MIC60_RAT
ID MIC60_RAT Reviewed; 609 AA.
AC Q3KR86;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=MICOS complex subunit Mic60;
DE AltName: Full=Mitochondrial inner membrane protein {ECO:0000250|UniProtKB:Q8CAQ8, ECO:0000312|EMBL:AAI05842.1};
DE AltName: Full=Mitofilin {ECO:0000250|UniProtKB:Q8CAQ8};
DE Flags: Precursor; Fragment;
GN Name=Immt {ECO:0000312|EMBL:AAI05842.1, ECO:0000312|RGD:1310684};
GN Synonyms=Mic60;
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] {ECO:0000312|EMBL:AAI05842.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway {ECO:0000269|PubMed:15489334};
RC TISSUE=Testis {ECO:0000312|EMBL:AAI05842.1};
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 [2] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Maurya D.K., Bhargava P.;
RL Submitted (JAN-2009) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, 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. Plays an important
CC role in the maintenance of the MICOS complex stability and the
CC mitochondrial cristae morphology. {ECO:0000250|UniProtKB:Q16891}.
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 (By similarity). This complex was also known under
CC the names MINOS or MitOS complex. The MICOS complex associates with
CC mitochondrial outer membrane proteins SAMM50, MTX1 and MTX2 (together
CC described as components of the mitochondrial outer membrane sorting
CC assembly machinery (SAM) complex) and DNAJC11, mitochondrial inner
CC membrane protein TMEM11 and with HSPA9 (By similarity). The MICOS and
CC SAM complexes together with DNAJC11 are part of a large protein complex
CC spanning both membranes termed the mitochondrial intermembrane space
CC bridging (MIB) complex (By similarity). Interacts with HSPA1A/HSPA1B
CC and OPA1, preferentially with the soluble OPA1 form (By similarity).
CC Interacts with MICOS13/MIC13, MICOS10/MIC10, CHCHD3/MIC19,
CC CHCHD6/MIC25, SAMM50 and TMEM11 (By similarity). Interacts with
CC APOO/MIC23/MIC26 and APOOL/MIC27 (By similarity). Interacts with ARMC1
CC (By similarity). Interacts with ARMC12 (By similarity).
CC {ECO:0000250|UniProtKB:Q16891, ECO:0000250|UniProtKB:Q8CAQ8}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q16891}; Single-pass membrane protein
CC {ECO:0000255}. Mitochondrion {ECO:0000250|UniProtKB:Q16891}.
CC -!- SIMILARITY: Belongs to the MICOS complex subunit Mic60 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI05842.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; BC105841; AAI05842.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001030100.1; NM_001034928.1.
DR AlphaFoldDB; Q3KR86; -.
DR SMR; Q3KR86; -.
DR BioGRID; 260179; 8.
DR IntAct; Q3KR86; 4.
DR MINT; Q3KR86; -.
DR STRING; 10116.ENSRNOP00000051091; -.
DR iPTMnet; Q3KR86; -.
DR PhosphoSitePlus; Q3KR86; -.
DR jPOST; Q3KR86; -.
DR PaxDb; Q3KR86; -.
DR PeptideAtlas; Q3KR86; -.
DR PRIDE; Q3KR86; -.
DR GeneID; 312444; -.
DR KEGG; rno:312444; -.
DR UCSC; RGD:1310684; rat.
DR CTD; 10989; -.
DR RGD; 1310684; Immt.
DR eggNOG; KOG1854; Eukaryota.
DR InParanoid; Q3KR86; -.
DR OrthoDB; 1073064at2759; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q3KR86; RN.
DR GO; GO:0061617; C:MICOS complex; ISO:RGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0042407; P:cristae formation; ISO:RGD.
DR GO; GO:0051560; P:mitochondrial calcium ion homeostasis; ISO:RGD.
DR GO; GO:0009409; P:response to cold; IEP:RGD.
DR InterPro; IPR019133; Mt-IM_prot_Mitofilin.
DR PANTHER; PTHR15415; PTHR15415; 1.
DR Pfam; PF09731; Mitofilin; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..>609
FT /note="MICOS complex subunit Mic60"
FT /id="PRO_0000397215"
FT TOPO_DOM 34..45
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..>609
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REGION 127..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 232..270
FT /evidence="ECO:0000255"
FT COILED 350..397
FT /evidence="ECO:0000255"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16891"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16891"
FT MOD_RES 174
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16891"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16891"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16891"
FT MOD_RES 403
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16891"
FT NON_TER 609
FT /evidence="ECO:0000305"
SQ SEQUENCE 609 AA; 67177 MW; FB3AE72D9F570AA7 CRC64;
MLRACQLSGV TVAAQSCLCG KFVLRPLRPC RRYSTSSSSG VTAGKIAGAG LLFVGGGIGG
TILYAKWDSH FRESVEKTIP YSDKLFGMVL GSAPYTVPLP KKPIQSGPLK ISSVSEVMTD
SELPMAQTQE TNGDTPASAA GDPAPEVEHE DTINTECPNT DEGTSTFVTA ALAKSLEDAL
NQTATVTRQT ITAQNAAVQA VKAHSSTLKT AMDNSEIAGE KKSAQWRTVE GALKERRKAV
DEAADALLKA KEELEKMKTI IEDAKKREIA GATPYITAAE EKLHSMIVDL DSVVKKVQAA
QSEAKVVSQY HELVVQARDD FRKELDSITP DITPGWKGMS ISDLAGTLST DDLNALIAHA
HRRIDQLNRE LAQQKATEKQ HIELALERQK LEEKRAFDSA VAKALEHHRS EIQAEQDRKV
EEVRDAMENE MRTQLRRQAA AHTDHLRDVL KVQEQELKFE FEQDLSEKLS EQELEFHRRS
QEQMDNFTLD INTAYARLRG IEQAVQSHAV AEEEARKAHQ LWLSVEALKY SMKTSSAEMP
TIPLGSAVEA IRVSCSDNEF TQALTAAIPP ESLTRGVYSE ETLRARFYAV QKLAGRVAMI
DETKNSLYQ
