COX16_MOUSE
ID COX16_MOUSE Reviewed; 106 AA.
AC Q9CR63; Q8BNX4; Q99J15;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Cytochrome c oxidase assembly protein COX16 homolog, mitochondrial {ECO:0000305};
GN Name=Cox16 {ECO:0000312|MGI:MGI:1913522};
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Aorta, Cerebellum, Oviduct, Pancreas, Small intestine, Thymus, and
RC Vein;
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] (ISOFORM 2).
RC STRAIN=FVB/N-3; TISSUE=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).
CC -!- FUNCTION: Required for the assembly of the mitochondrial respiratory
CC chain complex IV (CIV), also known as cytochrome c oxidase. Promotes
CC the insertion of copper into the active site of cytochrome c oxidase
CC subunit II (MT-CO2/COX2). Interacts specifically with newly synthesized
CC MT-CO2/COX and its copper center-forming metallochaperones SCO1, SCO2
CC and COA6. Probably facilitates MT-CO2/COX2 association with the MITRAC
CC assembly intermediate containing MT-CO1/COX1, thereby participating in
CC merging the MT-CO1/COX1 and MT-CO2/COX2 assembly lines.
CC {ECO:0000250|UniProtKB:Q9P0S2}.
CC -!- SUBUNIT: Associates with the MITRAC complex. Interacts with MT-CO2/COX;
CC specifically interacts with newly synthesized MT-CO2/COX. Interacts
CC with SCO1, SCO2 and COA6. {ECO:0000250|UniProtKB:Q9P0S2}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9P0S2}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9P0S2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CR63-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CR63-2; Sequence=VSP_014603;
CC -!- SIMILARITY: Belongs to the COX16 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK007450; BAB25045.1; -; mRNA.
DR EMBL; AK007562; BAB25110.1; -; mRNA.
DR EMBL; AK008486; BAB25693.1; -; mRNA.
DR EMBL; AK040003; BAC30495.1; -; mRNA.
DR EMBL; AK079975; BAC37796.1; -; mRNA.
DR EMBL; AK082374; BAC38480.1; -; mRNA.
DR EMBL; AK087666; BAC39960.1; -; mRNA.
DR EMBL; AK088794; BAC40576.1; -; mRNA.
DR EMBL; BC005675; AAH05675.1; -; mRNA.
DR CCDS; CCDS26020.1; -. [Q9CR63-1]
DR CCDS; CCDS83976.1; -. [Q9CR63-2]
DR RefSeq; NP_001296737.1; NM_001309808.1.
DR RefSeq; NP_001296738.1; NM_001309809.2. [Q9CR63-2]
DR RefSeq; NP_001296739.1; NM_001309810.2.
DR RefSeq; NP_079737.1; NM_025461.6. [Q9CR63-1]
DR AlphaFoldDB; Q9CR63; -.
DR STRING; 10090.ENSMUSP00000002757; -.
DR PhosphoSitePlus; Q9CR63; -.
DR SwissPalm; Q9CR63; -.
DR MaxQB; Q9CR63; -.
DR PaxDb; Q9CR63; -.
DR PeptideAtlas; Q9CR63; -.
DR PRIDE; Q9CR63; -.
DR ProteomicsDB; 284147; -. [Q9CR63-1]
DR ProteomicsDB; 284148; -. [Q9CR63-2]
DR Antibodypedia; 25128; 57 antibodies from 16 providers.
DR DNASU; 66272; -.
DR Ensembl; ENSMUST00000002757; ENSMUSP00000002757; ENSMUSG00000091803. [Q9CR63-1]
DR Ensembl; ENSMUST00000110340; ENSMUSP00000105969; ENSMUSG00000091803. [Q9CR63-2]
DR GeneID; 66272; -.
DR KEGG; mmu:66272; -.
DR UCSC; uc007oce.1; mouse. [Q9CR63-1]
DR CTD; 51241; -.
DR MGI; MGI:1913522; Cox16.
DR VEuPathDB; HostDB:ENSMUSG00000091803; -.
DR eggNOG; ENOG502S3RD; Eukaryota.
DR GeneTree; ENSGT00520000055955; -.
DR HOGENOM; CLU_163592_0_0_1; -.
DR InParanoid; Q9CR63; -.
DR OMA; RTMTFGV; -.
DR OrthoDB; 1550606at2759; -.
DR PhylomeDB; Q9CR63; -.
DR TreeFam; TF324420; -.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR BioGRID-ORCS; 66272; 16 hits in 73 CRISPR screens.
DR PRO; PR:Q9CR63; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9CR63; protein.
DR Bgee; ENSMUSG00000091803; Expressed in spermatocyte and 233 other tissues.
DR ExpressionAtlas; Q9CR63; baseline and differential.
DR Genevisible; Q9CR63; MM.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; ISS:UniProtKB.
DR InterPro; IPR020164; Cyt_c_Oxase_assmbl_COX16.
DR Pfam; PF14138; COX16; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..106
FT /note="Cytochrome c oxidase assembly protein COX16 homolog,
FT mitochondrial"
FT /id="PRO_0000019557"
FT TOPO_DOM 1..15
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q9P0S2"
FT TRANSMEM 16..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..106
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q9P0S2"
FT REGION 81..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 69..106
FT /note="KIKDSTFENWKNIRGPRPWEDPQLLQGRNPETLKPKTT -> RLLCLLCRQ
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_014603"
FT CONFLICT 40
FT /note="R -> Q (in Ref. 1; BAC37796)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 106 AA; 12266 MW; 1A765726532211B0 CRC64;
MIAPAVLRAL RKNKTLRYGV PMLLLVVGGS FGLREFSQIR YDAVTIKIDP ELEKKLKVNK
ITLESEYEKI KDSTFENWKN IRGPRPWEDP QLLQGRNPET LKPKTT