S2513_RAT
ID S2513_RAT Reviewed; 676 AA.
AC F1LZW6;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 4.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Electrogenic aspartate/glutamate antiporter SLC25A13, mitochondrial {ECO:0000305|PubMed:4436323, ECO:0000305|PubMed:486467};
DE AltName: Full=Solute carrier family 25 member 13 {ECO:0000312|RGD:1565889};
GN Name=Slc25a13 {ECO:0000312|RGD:1565889};
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 FUNCTION, TRANSPORTER ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=4436323; DOI=10.1016/s0021-9258(19)81269-3;
RA LaNoue K.F., Tischler M.E.;
RT "Electrogenic characteristics of the mitochondrial glutamate-aspartate
RT antiporter.";
RL J. Biol. Chem. 249:7522-7528(1974).
RN [3]
RP FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=486467; DOI=10.1016/0005-2736(79)90407-3;
RA Palmieri F., Stipani I., Iacobazzi V.;
RT "The transport of L-cysteinesulfinate in rat liver mitochondria.";
RL Biochim. Biophys. Acta 555:531-546(1979).
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
CC (PubMed:4436323). 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 (PubMed:486467). {ECO:0000269|PubMed:4436323,
CC ECO:0000269|PubMed:486467}.
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:0000269|PubMed:4436323};
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:0000269|PubMed:486467};
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:0000269|PubMed:486467};
CC -!- ACTIVITY REGULATION: L-aspartate and 3-sulfino-L-alanine uptake are
CC both inhibited by glisoxepide. {ECO:0000269|PubMed:486467}.
CC -!- SUBUNIT: Homodimer (via N-terminus). {ECO:0000250|UniProtKB:Q9UJS0}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:4436323, ECO:0000305|PubMed:486467}; Multi-pass
CC membrane protein {ECO:0000255}.
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; AABR07059674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07059675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07072979; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; F1LZW6; -.
DR STRING; 10116.ENSRNOP00000013816; -.
DR jPOST; F1LZW6; -.
DR PaxDb; F1LZW6; -.
DR PRIDE; F1LZW6; -.
DR Ensembl; ENSRNOT00000013817.8; ENSRNOP00000013816.7; ENSRNOG00000009957.8.
DR RGD; 1565889; Slc25a13.
DR VEuPathDB; HostDB:ENSRNOG00000009957; -.
DR eggNOG; KOG0751; Eukaryota.
DR GeneTree; ENSGT00940000159344; -.
DR HOGENOM; CLU_014931_0_0_1; -.
DR InParanoid; F1LZW6; -.
DR OMA; KRLYANL; -.
DR TreeFam; TF313209; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000009957; Expressed in liver and 18 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0000514; F:3-sulfino-L-alanine: proton, glutamate antiporter activity; ISS:UniProtKB.
DR GO; GO:0000515; F:aspartate:glutamate, proton antiporter activity; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0015183; F:L-aspartate transmembrane transporter activity; ISO:RGD.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; ISO:RGD.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015810; P:aspartate transmembrane transport; ISO:RGD.
DR GO; GO:0006754; P:ATP biosynthetic process; ISO:RGD.
DR GO; GO:0045333; P:cellular respiration; ISO:RGD.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; ISO:RGD.
DR GO; GO:0043490; P:malate-aspartate shuttle; ISO:RGD.
DR GO; GO:0051592; P:response to calcium ion; ISO:RGD.
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; 2.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF103506; SSF103506; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50920; SOLCAR; 2.
PE 3: Inferred from homology;
KW Acetylation; Calcium; Membrane; Metal-binding; Methylation; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome; Repeat;
KW 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 /evidence="ECO:0000250|UniProtKB:Q9UJS0"
FT /id="PRO_0000455804"
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 125..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..312
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 354
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXX4"
FT MOD_RES 373
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXX4"
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:0000250|UniProtKB:Q9QXX4"
FT MOD_RES 485
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9QXX4"
FT MOD_RES 581
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXX4"
FT MOD_RES 663
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXX4"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJS0"
SQ SEQUENCE 676 AA; 74399 MW; EBFA45BE11C526C9 CRC64;
MAAAKVALTK RADPAELKAI FLKYASIEKN GEFFMSPHDF VTRYLNIFGE SQPNPKTVEL
LSGVVDQTKD GLISFQEFVA FESVLCAPDA LFMVAFQLFD KAGKGEVTFE DVRQVFGQTT
IHQHIPFNWD SEFVQLHFGK ERKRHLTYAE FTQFLLEIQL EHAKQAFVQR DNAKTGKVTA
IDFRDIMVTI RPHVLTPFVE ECLVAAAGGT RSHQVSFSYF NGFNSLLNNM ELIRKIYSTL
AGSRKDVEVT 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 SGVTDCFRKI LREEGPKALW KGAGARVFRS SPQFGVTLLT
YELLQRWFYV DFGGVKPVGS ELVPKSRITL PAPNPDHVGG YKLAVATFAG IENKFGLYLP
LFKPSASTSK VTAVGS
