ID MC25A_DANRE Reviewed; 239 AA. AC Q63ZW2; DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 02-DEC-2020, entry version 85. DE RecName: Full=MICOS complex subunit mic25a; DE AltName: Full=Coiled-coil-helix-coiled-coil-helix domain-containing protein 6; GN Name=chchd6a; Synonyms=mic25a; ORFNames=zgc:91802; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Component of the MICOS complex, a large protein complex of CC the mitochondrial inner membrane that plays crucial roles in the CC maintenance of crista junctions, inner membrane architecture, and CC formation of contact sites to the outer membrane. CC {ECO:0000250|UniProtKB:Q9BRQ6}. CC -!- SUBUNIT: Component of the mitochondrial contact site and cristae CC organizing system (MICOS) complex (also known as MINOS or MitOS CC complex). {ECO:0000250|UniProtKB:Q9BRQ6}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:Q9BRQ6}; Lipid-anchor CC {ECO:0000250|UniProtKB:Q9BRQ6}. CC -!- SIMILARITY: Belongs to the MICOS complex subunit Mic19 family. Metazoan CC Mic25 subfamily. {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; AL954678; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC082793; AAH82793.1; -; mRNA. DR RefSeq; NP_001005584.1; NM_001005584.1. DR RefSeq; XP_005162369.1; XM_005162312.2. DR STRING; 7955.ENSDARP00000116560; -. DR PaxDb; Q63ZW2; -. DR DNASU; 449542; -. DR Ensembl; ENSDART00000143933; ENSDARP00000116560; ENSDARG00000003206. DR GeneID; 449542; -. DR KEGG; dre:449542; -. DR CTD; 449542; -. DR ZFIN; ZDB-GENE-040930-2; chchd6a. DR eggNOG; KOG4083; Eukaryota. DR GeneTree; ENSGT00390000000903; -. DR HOGENOM; CLU_049040_0_0_1; -. DR InParanoid; Q63ZW2; -. DR OMA; SENVVHR; -. DR OrthoDB; 1234703at2759; -. DR PhylomeDB; Q63ZW2; -. DR TreeFam; TF333651; -. DR PRO; PR:Q63ZW2; -. DR Proteomes; UP000000437; Chromosome 23. DR Bgee; ENSDARG00000003206; Expressed in testis and 31 other tissues. DR ExpressionAtlas; Q63ZW2; baseline. DR GO; GO:0061617; C:MICOS complex; IBA:GO_Central. DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB. DR GO; GO:0042407; P:cristae formation; ISS:UniProtKB. DR GO; GO:0007007; P:inner mitochondrial membrane organization; IBA:GO_Central. DR PROSITE; PS51808; CHCH; 1. PE 2: Evidence at transcript level; KW Coiled coil; Disulfide bond; Lipoprotein; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Myristate; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000255" FT CHAIN 2..239 FT /note="MICOS complex subunit mic25a" FT /id="PRO_0000416910" FT DOMAIN 192..234 FT /note="CHCH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150" FT COILED 79..166 FT /evidence="ECO:0000255" FT MOTIF 195..205 FT /note="Cx9C motif 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150" FT MOTIF 216..226 FT /note="Cx9C motif 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000255" FT DISULFID 195..226 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150" FT DISULFID 205..216 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150" SQ SEQUENCE 239 AA; 27540 MW; A215A00FAD26DBEA CRC64; MGSGESTTRR VSFGLDEDDR VRILRGVKLS EDVLQRMRNT NADPRPPANN KENQGHQTRT PSTSDAQAPK TQAKTTFPDS KEELKKRYEQ QQAIIQEELA RIARKEREAA RQDISRAVQR ERAQTRQESE RAKQLGKQLD KKEAELKALE AFYQEQITQL EKKNEERFRM SAEQFHAAAT RSEANIKARN VEPVCLNLQA QILNCYRENR EQTLQCSDLA KEYMQCINAA KKNLLVNHG //