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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}.
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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
 
 
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