COX11_HUMAN
ID COX11_HUMAN Reviewed; 276 AA.
AC Q9Y6N1; D3DTY5; I3L220; Q6FHB7; Q9BRX0; Q9UME8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Cytochrome c oxidase assembly protein COX11, mitochondrial;
DE Flags: Precursor;
GN Name=COX11;
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 [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=9878253; DOI=10.1006/geno.1998.5580;
RA Petruzzella V., Tiranti V., Fernandez P., Ianna P., Carrozzo R.,
RA Zeviani M.;
RT "Identification and characterization of human cDNAs specific to BCS1,
RT PET112, SCO1, COX15, and COX11, five genes involved in the formation and
RT function of the mitochondrial respiratory chain.";
RL Genomics 54:494-504(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Hypothalamus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 125-276 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9110174; DOI=10.1101/gr.7.4.353;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [7]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=15229189; DOI=10.1093/hmg/ddh197;
RA Leary S.C., Kaufman B.A., Pellecchia G., Guercin G.H., Mattman A.,
RA Jaksch M., Shoubridge E.A.;
RT "Human SCO1 and SCO2 have independent, cooperative functions in copper
RT delivery to cytochrome c oxidase.";
RL Hum. Mol. Genet. 13:1839-1848(2004).
RN [8]
RP INTERACTION WITH CNNM4.
RX PubMed=15840172; DOI=10.1186/1744-8069-1-15;
RA Guo D., Ling J., Wang M.-H., She J.-X., Gu J., Wang C.-Y.;
RT "Physical interaction and functional coupling between ACDP4 and the
RT intracellular ion chaperone COX11, an implication of the role of ACDP4 in
RT essential metal ion transport and homeostasis.";
RL Mol. Pain 1:15-15(2005).
RN [9]
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 [10]
RP INTERACTION WITH RANBP2.
RX PubMed=34400285; DOI=10.1016/j.neulet.2021.136173;
RA Shibata A., Kasai M., Hoshino A., Tanaka T., Mizuguchi M.;
RT "RANBP2 mutation causing autosomal dominant acute necrotizing
RT encephalopathy attenuates its interaction with COX11.";
RL Neurosci. Lett. 763:136173-136173(2021).
CC -!- FUNCTION: Exerts its effect at some terminal stage of cytochrome c
CC oxidase synthesis, probably by being involved in the insertion of the
CC copper B into subunit I. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CNNM4/ACDP4. Interacts with RANBP2
CC (PubMed:34400285). {ECO:0000269|PubMed:15840172,
CC ECO:0000269|PubMed:34400285}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:15229189, ECO:0000269|PubMed:9878253}; Single-pass
CC membrane protein {ECO:0000269|PubMed:9878253}; Intermembrane side
CC {ECO:0000269|PubMed:9878253}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y6N1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y6N1-2; Sequence=VSP_046360;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9878253}.
CC -!- SIMILARITY: Belongs to the COX11/CtaG family. {ECO:0000305}.
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DR EMBL; AF044321; AAD08645.1; -; mRNA.
DR EMBL; CR541837; CAG46636.1; -; mRNA.
DR EMBL; AC007485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94548.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94550.1; -; Genomic_DNA.
DR EMBL; BC005895; AAH05895.1; -; mRNA.
DR EMBL; BI600359; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; U79270; AAB50214.1; -; mRNA.
DR CCDS; CCDS11583.1; -. [Q9Y6N1-1]
DR CCDS; CCDS58579.1; -. [Q9Y6N1-2]
DR RefSeq; NP_004366.1; NM_004375.4. [Q9Y6N1-1]
DR RefSeq; XP_011522644.1; XM_011524342.2. [Q9Y6N1-1]
DR RefSeq; XP_016879681.1; XM_017024192.1. [Q9Y6N1-1]
DR RefSeq; XP_016879682.1; XM_017024193.1. [Q9Y6N1-1]
DR RefSeq; XP_016879683.1; XM_017024194.1.
DR RefSeq; XP_016879684.1; XM_017024195.1.
DR RefSeq; XP_016879685.1; XM_017024196.1. [Q9Y6N1-2]
DR AlphaFoldDB; Q9Y6N1; -.
DR SMR; Q9Y6N1; -.
DR BioGRID; 107746; 36.
DR IntAct; Q9Y6N1; 16.
DR STRING; 9606.ENSP00000299335; -.
DR iPTMnet; Q9Y6N1; -.
DR PhosphoSitePlus; Q9Y6N1; -.
DR BioMuta; COX11; -.
DR DMDM; 60416378; -.
DR EPD; Q9Y6N1; -.
DR jPOST; Q9Y6N1; -.
DR MassIVE; Q9Y6N1; -.
DR MaxQB; Q9Y6N1; -.
DR PaxDb; Q9Y6N1; -.
DR PeptideAtlas; Q9Y6N1; -.
DR PRIDE; Q9Y6N1; -.
DR ProteomicsDB; 46815; -.
DR ProteomicsDB; 86740; -. [Q9Y6N1-1]
DR Antibodypedia; 30833; 146 antibodies from 25 providers.
DR DNASU; 1353; -.
DR Ensembl; ENST00000299335.8; ENSP00000299335.3; ENSG00000166260.13. [Q9Y6N1-1]
DR Ensembl; ENST00000572558.5; ENSP00000459302.1; ENSG00000166260.13. [Q9Y6N1-2]
DR Ensembl; ENST00000576370.5; ENSP00000459901.1; ENSG00000166260.13. [Q9Y6N1-1]
DR GeneID; 1353; -.
DR KEGG; hsa:1353; -.
DR MANE-Select; ENST00000299335.8; ENSP00000299335.3; NM_004375.5; NP_004366.1.
DR UCSC; uc010wng.2; human. [Q9Y6N1-1]
DR CTD; 1353; -.
DR DisGeNET; 1353; -.
DR GeneCards; COX11; -.
DR HGNC; HGNC:2261; COX11.
DR HPA; ENSG00000166260; Low tissue specificity.
DR MIM; 603648; gene.
DR neXtProt; NX_Q9Y6N1; -.
DR OpenTargets; ENSG00000166260; -.
DR PharmGKB; PA26777; -.
DR VEuPathDB; HostDB:ENSG00000166260; -.
DR eggNOG; KOG2540; Eukaryota.
DR GeneTree; ENSGT00390000007512; -.
DR HOGENOM; CLU_045000_1_0_1; -.
DR InParanoid; Q9Y6N1; -.
DR OMA; NKLECFC; -.
DR OrthoDB; 1287401at2759; -.
DR PhylomeDB; Q9Y6N1; -.
DR TreeFam; TF105072; -.
DR PathwayCommons; Q9Y6N1; -.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR SignaLink; Q9Y6N1; -.
DR BioGRID-ORCS; 1353; 223 hits in 1079 CRISPR screens.
DR ChiTaRS; COX11; human.
DR GenomeRNAi; 1353; -.
DR Pharos; Q9Y6N1; Tbio.
DR PRO; PR:Q9Y6N1; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9Y6N1; protein.
DR Bgee; ENSG00000166260; Expressed in biceps brachii and 217 other tissues.
DR ExpressionAtlas; Q9Y6N1; baseline and differential.
DR Genevisible; Q9Y6N1; HS.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0031304; C:intrinsic component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
DR GO; GO:0055065; P:metal ion homeostasis; IDA:UniProtKB.
DR GO; GO:0033132; P:negative regulation of glucokinase activity; IEA:Ensembl.
DR Gene3D; 2.60.370.10; -; 1.
DR HAMAP; MF_00155; CtaG; 1.
DR InterPro; IPR023471; CtaG/Cox11_dom_sf.
DR InterPro; IPR007533; Cyt_c_oxidase_assmbl_CtaG.
DR Pfam; PF04442; CtaG_Cox11; 1.
DR SUPFAM; SSF110111; SSF110111; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Copper; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..276
FT /note="Cytochrome c oxidase assembly protein COX11,
FT mitochondrial"
FT /id="PRO_0000006080"
FT TOPO_DOM ?..95
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:15229189"
FT TRANSMEM 96..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..276
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:15229189"
FT REGION 64..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 217..276
FT /note="CFCFEEQRLNPQEEVDMPVFFYIDPEFAEDPRMIKVDLITLSYTFFEAKEGH
FT KLPVPGYN -> ASKLHRVYVLESWHL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046360"
FT VARIANT 74
FT /note="P -> L (in dbSNP:rs34080917)"
FT /id="VAR_048831"
FT CONFLICT 187
FT /note="A -> V (in Ref. 5; AAH05895)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9Y6N1-2:223
FT /note="V -> G (in Ref. 4; BI600359)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 276 AA; 31430 MW; 1F2BD22E1E7DD52D CRC64;
MGGLWRPGWR CVPFCGWRWI HPGSPTRAAE RVEPFLRPEW SGTGGAERGL RWLGTWKRCS
LRARHPALQP PRRPKSSNPF TRAQEEERRR QNKTTLTYVA AVAVGMLGAS YAAVPLYRLY
CQTTGLGGSA VAGHASDKIE NMVPVKDRII KISFNADVHA SLQWNFRPQQ TEIYVVPGET
ALAFYRAKNP TDKPVIGIST YNIVPFEAGQ YFNKIQCFCF EEQRLNPQEE VDMPVFFYID
PEFAEDPRMI KVDLITLSYT FFEAKEGHKL PVPGYN
