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Protein

MICOS complex subunit Mic25

Gene

Chchd6

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.By similarity

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
MICOS complex subunit Mic25
Alternative name(s):
Coiled-coil-helix-coiled-coil-helix domain-containing protein 6
Gene namesi
Name:Chchd6
Synonyms:Mic25
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi1304561. Chchd6.

Subcellular locationi

  • Mitochondrion inner membrane By similarity; Lipid-anchor By similarity
  • Mitochondrion By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedSequence analysis
Chaini2 – 261260MICOS complex subunit Mic25PRO_0000416909Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineSequence analysis
Modified residuei13 – 131PhosphoserineBy similarity
Modified residuei31 – 311PhosphoserineBy similarity
Modified residuei33 – 331PhosphoserineCombined sources
Disulfide bondi223 ↔ 254By similarity
Disulfide bondi233 ↔ 244By similarity

Keywords - PTMi

Disulfide bond, Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiD4A7N1.
PeptideAtlasiD4A7N1.
PRIDEiD4A7N1.

PTM databases

iPTMnetiD4A7N1.

Expressioni

Gene expression databases

GenevisibleiD4A7N1. RN.

Interactioni

Subunit structurei

Component of the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MINOS1/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and QIL1/MIC13. This complex was also known under the names MINOS or MitOS complex. The MICOS complex associates with mitochondrial outer membrane proteins SAMM50, MTX1, MTX2 and DNAJC11, mitochondrial inner membrane protein TMEM11 and with HSPA9. Interacts with DISC1. Interacts with IMMT/MIC60.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000023122.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini216 – 25742CHCHAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili109 – 20294Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 CHCH domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4083. Eukaryota.
ENOG41126BR. LUCA.
GeneTreeiENSGT00390000000903.
InParanoidiD4A7N1.
KOiK17564.
OMAiLRAPHKE.
OrthoDBiEOG7NW6C3.
PhylomeDBiD4A7N1.
TreeFamiTF326279.

Family and domain databases

InterProiIPR007964. DUF737.
[Graphical view]
PfamiPF05300. DUF737. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

D4A7N1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSSESAEAR RVSFEMDEEE RVRVLQGIRL SESVVNRMKD CSQPSAGEQL
60 70 80 90 100
APGPGPECSV PVPTVPQPTI PVLTVPSPSV CGPAEGTYKA PQGDFKVSRA
110 120 130 140 150
ENSDGQQSSA VKEDLKKFQQ EQLAVQDELV KVARKEKEAT EKHLKASLPK
160 170 180 190 200
KKATHEQQQS DRLTRELKNR EAELSRRDTF YKEQQERIQE KNAELYKLSS
210 220 230 240 250
QQFHEAASKA ESTIKPRRVE PVCSGLQAQI LRCYRDHLHE VLLCSDLAKA
260
YQHCVSTARK G
Length:261
Mass (Da):29,211
Last modified:April 20, 2010 - v1
Checksum:iFF8DFC638481E424
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473957 Genomic DNA. Translation: EDL91332.1.
RefSeqiNP_001100078.1. NM_001106608.1.
UniGeneiRn.6212.

Genome annotation databases

EnsembliENSRNOT00000088753; ENSRNOP00000073575; ENSRNOG00000060248.
GeneIDi297436.
KEGGirno:297436.
UCSCiRGD:1304561. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473957 Genomic DNA. Translation: EDL91332.1.
RefSeqiNP_001100078.1. NM_001106608.1.
UniGeneiRn.6212.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000023122.

PTM databases

iPTMnetiD4A7N1.

Proteomic databases

PaxDbiD4A7N1.
PeptideAtlasiD4A7N1.
PRIDEiD4A7N1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000088753; ENSRNOP00000073575; ENSRNOG00000060248.
GeneIDi297436.
KEGGirno:297436.
UCSCiRGD:1304561. rat.

Organism-specific databases

CTDi84303.
RGDi1304561. Chchd6.

Phylogenomic databases

eggNOGiKOG4083. Eukaryota.
ENOG41126BR. LUCA.
GeneTreeiENSGT00390000000903.
InParanoidiD4A7N1.
KOiK17564.
OMAiLRAPHKE.
OrthoDBiEOG7NW6C3.
PhylomeDBiD4A7N1.
TreeFamiTF326279.

Miscellaneous databases

PROiD4A7N1.

Gene expression databases

GenevisibleiD4A7N1. RN.

Family and domain databases

InterProiIPR007964. DUF737.
[Graphical view]
PfamiPF05300. DUF737. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMIC25_RAT
AccessioniPrimary (citable) accession number: D4A7N1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2012
Last sequence update: April 20, 2010
Last modified: July 6, 2016
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.