.
DR STRING; 9606.ENSP00000379218; -.
DR iPTMnet; Q9GZY4; -.
DR PhosphoSitePlus; Q9GZY4; -.
DR BioMuta; COA1; -.
DR DMDM; 74733508; -.
DR EPD; Q9GZY4; -.
DR jPOST; Q9GZY4; -.
DR MassIVE; Q9GZY4; -.
DR MaxQB; Q9GZY4; -.
DR PaxDb; Q9GZY4; -.
DR PeptideAtlas; Q9GZY4; -.
DR PRIDE; Q9GZY4; -.
DR ProteomicsDB; 80173; -.
DR TopDownProteomics; Q9GZY4; -.
DR Antibodypedia; 2314; 84 antibodies from 15 providers.
DR DNASU; 55744; -.
DR Ensembl; ENST00000223336.11; ENSP00000223336.6; ENSG00000106603.20.
DR Ensembl; ENST00000310564.10; ENSP00000312100.6; ENSG00000106603.20.
DR Ensembl; ENST00000395879.5; ENSP00000379218.1; ENSG00000106603.20.
DR Ensembl; ENST00000415076.6; ENSP00000400759.1; ENSG00000106603.20.
DR Ensembl; ENST00000438444.5; ENSP00000395586.1; ENSG00000106603.20.
DR Ensembl; ENST00000446330.6; ENSP00000416406.1; ENSG00000106603.20.
DR Ensembl; ENST00000446564.5; ENSP00000413777.1; ENSG00000106603.20.
DR GeneID; 55744; -.
DR KEGG; hsa:55744; -.
DR MANE-Select; ENST00000223336.11; ENSP00000223336.6; NM_018224.4; NP_060694.2.
DR UCSC; uc003tin.2; human.
DR CTD; 55744; -.
DR DisGeNET; 55744; -.
DR GeneCards; COA1; -.
DR HGNC; HGNC:21868; COA1.
DR HPA; ENSG00000106603; Low tissue specificity.
DR MIM; 614769; gene.
DR neXtProt; NX_Q9GZY4; -.
DR OpenTargets; ENSG00000106603; -.
DR PharmGKB; PA162380473; -.
DR VEuPathDB; HostDB:ENSG00000106603; -.
DR eggNOG; ENOG502S561; Eukaryota.
DR GeneTree; ENSGT00440000033985; -.
DR HOGENOM; CLU_117249_0_0_1; -.
DR InParanoid; Q9GZY4; -.
DR OMA; HPIRSKF; -.
DR OrthoDB; 1443294at2759; -.
DR PhylomeDB; Q9GZY4; -.
DR TreeFam; TF324468; -.
DR PathwayCommons; Q9GZY4; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-6799198; Complex I biogenesis.
DR SignaLink; Q9GZY4; -.
DR BioGRID-ORCS; 55744; 18 hits in 1076 CRISPR screens.
DR ChiTaRS; COA1; human.
DR GenomeRNAi; 55744; -.
DR Pharos; Q9GZY4; Tbio.
DR PRO; PR:Q9GZY4; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9GZY4; protein.
DR Bgee; ENSG00000106603; Expressed in secondary oocyte and 189 other tissues.
DR ExpressionAtlas; Q9GZY4; baseline and differential.
DR Genevisible; Q9GZY4; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
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 InterPro; IPR014807; Coa1.
DR Pfam; PF08695; Coa1; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..146
FT /note="Cytochrome c oxidase assembly factor 1 homolog"
FT /id="PRO_0000279407"
FT TOPO_DOM 1..14
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..146
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT CONFLICT 2
FT /note="M -> T (in Ref. 1; BAB13932)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="A -> V (in Ref. 1; BAA91821)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="H -> R (in Ref. 1; BAB13932)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 146 AA; 16694 MW; 24582046A282291C CRC64;
MMWQKYAGSR RSMPLGARIL FHGVFYAGGF AIVYYLIQKF HSRALYYKLA VEQLQSHPEA
QEALGPPLNI HYLKLIDREN FVDIVDAKLK IPVSGSKSEG LLYVHSSRGG PFQRWHLDEV
FLELKDGQQI PVFKLSGENG DEVKKE
