S2546_MOUSE
ID S2546_MOUSE Reviewed; 418 AA.
AC Q9CQS4; Q3TUD3; Q3UGG7; Q8VDX9;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Mitochondrial outer membrane protein SLC25A46 {ECO:0000250|UniProtKB:Q96AG3};
DE AltName: Full=Solute carrier family 25 member 46 {ECO:0000312|MGI:MGI:1914703};
GN Name=Slc25a46 {ECO:0000312|MGI:MGI:1914703};
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].
RC STRAIN=C57BL/6J;
RC TISSUE=Forelimb, Lung, Small intestine, and Xiphoid cartilage;
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 MRNA].
RC STRAIN=Czech II; TISSUE=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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND THR-45, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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).
CC -!- FUNCTION: Transmembrane protein of the mitochondrial outer membrane
CC that controls mitochondrial organization. May regulate the assembly of
CC the MICOS (mitochondrial contact site and cristae organizing system)
CC complex which is essential to the biogenesis and dynamics of
CC mitochondrial cristae, the inwards folds of the inner mitochondrial
CC membrane. Through its interaction with the EMC (endoplasmic reticulum
CC membrane protein complex), could regulate mitochondrial lipid
CC homeostasis and thereby mitochondrial fission.
CC {ECO:0000250|UniProtKB:Q96AG3}.
CC -!- SUBUNIT: Associates with the mitochondrial contact site and cristae
CC organizing system (MICOS) complex. May associate with the endoplasmic
CC reticulum membrane protein complex (EMC).
CC {ECO:0000250|UniProtKB:Q96AG3}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q96AG3}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK004625; BAB23420.1; -; mRNA.
DR EMBL; AK008131; BAB25481.1; -; mRNA.
DR EMBL; AK030346; BAC26914.1; -; mRNA.
DR EMBL; AK031117; BAC27260.1; -; mRNA.
DR EMBL; AK147936; BAE28241.1; -; mRNA.
DR EMBL; AK160834; BAE36038.1; -; mRNA.
DR EMBL; BC020087; AAH20087.1; -; mRNA.
DR CCDS; CCDS29110.1; -.
DR RefSeq; NP_080441.1; NM_026165.3.
DR AlphaFoldDB; Q9CQS4; -.
DR BioGRID; 212197; 2.
DR IntAct; Q9CQS4; 1.
DR MINT; Q9CQS4; -.
DR STRING; 10090.ENSMUSP00000053325; -.
DR iPTMnet; Q9CQS4; -.
DR PhosphoSitePlus; Q9CQS4; -.
DR EPD; Q9CQS4; -.
DR MaxQB; Q9CQS4; -.
DR PaxDb; Q9CQS4; -.
DR PeptideAtlas; Q9CQS4; -.
DR PRIDE; Q9CQS4; -.
DR ProteomicsDB; 260893; -.
DR Antibodypedia; 13498; 120 antibodies from 23 providers.
DR DNASU; 67453; -.
DR Ensembl; ENSMUST00000060396; ENSMUSP00000053325; ENSMUSG00000024259.
DR GeneID; 67453; -.
DR KEGG; mmu:67453; -.
DR UCSC; uc008ehz.1; mouse.
DR CTD; 91137; -.
DR MGI; MGI:1914703; Slc25a46.
DR VEuPathDB; HostDB:ENSMUSG00000024259; -.
DR eggNOG; KOG2954; Eukaryota.
DR GeneTree; ENSGT00390000015874; -.
DR HOGENOM; CLU_047010_0_0_1; -.
DR InParanoid; Q9CQS4; -.
DR OMA; HKWNLKQ; -.
DR OrthoDB; 937901at2759; -.
DR PhylomeDB; Q9CQS4; -.
DR TreeFam; TF313365; -.
DR BioGRID-ORCS; 67453; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Slc25a46; mouse.
DR PRO; PR:Q9CQS4; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9CQS4; protein.
DR Bgee; ENSMUSG00000024259; Expressed in supraoptic nucleus and 264 other tissues.
DR ExpressionAtlas; Q9CQS4; baseline and differential.
DR Genevisible; Q9CQS4; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:MGI.
DR GO; GO:0061564; P:axon development; IBA:GO_Central.
DR GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IMP:MGI.
DR GO; GO:0042407; P:cristae formation; ISO:MGI.
DR GO; GO:0016358; P:dendrite development; IMP:MGI.
DR GO; GO:0031987; P:locomotion involved in locomotory behavior; IMP:MGI.
DR GO; GO:0000266; P:mitochondrial fission; ISS:UniProtKB.
DR GO; GO:0090149; P:mitochondrial membrane fission; IEA:InterPro.
DR GO; GO:0006839; P:mitochondrial transport; IMP:MGI.
DR GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR GO; GO:0022011; P:myelination in peripheral nervous system; IMP:MGI.
DR GO; GO:0021554; P:optic nerve development; IMP:MGI.
DR GO; GO:0048936; P:peripheral nervous system neuron axonogenesis; IMP:MGI.
DR GO; GO:0055091; P:phospholipid homeostasis; ISO:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:0008535; P:respiratory chain complex IV assembly; ISO:MGI.
DR GO; GO:0007416; P:synapse assembly; IMP:MGI.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR InterPro; IPR039158; SLC25A46.
DR PANTHER; PTHR21252; PTHR21252; 1.
DR Pfam; PF00153; Mito_carr; 1.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 2.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..418
FT /note="Mitochondrial outer membrane protein SLC25A46"
FT /id="PRO_0000291829"
FT TRANSMEM 103..123
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 96..187
FT /note="Solcar 1"
FT REPEAT 311..413
FT /note="Solcar 2"
FT REGION 46..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5EB62"
FT MOD_RES 45
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 48
FT /note="D -> G (in Ref. 1; BAE28241)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="E -> G (in Ref. 1; BAE36038)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="G -> S (in Ref. 2; AAH20087)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 46224 MW; 621A9892D62C6CD9 CRC64;
MHPRRPEGFD GLGYRGGVRD DPAFGGPFHA RSFGSGTELG HWVTTPPDIP GSRNLHWGEK
SPSYGVPSAP PTLEGSAEEP FPGGGEGPRP GPSSEQLNRF AGFGIGLASL FTENVLAHPC
IVLRRQCQVN YHARHYHLTP FSIINIMYSF NKTQGPRALW KGMGSTFIVQ GVTLGAEGII
SEFTPLPREV SHKLNPKQIG EHLLLKCLTY MVAMPFYSAS LIETVQSEII RDNTGILECV
KEGIGRVIGL GVPHSKRLLP LFSLIFPTVL HGVLHYIISS IIQKIVLLIL KRKTYNSHLA
ESTSPMQNML DAYFPELIAN FAASLCSDVI LYPLETVLHR LHIQGTRTII DNTDLGYEVL
PINTQYEGMR DCINTIKQEE GVFGFYKGFG AVIIQYTLHA TILQITKMIY STLLQNSI