S2513_MOUSE
ID S2513_MOUSE Reviewed; 676 AA.
AC Q9QXX4; Q9CZF6; Q9DCF5;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Electrogenic aspartate/glutamate antiporter SLC25A13, mitochondrial {ECO:0000250|UniProtKB:Q9UJS0};
DE AltName: Full=Citrin {ECO:0000303|PubMed:10610724};
DE AltName: Full=Solute carrier family 25 member 13 {ECO:0000312|MGI:MGI:1354721};
GN Name=Slc25a13 {ECO:0000312|MGI:MGI:1354721};
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 [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10610724; DOI=10.1006/geno.1999.6006;
RA Sinasac D.S., Crackower M.A., Lee J.R., Kobayashi K., Saheki T.,
RA Scherer S.W., Tsui L.-C.;
RT "Genomic structure of the adult-onset type II citrullinemia gene, SLC25A13,
RT and cloning and expression of its mouse homologue.";
RL Genomics 62:289-292(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and 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 [3]
RP PROTEIN SEQUENCE OF 175-184; 385-406; 410-417 AND 457-468, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Pancreas, 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 [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-485 AND LYS-581, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-18; LYS-354; LYS-373; LYS-485 AND
RP LYS-663, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Mitochondrial electrogenic aspartate/glutamate antiporter
CC that favors efflux of aspartate and entry of glutamate and proton
CC within the mitochondria as part of the malate-aspartate shuttle (By
CC similarity). Also mediates the uptake of L-cysteinesulfinate by
CC mitochondria in exchange of L-glutamate and proton. Can also exchange
CC L-cysteinesulfinate with aspartate in their anionic form without any
CC proton translocation (By similarity). {ECO:0000250|UniProtKB:F1LZW6,
CC ECO:0000250|UniProtKB:Q9UJS0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + L-aspartate(in) + L-glutamate(out) = H(+)(in) + L-
CC aspartate(out) + L-glutamate(in); Xref=Rhea:RHEA:70783,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991;
CC Evidence={ECO:0000250|UniProtKB:Q9UJS0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-sulfino-L-alanine(out) + H(+)(in) + L-glutamate(in) = 3-
CC sulfino-L-alanine(in) + H(+)(out) + L-glutamate(out);
CC Xref=Rhea:RHEA:70967, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:61085; Evidence={ECO:0000250|UniProtKB:Q9UJS0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-sulfino-L-alanine(out) + L-aspartate(in) = 3-sulfino-L-
CC alanine(in) + L-aspartate(out); Xref=Rhea:RHEA:70975,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:61085;
CC Evidence={ECO:0000250|UniProtKB:F1LZW6};
CC -!- SUBUNIT: Homodimer (via N-terminus). {ECO:0000250|UniProtKB:Q9UJS0}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9UJS0}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9UJS0}.
CC -!- TISSUE SPECIFICITY: At 10.5 dpc, expressed in branchial arches, a well
CC as in the limb and tail buds. At 13.5 dpc expression is predominant in
CC epithelial structures and the forebrain, kidney and liver. Expression
CC in liver is maintained into adulthood. {ECO:0000269|PubMed:10610724}.
CC -!- DOMAIN: The EF-hand 2 domain within the regulatory N-terminal domain
CC binds one calcium in the mitochondrial intermembrane space. Calcium
CC triggers the binding of the regulatory N-terminal domain to the C-
CC terminal domain, opening a vestibule which allows the substrates to be
CC translocated through the carrier domain (By similarity). In the absence
CC of calcium, the linker loop domain may close the vestibule and prevent
CC substrates from entering the carrier domain (By similarity).
CC {ECO:0000250|UniProtKB:O75746, ECO:0000250|UniProtKB:Q9UJS0}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AF164632; AAF21426.1; -; mRNA.
DR EMBL; AK002829; BAB22390.1; -; mRNA.
DR EMBL; AK012670; BAB28397.1; -; mRNA.
DR CCDS; CCDS39421.1; -.
DR RefSeq; NP_001171043.1; NM_001177572.1.
DR RefSeq; NP_056644.1; NM_015829.3.
DR AlphaFoldDB; Q9QXX4; -.
DR SMR; Q9QXX4; -.
DR BioGRID; 206130; 11.
DR IntAct; Q9QXX4; 8.
DR MINT; Q9QXX4; -.
DR STRING; 10090.ENSMUSP00000015256; -.
DR iPTMnet; Q9QXX4; -.
DR PhosphoSitePlus; Q9QXX4; -.
DR SwissPalm; Q9QXX4; -.
DR EPD; Q9QXX4; -.
DR jPOST; Q9QXX4; -.
DR MaxQB; Q9QXX4; -.
DR PaxDb; Q9QXX4; -.
DR PRIDE; Q9QXX4; -.
DR ProteomicsDB; 283533; -.
DR Antibodypedia; 15932; 224 antibodies from 30 providers.
DR DNASU; 50799; -.
DR Ensembl; ENSMUST00000015256; ENSMUSP00000015256; ENSMUSG00000015112.
DR Ensembl; ENSMUST00000188414; ENSMUSP00000139571; ENSMUSG00000015112.
DR GeneID; 50799; -.
DR KEGG; mmu:50799; -.
DR UCSC; uc009awp.2; mouse.
DR CTD; 10165; -.
DR MGI; MGI:1354721; Slc25a13.
DR VEuPathDB; HostDB:ENSMUSG00000015112; -.
DR eggNOG; KOG0751; Eukaryota.
DR GeneTree; ENSGT00940000159344; -.
DR HOGENOM; CLU_014931_3_0_1; -.
DR InParanoid; Q9QXX4; -.
DR OMA; KRLYANL; -.
DR OrthoDB; 1007928at2759; -.
DR PhylomeDB; Q9QXX4; -.
DR TreeFam; TF313209; -.
DR Reactome; R-MMU-70263; Gluconeogenesis.
DR Reactome; R-MMU-8963693; Aspartate and asparagine metabolism.
DR BioGRID-ORCS; 50799; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Slc25a13; mouse.
DR PRO; PR:Q9QXX4; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9QXX4; protein.
DR Bgee; ENSMUSG00000015112; Expressed in interventricular septum and 197 other tissues.
DR Genevisible; Q9QXX4; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0000514; F:3-sulfino-L-alanine: proton, glutamate antiporter activity; ISS:UniProtKB.
DR GO; GO:0015297; F:antiporter activity; ISO:MGI.
DR GO; GO:0000515; F:aspartate:glutamate, proton antiporter activity; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0015183; F:L-aspartate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IMP:MGI.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015810; P:aspartate transmembrane transport; IMP:MGI.
DR GO; GO:0006754; P:ATP biosynthetic process; ISO:MGI.
DR GO; GO:0045333; P:cellular respiration; ISO:MGI.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; ISS:UniProtKB.
DR GO; GO:0043490; P:malate-aspartate shuttle; IMP:MGI.
DR GO; GO:0051592; P:response to calcium ion; ISS:UniProtKB.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR029658; Aralar2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR PANTHER; PTHR45678:SF12; PTHR45678:SF12; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF103506; SSF103506; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Acetylation; Calcium; Direct protein sequencing; Membrane; Metal-binding;
KW Methylation; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UJS0"
FT CHAIN 2..676
FT /note="Electrogenic aspartate/glutamate antiporter
FT SLC25A13, mitochondrial"
FT /id="PRO_0000090602"
FT TOPO_DOM 2..332
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 333..350
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TOPO_DOM 351..393
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 394..413
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TOPO_DOM 414..436
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 437..450
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TOPO_DOM 451..485
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 486..505
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TOPO_DOM 506..524
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 525..542
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TOPO_DOM 543..581
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 582..601
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TOPO_DOM 602..676
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT DOMAIN 51..86
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 87..122
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 123..157
FT /note="EF-hand 3"
FT /evidence="ECO:0000305"
FT DOMAIN 158..193
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 327..419
FT /note="Solcar 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 427..511
FT /note="Solcar 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 519..607
FT /note="Solcar 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REGION 2..295
FT /note="Regulatory N-terminal domain"
FT /evidence="ECO:0000250|UniProtKB:Q9UJS0"
FT REGION 296..311
FT /note="Linker loop domain"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT REGION 322..613
FT /note="Carrier domain"
FT /evidence="ECO:0000250|UniProtKB:Q9UJS0"
FT REGION 614..676
FT /note="C-terminal domain"
FT /evidence="ECO:0000250|UniProtKB:Q9UJS0"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9UJS0"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9UJS0"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9UJS0"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9UJS0"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9UJS0"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJS0"
FT MOD_RES 18
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 354
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 373
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 454
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJS0"
FT MOD_RES 485
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 485
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 581
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 663
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJS0"
FT CONFLICT 312
FT /note="Missing (in Ref. 2; BAB28397)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="S -> F (in Ref. 2; BAB22390)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 676 AA; 74467 MW; 5E3952F08E5E58C5 CRC64;
MAAAKVALTK RADPAELKAI FLKYASIEKN GEFFMSPHDF VTRYLNIFGE SQPNPKTVEL
LSGVVDQTKD GLISFQEFVA FESVLCAPDA LFMVAFQLFD KAGKGEVTFE DVKQIFGQTT
IHQHIPFNWD SEFVQLHFGK ERKRHLTYAE FTQFLLEIQL EHAKQAFVQR DNAKTGKVSA
IDFRDIMVTI RPHVLTPFVE ECLVAAAGGT RSHQVSFSYF NGFNSLLNNM ELIRKIYSTL
AGNRKDVEVT KEEFALAAQK FGQVTPMEVD ILFQLADLYE PRGRMTLADI ERIAPLEEGM
LPFNLAEAQR QQKASGDAAR PFLLQLAESA YRFGLGSIAG AVGATAVYPI DLVKTRMQNQ
RSTGSFVGEL MYKNSFDCFK KVLRYEGFFG LYRGLLPQLL GVAPEKAIKL TVNDFVRDKF
MHKDGSVPLL AEIFAGGCAG GSQVIFTNPL EIVKIRLQVA GEITTGPRVS ALSVVRDLGF
FGIYKGAKAC FLRDIPFSAI YFPCYAHVKA SFANEDGQVS PGSLLLAGAI AGMPAASLVT
PADVIKTRLQ VAARAGQTTY NGVTDCFRKI LREEGPKALW KGVAARVFRS SPQFGVTLLT
YELLQRWFYV DFGGVKPVGS EPVPKSRITL PAPNPDHVGG YKLAVATFAG IENKFGLYLP
LFKPSASTSK VTAGDS
