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MIC25_RAT
ID   MIC25_RAT               Reviewed;         261 AA.
AC   D4A7N1;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=MICOS complex subunit Mic25;
DE   AltName: Full=Coiled-coil-helix-coiled-coil-helix domain-containing protein 6;
GN   Name=Chchd6; Synonyms=Mic25;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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, composed of at least MICOS10/MIC10,
CC       CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26
CC       and MICOS13/MIC13. This complex was also known under the names MINOS or
CC       MitOS complex. The MICOS complex associates with mitochondrial outer
CC       membrane proteins SAMM50, MTX1 and MTX2 (together described as
CC       components of the mitochondrial outer membrane sorting assembly
CC       machinery (SAM) complex) and DNAJC11, mitochondrial inner membrane
CC       protein TMEM11 and with HSPA9. The MICOS and SAM complexes together
CC       with DNAJC11 are part of a large protein complex spanning both
CC       membranes termed the mitochondrial intermembrane space bridging (MIB)
CC       complex. Interacts with DISC1. Interacts with IMMT/MIC60.
CC       {ECO:0000250|UniProtKB:Q9BRQ6}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q9BRQ6}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:Q9BRQ6}. Mitochondrion
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; CH473957; EDL91332.1; -; Genomic_DNA.
DR   RefSeq; NP_001100078.1; NM_001106608.1.
DR   AlphaFoldDB; D4A7N1; -.
DR   SMR; D4A7N1; -.
DR   BioGRID; 255582; 1.
DR   IntAct; D4A7N1; 1.
DR   MINT; D4A7N1; -.
DR   STRING; 10116.ENSRNOP00000023122; -.
DR   iPTMnet; D4A7N1; -.
DR   PhosphoSitePlus; D4A7N1; -.
DR   jPOST; D4A7N1; -.
DR   PaxDb; D4A7N1; -.
DR   PeptideAtlas; D4A7N1; -.
DR   PRIDE; D4A7N1; -.
DR   GeneID; 297436; -.
DR   KEGG; rno:297436; -.
DR   UCSC; RGD:1304561; rat.
DR   CTD; 84303; -.
DR   RGD; 1304561; Chchd6.
DR   VEuPathDB; HostDB:ENSRNOG00000060248; -.
DR   eggNOG; KOG4083; Eukaryota.
DR   HOGENOM; CLU_049040_0_0_1; -.
DR   InParanoid; D4A7N1; -.
DR   OMA; QHTAYLC; -.
DR   OrthoDB; 1234703at2759; -.
DR   PhylomeDB; D4A7N1; -.
DR   TreeFam; TF326279; -.
DR   PRO; PR:D4A7N1; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Proteomes; UP000234681; Chromosome 4.
DR   Bgee; ENSRNOG00000060248; Expressed in testis and 20 other tissues.
DR   Genevisible; D4A7N1; RN.
DR   GO; GO:0061617; C:MICOS complex; ISO:RGD.
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   InterPro; IPR007964; MIC19/MIC25.
DR   InterPro; IPR042860; MIC25.
DR   PANTHER; PTHR47609; PTHR47609; 1.
DR   Pfam; PF05300; MIC19_MIC25; 1.
DR   PROSITE; PS51808; CHCH; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Disulfide bond; Lipoprotein; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Myristate; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..261
FT                   /note="MICOS complex subunit Mic25"
FT                   /id="PRO_0000416909"
FT   DOMAIN          220..261
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   REGION          39..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          81..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          109..202
FT                   /evidence="ECO:0000255"
FT   MOTIF           223..233
FT                   /note="Cx9C motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           244..254
FT                   /note="Cx9C motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRQ6"
FT   MOD_RES         31
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VN4"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        223..254
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        233..244
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ   SEQUENCE   261 AA;  29211 MW;  FF8DFC638481E424 CRC64;
     MGSSESAEAR RVSFEMDEEE RVRVLQGIRL SESVVNRMKD CSQPSAGEQL APGPGPECSV
     PVPTVPQPTI PVLTVPSPSV CGPAEGTYKA PQGDFKVSRA ENSDGQQSSA VKEDLKKFQQ
     EQLAVQDELV KVARKEKEAT EKHLKASLPK KKATHEQQQS DRLTRELKNR EAELSRRDTF
     YKEQQERIQE KNAELYKLSS QQFHEAASKA ESTIKPRRVE PVCSGLQAQI LRCYRDHLHE
     VLLCSDLAKA YQHCVSTARK G
 
 
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