ID   MIC10_HUMAN             Reviewed;          78 AA.
AC   Q5TGZ0; Q96G68;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   02-OCT-2024, entry version 139.
DE   RecName: Full=MICOS complex subunit MIC10 {ECO:0000305};
DE   AltName: Full=Mitochondrial inner membrane organizing system protein 1;
GN   Name=MICOS10 {ECO:0000312|HGNC:HGNC:32068};
GN   Synonyms=C1orf151, MIC10, MINOS1 {ECO:0000312|HGNC:HGNC:32068};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Uterus;
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   [3]
RP   IDENTIFICATION IN THE MICOS COMPLEX, FUNCTION, SUBCELLULAR LOCATION, AND
RP   TOPOLOGY.
RX   PubMed=22114354; DOI=10.1091/mbc.e11-09-0774;
RA   Alkhaja A.K., Jans D.C., Nikolov M., Vukotic M., Lytovchenko O.,
RA   Ludewig F., Schliebs W., Riedel D., Urlaub H., Jakobs S., Deckers M.;
RT   "MINOS1 is a conserved component of mitofilin complexes and required for
RT   mitochondrial function and cristae organization.";
RL   Mol. Biol. Cell 23:247-257(2012).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [5]
RP   NOMENCLATURE.
RX   PubMed=24687277; DOI=10.1083/jcb.201401006;
RA   Pfanner N., van der Laan M., Amati P., Capaldi R.A., Caudy A.A.,
RA   Chacinska A., Darshi M., Deckers M., Hoppins S., Icho T., Jakobs S., Ji J.,
RA   Kozjak-Pavlovic V., Meisinger C., Odgren P.R., Park S.K., Rehling P.,
RA   Reichert A.S., Sheikh M.S., Taylor S.S., Tsuchida N., van der Bliek A.M.,
RA   van der Klei I.J., Weissman J.S., Westermann B., Zha J., Neupert W.,
RA   Nunnari J.;
RT   "Uniform nomenclature for the mitochondrial contact site and cristae
RT   organizing system.";
RL   J. Cell Biol. 204:1083-1086(2014).
RN   [6]
RP   INTERACTION WITH APOO; APOOL AND IMMT.
RX   PubMed=25764979; DOI=10.1016/j.bbamcr.2015.03.004;
RA   Koob S., Barrera M., Anand R., Reichert A.S.;
RT   "The non-glycosylated isoform of MIC26 is a constituent of the mammalian
RT   MICOS complex and promotes formation of crista junctions.";
RL   Biochim. Biophys. Acta 1853:1551-1563(2015).
RN   [7]
RP   INTERACTION WITH MICOS13 AND IMMT.
RX   PubMed=25997101; DOI=10.7554/elife.06265;
RA   Guarani V., McNeill E.M., Paulo J.A., Huttlin E.L., Froehlich F.,
RA   Gygi S.P., Van Vactor D., Harper J.W.;
RT   "QIL1 is a novel mitochondrial protein required for MICOS complex stability
RT   and cristae morphology.";
RL   Elife 4:0-0(2015).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [9]
RP   INTERACTION WITH ARMC1.
RX   PubMed=31644573; DOI=10.1371/journal.pone.0218303;
RA   Wagner F., Kunz T.C., Chowdhury S.R., Thiede B., Fraunholz M., Eger D.,
RA   Kozjak-Pavlovic V.;
RT   "Armadillo repeat-containing protein 1 is a dual localization protein
RT   associated with mitochondrial intermembrane space bridging complex.";
RL   PLoS ONE 14:e0218303-e0218303(2019).
RN   [10]
RP   FUNCTION.
RX   PubMed=33130824; DOI=10.1038/s41419-020-03152-y;
RA   Hu C., Shu L., Huang X., Yu J., Li L., Gong L., Yang M., Wu Z., Gao Z.,
RA   Zhao Y., Chen L., Song Z.;
RT   "OPA1 and MICOS Regulate mitochondrial crista dynamics and formation.";
RL   Cell Death Dis. 11:940-940(2020).
RN   [11]
RP   FUNCTION.
RX   PubMed=32567732; DOI=10.15252/embj.2019104105;
RA   Stephan T., Brueser C., Deckers M., Steyer A.M., Balzarotti F., Barbot M.,
RA   Behr T.S., Heim G., Huebner W., Ilgen P., Lange F., Pacheu-Grau D.,
RA   Pape J.K., Stoldt S., Huser T., Hell S.W., Moebius W., Rehling P.,
RA   Riedel D., Jakobs S.;
RT   "MICOS assembly controls mitochondrial inner membrane remodeling and crista
RT   junction redistribution to mediate cristae formation.";
RL   EMBO J. 39:e104105-e104105(2020).
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:0000269|PubMed:22114354, ECO:0000269|PubMed:32567732,
CC       ECO:0000269|PubMed:33130824}.
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 IMMT/MIC60 and MICOS13/MIC13. Interacts with
CC       APOO/MIC23/MIC26 and APOOL/MIC27. Interacts with ARMC1
CC       (PubMed:31644573). {ECO:0000269|PubMed:22114354,
CC       ECO:0000269|PubMed:25764979, ECO:0000269|PubMed:25997101,
CC       ECO:0000269|PubMed:31644573}.
CC   -!- INTERACTION:
CC       Q5TGZ0; P55056: APOC4; NbExp=3; IntAct=EBI-12886442, EBI-18302142;
CC       Q5TGZ0; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-12886442, EBI-7062247;
CC       Q5TGZ0; O95563: MPC2; NbExp=3; IntAct=EBI-12886442, EBI-719403;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:22114354}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:22114354}. Note=The C-terminus is located in the
CC       intermembrane space (By similarity), while the location of the N-
CC       terminus has not been determined yet. As some programs predict the
CC       presence of 2 closely apposed membrane domains, it has been proposed
CC       that the protein may cross the membrane twice and that both termini may
CC       face the intermembrane space (PubMed:22114354). {ECO:0000250,
CC       ECO:0000269|PubMed:22114354}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5TGZ0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5TGZ0-2; Sequence=VSP_042062, VSP_042063;
CC   -!- SIMILARITY: Belongs to the MICOS complex subunit Mic10 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH09927.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL031727; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC009927; AAH09927.1; ALT_INIT; mRNA.
DR   EMBL; BC070388; AAH70388.1; -; mRNA.
DR   CCDS; CCDS30620.1; -. [Q5TGZ0-1]
DR   RefSeq; NP_001027535.1; NM_001032363.3. [Q5TGZ0-1]
DR   AlphaFoldDB; Q5TGZ0; -.
DR   BioGRID; 136699; 83.
DR   ComplexPortal; CPX-6141; MICOS mitochondrial contact site and cristae organizing system complex.
DR   CORUM; Q5TGZ0; -.
DR   IntAct; Q5TGZ0; 3.
DR   STRING; 9606.ENSP00000325562; -.
DR   ChEMBL; CHEMBL4105956; -.
DR   TCDB; 8.A.156.1.2; the micos complex (micos-c) family.
DR   iPTMnet; Q5TGZ0; -.
DR   PhosphoSitePlus; Q5TGZ0; -.
DR   SwissPalm; Q5TGZ0; -.
DR   BioMuta; MINOS1; -.
DR   DMDM; 74746535; -.
DR   jPOST; Q5TGZ0; -.
DR   MassIVE; Q5TGZ0; -.
DR   PaxDb; 9606-ENSP00000325562; -.
DR   PeptideAtlas; Q5TGZ0; -.
DR   ProteomicsDB; 65135; -. [Q5TGZ0-1]
DR   ProteomicsDB; 65136; -. [Q5TGZ0-2]
DR   Pumba; Q5TGZ0; -.
DR   TopDownProteomics; Q5TGZ0-1; -. [Q5TGZ0-1]
DR   Antibodypedia; 29686; 110 antibodies from 17 providers.
DR   DNASU; 440574; -.
DR   Ensembl; ENST00000322753.7; ENSP00000325562.6; ENSG00000173436.15. [Q5TGZ0-1]
DR   GeneID; 440574; -.
DR   KEGG; hsa:440574; -.
DR   MANE-Select; ENST00000322753.7; ENSP00000325562.6; NM_001032363.4; NP_001027535.1.
DR   UCSC; uc001bci.3; human. [Q5TGZ0-1]
DR   AGR; HGNC:32068; -.
DR   CTD; 440574; -.
DR   DisGeNET; 440574; -.
DR   GeneCards; MICOS10; -.
DR   HGNC; HGNC:32068; MICOS10.
DR   HPA; ENSG00000173436; Low tissue specificity.
DR   MIM; 616574; gene.
DR   neXtProt; NX_Q5TGZ0; -.
DR   PharmGKB; PA142672468; -.
DR   VEuPathDB; HostDB:ENSG00000173436; -.
DR   eggNOG; KOG4604; Eukaryota.
DR   GeneTree; ENSGT00390000005732; -.
DR   HOGENOM; CLU_068905_2_1_1; -.
DR   InParanoid; Q5TGZ0; -.
DR   OMA; QHDFRLP; -.
DR   OrthoDB; 3684148at2759; -.
DR   PhylomeDB; Q5TGZ0; -.
DR   TreeFam; TF300259; -.
DR   PathwayCommons; Q5TGZ0; -.
DR   Reactome; R-HSA-8949613; Cristae formation.
DR   SignaLink; Q5TGZ0; -.
DR   BioGRID-ORCS; 440574; 344 hits in 1084 CRISPR screens.
DR   ChiTaRS; MINOS1; human.
DR   GenomeRNAi; 440574; -.
DR   Pharos; Q5TGZ0; Tbio.
DR   PRO; PR:Q5TGZ0; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q5TGZ0; protein.
DR   Bgee; ENSG00000173436; Expressed in mucosa of transverse colon and 146 other cell types or tissues.
DR   ExpressionAtlas; Q5TGZ0; baseline and differential.
DR   GO; GO:0140275; C:MIB complex; HDA:UniProtKB.
DR   GO; GO:0061617; C:MICOS complex; HDA:UniProtKB.
DR   GO; GO:0044284; C:mitochondrial crista junction; NAS:ComplexPortal.
DR   GO; GO:0005743; C:mitochondrial inner membrane; NAS:ComplexPortal.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0001401; C:SAM complex; HDA:UniProtKB.
DR   GO; GO:0042407; P:cristae formation; IMP:UniProtKB.
DR   GO; GO:0007007; P:inner mitochondrial membrane organization; IC:UniProtKB.
DR   InterPro; IPR007512; Mic10.
DR   PANTHER; PTHR21304:SF14; MICOS COMPLEX SUBUNIT MIC10; 1.
DR   PANTHER; PTHR21304; UNCHARACTERIZED; 1.
DR   Pfam; PF04418; DUF543; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Proteomics identification;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378,
FT                   ECO:0007744|PubMed:25944712"
FT   CHAIN           2..78
FT                   /note="MICOS complex subunit MIC10"
FT                   /id="PRO_0000249459"
FT   TRANSMEM        17..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        37..78
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378,
FT                   ECO:0007744|PubMed:25944712"
FT   VAR_SEQ         22..24
FT                   /note="GTG -> ESW (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_042062"
FT   VAR_SEQ         25..78
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_042063"
SQ   SEQUENCE   78 AA;  8808 MW;  6E4F618F07E969BE CRC64;
     MSESELGRKW DRCLADAVVK IGTGFGLGIV FSLTFFKRRM WPLAFGSGMG LGMAYSNCQH
     DFQAPYLLHG KYVKEQEQ
//