COXM1_MOUSE
ID COXM1_MOUSE Reviewed; 106 AA.
AC Q9CPZ8; Q6PH95; Q80ZR0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=COX assembly mitochondrial protein homolog;
DE Short=Cmc1p;
GN Name=Cmc1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, and Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Brain, and Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000250|UniProtKB:Q7Z7K0}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q7Z7K0}.
CC Note=Colocalizes with MT-CO1. {ECO:0000250|UniProtKB:Q7Z7K0}.
CC -!- SIMILARITY: Belongs to the CMC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH48547.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK020626; BAB32155.1; -; mRNA.
DR EMBL; AK168728; BAE40569.1; -; mRNA.
DR EMBL; BC048547; AAH48547.1; ALT_INIT; mRNA.
DR EMBL; BC056653; AAH56653.1; -; mRNA.
DR CCDS; CCDS40800.1; -.
DR RefSeq; NP_080718.1; NM_026442.3.
DR AlphaFoldDB; Q9CPZ8; -.
DR SMR; Q9CPZ8; -.
DR BioGRID; 212523; 7.
DR STRING; 10090.ENSMUSP00000047904; -.
DR iPTMnet; Q9CPZ8; -.
DR PhosphoSitePlus; Q9CPZ8; -.
DR EPD; Q9CPZ8; -.
DR jPOST; Q9CPZ8; -.
DR MaxQB; Q9CPZ8; -.
DR PaxDb; Q9CPZ8; -.
DR PeptideAtlas; Q9CPZ8; -.
DR PRIDE; Q9CPZ8; -.
DR ProteomicsDB; 285269; -.
DR Antibodypedia; 49957; 47 antibodies from 15 providers.
DR DNASU; 67899; -.
DR Ensembl; ENSMUST00000044220; ENSMUSP00000047904; ENSMUSG00000039163.
DR GeneID; 67899; -.
DR KEGG; mmu:67899; -.
DR UCSC; uc009rzl.2; mouse.
DR CTD; 152100; -.
DR MGI; MGI:1915149; Cmc1.
DR VEuPathDB; HostDB:ENSMUSG00000039163; -.
DR eggNOG; KOG4624; Eukaryota.
DR GeneTree; ENSGT00390000018696; -.
DR HOGENOM; CLU_142621_1_1_1; -.
DR InParanoid; Q9CPZ8; -.
DR OMA; FEECCKA; -.
DR OrthoDB; 1575179at2759; -.
DR PhylomeDB; Q9CPZ8; -.
DR TreeFam; TF314632; -.
DR BioGRID-ORCS; 67899; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Cmc1; mouse.
DR PRO; PR:Q9CPZ8; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9CPZ8; protein.
DR Bgee; ENSMUSG00000039163; Expressed in manus and 229 other tissues.
DR ExpressionAtlas; Q9CPZ8; baseline and differential.
DR Genevisible; Q9CPZ8; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
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:0000250|UniProtKB:Q7Z7K0"
FT CHAIN 2..106
FT /note="COX assembly mitochondrial protein homolog"
FT /id="PRO_0000317186"
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:0000250|UniProtKB:Q7Z7K0"
FT DISULFID 31..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 41..53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT CONFLICT 23
FT /note="I -> M (in Ref. 2; AAH56653)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 106 AA; 12553 MW; E23A6A0AB9381D8F CRC64;
MALDPAEQHL RHVEKDVLIP KIIREKARER CSEQVEDFTR CCKDSGILMV LKCRKENSAL
KDCLTAYYND PAFYEECKLE YLKEREEFRK TGVPTKKRLQ KLPTNM
