MIC60_MOUSE
ID MIC60_MOUSE Reviewed; 757 AA.
AC Q8CAQ8; Q66JS4; Q7TNE2; Q8C7V1; Q8CCI0; Q8CDA8; Q9D9F6;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=MICOS complex subunit Mic60;
DE AltName: Full=Mitochondrial inner membrane protein;
DE AltName: Full=Mitofilin;
DE Flags: Precursor;
GN Name=Immt; Synonyms=Mic60;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 503-757 (ISOFORM 5).
RC STRAIN=C57BL/6J; TISSUE=Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP PROTEIN SEQUENCE OF 353-365; 395-409; 581-599 AND 672-688, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 475-757.
RC STRAIN=Czech II, and FVB/N; TISSUE=Kidney, and Mammary tumor;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-506, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INTERACTION WITH CHCHD3 AND OPA1.
RX PubMed=21081504; DOI=10.1074/jbc.m110.171975;
RA Darshi M., Mendiola V.L., Mackey M.R., Murphy A.N., Koller A.,
RA Perkins G.A., Ellisman M.H., Taylor S.S.;
RT "ChChd3, an inner mitochondrial membrane protein, is essential for
RT maintaining crista integrity and mitochondrial function.";
RL J. Biol. Chem. 286:2918-2932(2011).
RN [7]
RP INTERACTION WITH ARMC12.
RX PubMed=33536340; DOI=10.1073/pnas.2018355118;
RA Shimada K., Park S., Miyata H., Yu Z., Morohoshi A., Oura S., Matzuk M.M.,
RA Ikawa M.;
RT "ARMC12 regulates spatiotemporal mitochondrial dynamics during
RT spermiogenesis and is required for male fertility.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
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 MICOS13/MIC13,
CC MICOS10/MIC10, CHCHD6/MIC25, SAMM50 and TMEM11 (By similarity).
CC Interacts with CHCHD3/MIC19 (PubMed:21081504). Interacts with
CC APOO/MIC23/MIC26 and APOOL/MIC27 (By similarity). Interacts with
CC HSPA1A/HSPA1B and OPA1, preferentially with the soluble OPA1 form
CC (PubMed:21081504). Interacts with ARMC1 (By similarity). Interacts with
CC ARMC12 (PubMed:33536340). {ECO:0000250|UniProtKB:Q16891,
CC ECO:0000269|PubMed:21081504, ECO:0000269|PubMed:33536340}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q16891}; Single-pass membrane protein
CC {ECO:0000255}. Mitochondrion {ECO:0000250|UniProtKB:Q16891}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8CAQ8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CAQ8-2; Sequence=VSP_007003;
CC Name=3;
CC IsoId=Q8CAQ8-3; Sequence=VSP_007003, VSP_007004, VSP_007005;
CC Name=4;
CC IsoId=Q8CAQ8-4; Sequence=VSP_007003, VSP_013222, VSP_013223;
CC Name=5;
CC IsoId=Q8CAQ8-5; Sequence=VSP_013224;
CC -!- MISCELLANEOUS: [Isoform 4]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MICOS complex subunit Mic60 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB24817.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB24817.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK006977; BAB24817.1; ALT_SEQ; mRNA.
DR EMBL; AK030841; BAC27154.1; -; mRNA.
DR EMBL; AK033126; BAC28163.1; -; mRNA.
DR EMBL; AK038129; BAC29936.1; -; mRNA.
DR EMBL; AK049189; BAC33599.1; -; mRNA.
DR EMBL; BC055840; AAH55840.1; -; mRNA.
DR EMBL; BC080790; AAH80790.1; -; mRNA.
DR CCDS; CCDS39509.1; -. [Q8CAQ8-1]
DR CCDS; CCDS57425.1; -. [Q8CAQ8-2]
DR CCDS; CCDS57426.1; -. [Q8CAQ8-3]
DR RefSeq; NP_001240610.1; NM_001253681.1. [Q8CAQ8-2]
DR RefSeq; NP_001240616.1; NM_001253687.1. [Q8CAQ8-3]
DR RefSeq; NP_001240617.1; NM_001253688.1.
DR RefSeq; NP_083949.2; NM_029673.3. [Q8CAQ8-1]
DR AlphaFoldDB; Q8CAQ8; -.
DR SMR; Q8CAQ8; -.
DR BioGRID; 218208; 50.
DR CORUM; Q8CAQ8; -.
DR DIP; DIP-32050N; -.
DR IntAct; Q8CAQ8; 44.
DR MINT; Q8CAQ8; -.
DR STRING; 10090.ENSMUSP00000066181; -.
DR iPTMnet; Q8CAQ8; -.
DR PhosphoSitePlus; Q8CAQ8; -.
DR SwissPalm; Q8CAQ8; -.
DR REPRODUCTION-2DPAGE; Q8CAQ8; -.
DR EPD; Q8CAQ8; -.
DR jPOST; Q8CAQ8; -.
DR MaxQB; Q8CAQ8; -.
DR PaxDb; Q8CAQ8; -.
DR PeptideAtlas; Q8CAQ8; -.
DR PRIDE; Q8CAQ8; -.
DR ProteomicsDB; 290234; -. [Q8CAQ8-1]
DR ProteomicsDB; 290235; -. [Q8CAQ8-2]
DR ProteomicsDB; 290236; -. [Q8CAQ8-3]
DR ProteomicsDB; 290237; -. [Q8CAQ8-4]
DR ProteomicsDB; 290238; -. [Q8CAQ8-5]
DR Antibodypedia; 32043; 353 antibodies from 35 providers.
DR DNASU; 76614; -.
DR Ensembl; ENSMUST00000064062; ENSMUSP00000066181; ENSMUSG00000052337. [Q8CAQ8-1]
DR Ensembl; ENSMUST00000101301; ENSMUSP00000098859; ENSMUSG00000052337. [Q8CAQ8-2]
DR Ensembl; ENSMUST00000114151; ENSMUSP00000109788; ENSMUSG00000052337. [Q8CAQ8-3]
DR GeneID; 76614; -.
DR KEGG; mmu:76614; -.
DR UCSC; uc009che.2; mouse. [Q8CAQ8-4]
DR UCSC; uc009chi.2; mouse. [Q8CAQ8-1]
DR UCSC; uc009chj.2; mouse. [Q8CAQ8-2]
DR UCSC; uc009chm.2; mouse. [Q8CAQ8-3]
DR CTD; 10989; -.
DR MGI; MGI:1923864; Immt.
DR VEuPathDB; HostDB:ENSMUSG00000052337; -.
DR eggNOG; KOG1854; Eukaryota.
DR GeneTree; ENSGT00390000002313; -.
DR InParanoid; Q8CAQ8; -.
DR OMA; STYEAFS; -.
DR OrthoDB; 1073064at2759; -.
DR PhylomeDB; Q8CAQ8; -.
DR TreeFam; TF312832; -.
DR BioGRID-ORCS; 76614; 15 hits in 72 CRISPR screens.
DR ChiTaRS; Immt; mouse.
DR PRO; PR:Q8CAQ8; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8CAQ8; protein.
DR Bgee; ENSMUSG00000052337; Expressed in myocardium of ventricle and 257 other tissues.
DR ExpressionAtlas; Q8CAQ8; baseline and differential.
DR Genevisible; Q8CAQ8; MM.
DR GO; GO:0061617; C:MICOS complex; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0042407; P:cristae formation; ISO:MGI.
DR GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IMP:MGI.
DR GO; GO:0070050; P:neuron cellular homeostasis; IMP:MGI.
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; Alternative splicing; Coiled coil; Direct protein sequencing;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..757
FT /note="MICOS complex subunit Mic60"
FT /id="PRO_0000084185"
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..757
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REGION 164..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 199..231
FT /evidence="ECO:0000255"
FT COILED 279..317
FT /evidence="ECO:0000255"
FT COILED 397..442
FT /evidence="ECO:0000255"
FT COMPBIAS 173..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 210
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16891"
FT MOD_RES 221
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16891"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3KR86"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16891"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16891"
FT MOD_RES 450
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16891"
FT MOD_RES 506
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT VAR_SEQ 141..151
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007003"
FT VAR_SEQ 186..218
FT /note="EEAFSSSVRERPPEEVAARLAQQEKQEQVEMES -> A (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007004"
FT VAR_SEQ 186..194
FT /note="EEAFSSSVR -> GSLIIYIML (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013222"
FT VAR_SEQ 195..757
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013223"
FT VAR_SEQ 387..392
FT /note="SISDLA -> T (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007005"
FT VAR_SEQ 757
FT /note="E -> FWIKAVFKSQMSNPTSFKVTRLNSVQKNRSSPLI (in isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013224"
FT CONFLICT 532
FT /note="D -> E (in Ref. 1; BAB24817)"
FT /evidence="ECO:0000305"
FT CONFLICT 658
FT /note="F -> L (in Ref. 1; BAB24817)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 757 AA; 83900 MW; 5EB37BCA054BD7A6 CRC64;
MLRACQLSGV TVAAQSCLCG KFVLRPLRPC RRYSTSSSSG LTAGKIAGAG LLFVGGGIGG
TILYAKWDSH FRESVEKTIP YSDKLFGMVL GSAPYTVPLP KKPVQSGPLK ISSVSEVMKD
SKLPVAQSQK TKGDTPASAA STGAAQIISA AGDTLSVPAP AVQHEDTIKT ECPNTNEGKS
TSETTEEAFS SSVRERPPEE VAARLAQQEK QEQVEMESLA KSLEDALNRT SSVTLQTITA
QNAAVQAVKA HSNILKTAMD NSEIAGEKKS AQWRTVEGAL KERRKAVDEA ADALLKAKEE
LEKMKTIIED AKKREIAGAT PHITAAEGRL HNMIVDLDNV VKKVQAAQSE AKVVSQYHEL
VVQARDDFRK ELDSITPDIT PGWKGMSISD LAGKLSTDDL NSLIAHAHRR IDQLNRELAQ
QKATEKQHIE LALEKHKLEE KRTFDSAVAK ALEHHRSEIQ AEQDRKVEEV RDAMENEMRT
QLRRQAAAHT DHLRDVLKVQ EQELKYEFEQ GLSEKLSEQE LEFRRRSQEQ MDSFTLDINT
AYARLRGIEQ AVQSHAVAEE EARKAHQLWL SVEALKYSMK TSSAEMPTIP LGSAVEAIRV
NCSDNEFTQA LTAAIPPESL TRGVYSEETL RARFYAVQKL ARRVAMIDET RNSLYQYFLS
YLQSLLLFPP KQLKPPAELY PEDINTFKLL SYASYCIEHG DLELAAKFVN QLKGESRRVA
QDWLKEARMT LETKQIVEIL TAYASAVGIG TTQVQQE
