MIC26_MOUSE
ID MIC26_MOUSE Reviewed; 198 AA.
AC Q9DCZ4; B1ASQ2; B1ASQ3; Q9D186;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=MICOS complex subunit Mic26;
DE AltName: Full=Apolipoprotein O;
DE AltName: Full=MICOS complex subunit Mic23;
DE AltName: Full=Protein FAM121B;
DE Flags: Precursor;
GN Name=Apoo; Synonyms=Fam121b, Mic23, Mic26;
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 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Mammary cancer;
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 [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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24743151; DOI=10.1172/jci74668;
RA Turkieh A., Caubere C., Barutaut M., Desmoulin F., Harmancey R.,
RA Galinier M., Berry M., Dambrin C., Polidori C., Casteilla L., Koukoui F.,
RA Rouet P., Smih F.;
RT "Apolipoprotein O is mitochondrial and promotes lipotoxicity in heart.";
RL J. Clin. Invest. 124:2277-2286(2014).
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 a crucial role
CC in crista junction formation and mitochondrial function (By
CC similarity). Can induce cardiac lipotoxicity by enhancing mitochondrial
CC respiration and fatty acid metabolism in cardiac myoblasts
CC (PubMed:24743151). Promotes cholesterol efflux from macrophage cells.
CC Detected in HDL, LDL and VLDL. Secreted by a microsomal triglyceride
CC transfer protein (MTTP)-dependent mechanism, probably as a VLDL-
CC associated protein that is subsequently transferred to HDL (By
CC similarity). {ECO:0000250|UniProtKB:Q9BUR5,
CC ECO:0000269|PubMed:24743151}.
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. Interacts with MICOS10/MIC10 and
CC APOOL/MIC27. {ECO:0000250|UniProtKB:Q9BUR5}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9BUR5}; Single-pass membrane protein
CC {ECO:0000255}. Mitochondrion {ECO:0000269|PubMed:24743151}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:Q9BUR5}. Golgi apparatus
CC membrane {ECO:0000250|UniProtKB:Q9BUR5}. Note=Exists in three distinct
CC forms: a glycosylated and secreted form, an ER/Golgi-resident form and
CC a non-glycosylated mitochondrial form. {ECO:0000250|UniProtKB:Q9BUR5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9DCZ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DCZ4-2; Sequence=VSP_057812;
CC Name=3;
CC IsoId=Q9DCZ4-3; Sequence=VSP_057813;
CC -!- SIMILARITY: Belongs to the apolipoprotein O/MICOS complex subunit Mic27
CC family. {ECO:0000305}.
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DR EMBL; AK002320; BAB22011.1; -; mRNA.
DR EMBL; AK003831; BAB23025.1; -; mRNA.
DR EMBL; AC154603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL627302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT009733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466637; EDL29756.1; -; Genomic_DNA.
DR EMBL; BC107209; AAI07210.1; -; mRNA.
DR EMBL; BC016557; AAH16557.1; -; mRNA.
DR CCDS; CCDS53136.1; -. [Q9DCZ4-1]
DR CCDS; CCDS57769.1; -. [Q9DCZ4-3]
DR CCDS; CCDS57770.1; -. [Q9DCZ4-2]
DR RefSeq; NP_001186266.1; NM_001199337.1. [Q9DCZ4-3]
DR RefSeq; NP_001186267.1; NM_001199338.1. [Q9DCZ4-2]
DR RefSeq; NP_001186268.1; NM_001199339.1. [Q9DCZ4-2]
DR RefSeq; NP_080949.2; NM_026673.4. [Q9DCZ4-1]
DR AlphaFoldDB; Q9DCZ4; -.
DR BioGRID; 212802; 27.
DR IntAct; Q9DCZ4; 2.
DR MINT; Q9DCZ4; -.
DR STRING; 10090.ENSMUSP00000109531; -.
DR GlyGen; Q9DCZ4; 1 site.
DR iPTMnet; Q9DCZ4; -.
DR PhosphoSitePlus; Q9DCZ4; -.
DR SwissPalm; Q9DCZ4; -.
DR CPTAC; non-CPTAC-3478; -.
DR EPD; Q9DCZ4; -.
DR jPOST; Q9DCZ4; -.
DR MaxQB; Q9DCZ4; -.
DR PaxDb; Q9DCZ4; -.
DR PRIDE; Q9DCZ4; -.
DR ProteomicsDB; 295903; -. [Q9DCZ4-1]
DR ProteomicsDB; 295904; -. [Q9DCZ4-2]
DR ProteomicsDB; 295905; -. [Q9DCZ4-3]
DR Antibodypedia; 564; 181 antibodies from 27 providers.
DR Ensembl; ENSMUST00000113895; ENSMUSP00000109528; ENSMUSG00000079508. [Q9DCZ4-2]
DR Ensembl; ENSMUST00000113896; ENSMUSP00000109529; ENSMUSG00000079508. [Q9DCZ4-2]
DR Ensembl; ENSMUST00000113897; ENSMUSP00000109530; ENSMUSG00000079508. [Q9DCZ4-3]
DR Ensembl; ENSMUST00000113898; ENSMUSP00000109531; ENSMUSG00000079508. [Q9DCZ4-1]
DR GeneID; 68316; -.
DR KEGG; mmu:68316; -.
DR UCSC; uc009ttl.2; mouse. [Q9DCZ4-1]
DR UCSC; uc012hmd.1; mouse.
DR CTD; 79135; -.
DR MGI; MGI:1915566; Apoo.
DR VEuPathDB; HostDB:ENSMUSG00000079508; -.
DR eggNOG; KOG4798; Eukaryota.
DR GeneTree; ENSGT00530000063666; -.
DR InParanoid; Q9DCZ4; -.
DR OMA; YTSWCQD; -.
DR OrthoDB; 1605767at2759; -.
DR PhylomeDB; Q9DCZ4; -.
DR TreeFam; TF315313; -.
DR BioGRID-ORCS; 68316; 1 hit in 69 CRISPR screens.
DR ChiTaRS; Apoo; mouse.
DR PRO; PR:Q9DCZ4; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9DCZ4; protein.
DR Bgee; ENSMUSG00000079508; Expressed in quadriceps femoris and 64 other tissues.
DR Genevisible; Q9DCZ4; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0061617; C:MICOS complex; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0042407; P:cristae formation; ISS:UniProtKB.
DR InterPro; IPR019166; MIC26/MIC27.
DR InterPro; IPR033182; MIC26/MIC27_animal.
DR PANTHER; PTHR14564; PTHR14564; 1.
DR Pfam; PF09769; ApoO; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..198
FT /note="MICOS complex subunit Mic26"
FT /id="PRO_0000254647"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..34
FT /note="Missing (in isoform 2)"
FT /id="VSP_057812"
FT VAR_SEQ 1..3
FT /note="MFK -> MPFWGCGEDEARSGRCR (in isoform 3)"
FT /id="VSP_057813"
SQ SEQUENCE 198 AA; 22604 MW; 6BB8364AF7DC6A3E CRC64;
MFKVIQRSVG PASLSLLTFR VYAAPKKDSP HKSYMKIDEL SLYSVPEGQS KYVEEPRTQL
EENISQLRHH CEPYTSFCQE IYSHTKPKVD HFVQWGVDNY NYLQNAPPGF FPRLGVIGFA
GFVGLLFARG SKIKKLVYPP FFMGLGASVY YPQQAITIAQ ITGEKLYDWG LRGYIVIEDL
WKQNFQKPGN VKNSPGNK
