MC25A_DANRE
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 03-AUG-2022, entry version 89.
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}.
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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 AlphaFoldDB; Q63ZW2; -.
DR SMR; Q63ZW2; -.
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; LRCYRDN; -.
DR OrthoDB; 1234703at2759; -.
DR PhylomeDB; Q63ZW2; -.
DR TreeFam; TF333651; -.
DR PRO; PR:Q63ZW2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 23.
DR Bgee; ENSDARG00000003206; Expressed in testis and 26 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 InterPro; IPR007964; MIC19/MIC25.
DR Pfam; PF05300; MIC19_MIC25; 1.
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 REGION 27..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 COMPBIAS 34..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
