COXM1_HUMAN
ID COXM1_HUMAN Reviewed; 106 AA.
AC Q7Z7K0; Q68DJ7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=COX assembly mitochondrial protein homolog;
DE Short=Cmc1p;
GN Name=CMC1; Synonyms=C3orf68;
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=Liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
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 [3]
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 [4]
RP SUBCELLULAR LOCATION.
RX PubMed=18443040; DOI=10.1128/mcb.01920-07;
RA Horn D., Al-Ali H., Barrientos A.;
RT "Cmc1p is a conserved mitochondrial twin CX(9)C protein involved in
RT cytochrome c oxidase biogenesis.";
RL Mol. Cell. Biol. 28:4354-4364(2008).
RN [5]
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 [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 IDENTIFICATION IN SOME MITRAC 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 [8]
RP SUBCELLULAR LOCATION, AND DISULFIDE BONDS.
RX PubMed=23676665; DOI=10.1091/mbc.e12-12-0862;
RA Fischer M., Horn S., Belkacemi A., Kojer K., Petrungaro C., Habich M.,
RA Ali M., Kuettner V., Bien M., Kauff F., Dengjel J., Herrmann J.M.,
RA Riemer J.;
RT "Protein import and oxidative folding in the mitochondrial intermembrane
RT space of intact mammalian cells.";
RL Mol. Biol. Cell 24:2160-2170(2013).
RN [9]
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=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: Component of the MITRAC (mitochondrial translation regulation
CC assembly intermediate of cytochrome c oxidase complex) complex, that
CC regulates cytochrome c oxidase assembly. {ECO:0000250}.
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 {ECO:0000269|PubMed:23260140}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18443040,
CC ECO:0000269|PubMed:23676665}. Note=Colocalizes with MT-CO1.
CC -!- SIMILARITY: Belongs to the CMC family. {ECO:0000305}.
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DR EMBL; CR749370; CAH18223.1; -; mRNA.
DR EMBL; CH471055; EAW64390.1; -; Genomic_DNA.
DR EMBL; BC052644; AAH52644.1; -; mRNA.
DR CCDS; CCDS33722.1; -.
DR RefSeq; NP_872329.1; NM_182523.1.
DR AlphaFoldDB; Q7Z7K0; -.
DR SMR; Q7Z7K0; -.
DR BioGRID; 127426; 11.
DR CORUM; Q7Z7K0; -.
DR IntAct; Q7Z7K0; 5.
DR MINT; Q7Z7K0; -.
DR STRING; 9606.ENSP00000418348; -.
DR iPTMnet; Q7Z7K0; -.
DR PhosphoSitePlus; Q7Z7K0; -.
DR BioMuta; CMC1; -.
DR DMDM; 74738888; -.
DR EPD; Q7Z7K0; -.
DR jPOST; Q7Z7K0; -.
DR MassIVE; Q7Z7K0; -.
DR MaxQB; Q7Z7K0; -.
DR PaxDb; Q7Z7K0; -.
DR PeptideAtlas; Q7Z7K0; -.
DR PRIDE; Q7Z7K0; -.
DR ProteomicsDB; 69555; -.
DR Antibodypedia; 49957; 47 antibodies from 15 providers.
DR DNASU; 152100; -.
DR Ensembl; ENST00000466830.6; ENSP00000418348.1; ENSG00000187118.14.
DR GeneID; 152100; -.
DR KEGG; hsa:152100; -.
DR MANE-Select; ENST00000466830.6; ENSP00000418348.1; NM_182523.2; NP_872329.1.
DR UCSC; uc003cea.4; human.
DR CTD; 152100; -.
DR DisGeNET; 152100; -.
DR GeneCards; CMC1; -.
DR HGNC; HGNC:28783; CMC1.
DR HPA; ENSG00000187118; Low tissue specificity.
DR MIM; 615166; gene.
DR neXtProt; NX_Q7Z7K0; -.
DR OpenTargets; ENSG00000187118; -.
DR PharmGKB; PA162382538; -.
DR VEuPathDB; HostDB:ENSG00000187118; -.
DR eggNOG; KOG4624; Eukaryota.
DR GeneTree; ENSGT00390000018696; -.
DR HOGENOM; CLU_142621_1_1_1; -.
DR InParanoid; Q7Z7K0; -.
DR OMA; FEECCKA; -.
DR OrthoDB; 1575179at2759; -.
DR PhylomeDB; Q7Z7K0; -.
DR TreeFam; TF314632; -.
DR PathwayCommons; Q7Z7K0; -.
DR SignaLink; Q7Z7K0; -.
DR BioGRID-ORCS; 152100; 148 hits in 1045 CRISPR screens.
DR ChiTaRS; CMC1; human.
DR GenomeRNAi; 152100; -.
DR Pharos; Q7Z7K0; Tdark.
DR PRO; PR:Q7Z7K0; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q7Z7K0; protein.
DR Bgee; ENSG00000187118; Expressed in granulocyte and 178 other tissues.
DR ExpressionAtlas; Q7Z7K0; baseline and differential.
DR Genevisible; Q7Z7K0; HS.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR013892; Cyt_c_biogenesis_Cmc1-like.
DR PANTHER; PTHR22977; PTHR22977; 1.
DR Pfam; PF08583; Cmc1; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Copper; Disulfide bond; Metal-binding; Mitochondrion;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..106
FT /note="COX assembly mitochondrial protein homolog"
FT /id="PRO_0000317185"
FT DOMAIN 28..71
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 31..41
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 53..63
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:25944712"
FT DISULFID 31..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150,
FT ECO:0000305|PubMed:23676665"
FT DISULFID 41..53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150,
FT ECO:0000305|PubMed:23676665"
FT CONFLICT 68
FT /note="Missing (in Ref. 1; CAH18223)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 106 AA; 12490 MW; CBC29CCCB76BA721 CRC64;
MALDPADQHL RHVEKDVLIP KIMREKAKER CSEQVQDFTK CCKNSGVLMV VKCRKENSAL
KECLTAYYND PAFYEECKME YLKEREEFRK TGIPTKKRLQ KLPTSM
