S2546_RAT
ID S2546_RAT Reviewed; 418 AA.
AC Q5EB62;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Mitochondrial outer membrane protein SLC25A46 {ECO:0000250|UniProtKB:Q96AG3};
DE AltName: Full=Solute carrier family 25 member 46 {ECO:0000312|RGD:1305072};
GN Name=Slc25a46 {ECO:0000312|RGD:1305072};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 165-418.
RC TISSUE=Liver;
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 TISSUE SPECIFICITY.
RX PubMed=16949250; DOI=10.1016/j.ygeno.2006.06.016;
RA Haitina T., Lindblom J., Renstroem T., Fredriksson R.;
RT "Fourteen novel human members of mitochondrial solute carrier family 25
RT (SLC25) widely expressed in the central nervous system.";
RL Genomics 88:779-790(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-35 AND THR-45, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in hindbrain,
CC spinal cord and brain coronal sections containing corpus callosum,
CC fornix, optic chiasm, thalamus, hypothalamus, midbrain, pons and
CC cerebellum. {ECO:0000269|PubMed:16949250}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AABR03109497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC090000; AAH90000.1; -; mRNA.
DR RefSeq; NP_001093985.1; NM_001100515.1.
DR AlphaFoldDB; Q5EB62; -.
DR STRING; 10116.ENSRNOP00000023032; -.
DR iPTMnet; Q5EB62; -.
DR PhosphoSitePlus; Q5EB62; -.
DR jPOST; Q5EB62; -.
DR PaxDb; Q5EB62; -.
DR PRIDE; Q5EB62; -.
DR Ensembl; ENSRNOT00000023032; ENSRNOP00000023032; ENSRNOG00000017091.
DR GeneID; 291709; -.
DR KEGG; rno:291709; -.
DR UCSC; RGD:1305072; rat.
DR CTD; 91137; -.
DR RGD; 1305072; Slc25a46.
DR eggNOG; KOG2954; Eukaryota.
DR GeneTree; ENSGT00390000015874; -.
DR HOGENOM; CLU_047010_0_0_1; -.
DR InParanoid; Q5EB62; -.
DR OMA; HKWNLKQ; -.
DR OrthoDB; 937901at2759; -.
DR PhylomeDB; Q5EB62; -.
DR TreeFam; TF313365; -.
DR PRO; PR:Q5EB62; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000017091; Expressed in quadriceps femoris and 19 other tissues.
DR ExpressionAtlas; Q5EB62; baseline and differential.
DR Genevisible; Q5EB62; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0000422; P:autophagy of mitochondrion; ISO:RGD.
DR GO; GO:0061564; P:axon development; IBA:GO_Central.
DR GO; GO:0021702; P:cerebellar Purkinje cell differentiation; ISO:RGD.
DR GO; GO:0042407; P:cristae formation; ISO:RGD.
DR GO; GO:0016358; P:dendrite development; ISO:RGD.
DR GO; GO:0031987; P:locomotion involved in locomotory behavior; ISO:RGD.
DR GO; GO:0000266; P:mitochondrial fission; ISS:UniProtKB.
DR GO; GO:0090149; P:mitochondrial membrane fission; ISO:RGD.
DR GO; GO:0006839; P:mitochondrial transport; ISO:RGD.
DR GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR GO; GO:0022011; P:myelination in peripheral nervous system; ISO:RGD.
DR GO; GO:0021554; P:optic nerve development; ISO:RGD.
DR GO; GO:0048936; P:peripheral nervous system neuron axonogenesis; ISO:RGD.
DR GO; GO:0055091; P:phospholipid homeostasis; ISO:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:RGD.
DR GO; GO:0008535; P:respiratory chain complex IV assembly; ISO:RGD.
DR GO; GO:0007416; P:synapse assembly; ISO:RGD.
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_0000291830"
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..416
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:22673903"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 45
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 418 AA; 46210 MW; DF0920EFF44F4B80 CRC64;
MHPRRPEGFD GLGYRGGVRD DPAFGGPFHA RSFGSGTELG HWVTTPPDIP GSRNLHWGEK
SPSYGVPSAP PTLEGPAEEP FPGGGDGPRP GRSSEQLNRF AGFGIGLASL FTENVLAHPC
IVLRRQCQVN YHARHYHLTP FSVINIMYSF NKTQGPRALW KGMGSTFIVQ GVTLGAEGII
SEFTPLPREV SQKWNPKQIG EHLLLKCLTY MVAMPFYSAS LIETVQSEII RDNTGILECV
KEGIGRVIGL GVPHSKRLLP LFSLIFPTVL HGVLHYIISS IIQKIVLLIL KRKTCSSHLA
ESTSPMQNML DAYFPELIAN FAASLCSDVI LYPLETVLHR LHIQGTRTII DNTDLGYEVL
PINTQYEGMR DCVNTIKQEE GVFGFYKGFG AVIIQYTLHA TILQITKIIY STLLQNSI
