S2513_MACFA
ID S2513_MACFA Reviewed; 674 AA.
AC Q8HXW2;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Electrogenic aspartate/glutamate antiporter SLC25A13, mitochondrial {ECO:0000250|UniProtKB:Q9UJS0};
DE AltName: Full=Solute carrier family 25 member 13 {ECO:0000250|UniProtKB:Q9UJS0};
GN Name=SLC25A13 {ECO:0000250|UniProtKB:Q9UJS0}; ORFNames=QflA-10133;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Frontal cortex;
RA Kusuda J., Osada N., Hida M., Sugano S., Hashimoto K.;
RT "Isolation and characterization of cDNA for macaque neurological disease
RT genes.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
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; AB083329; BAC20608.1; -; mRNA.
DR RefSeq; NP_001270156.1; NM_001283227.1.
DR AlphaFoldDB; Q8HXW2; -.
DR SMR; Q8HXW2; -.
DR STRING; 9541.XP_005550214.1; -.
DR GeneID; 102115095; -.
DR CTD; 10165; -.
DR eggNOG; KOG0751; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0015810; P:aspartate transmembrane transport; ISS:UniProtKB.
DR GO; GO:0006754; P:ATP biosynthetic process; ISS:UniProtKB.
DR GO; GO:0045333; P:cellular respiration; ISS:UniProtKB.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; ISS:UniProtKB.
DR GO; GO:0043490; P:malate-aspartate shuttle; ISS:UniProtKB.
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; 2.
DR PROSITE; PS50920; SOLCAR; 3.
PE 2: Evidence at transcript level;
KW Acetylation; Calcium; Membrane; Metal-binding; Methylation; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UJS0"
FT CHAIN 2..674
FT /note="Electrogenic aspartate/glutamate antiporter
FT SLC25A13, mitochondrial"
FT /id="PRO_0000090601"
FT TOPO_DOM 2..331
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 332..349
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TOPO_DOM 350..392
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 393..412
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TOPO_DOM 413..435
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 436..449
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TOPO_DOM 450..484
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 485..504
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TOPO_DOM 505..523
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 524..541
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TOPO_DOM 542..580
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 581..599
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TOPO_DOM 600..674
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 326..418
FT /note="Solcar 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 426..510
FT /note="Solcar 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 518..605
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 321..611
FT /note="Carrier domain"
FT /evidence="ECO:0000250|UniProtKB:Q9UJS0"
FT REGION 612..674
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 353
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXX4"
FT MOD_RES 372
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXX4"
FT MOD_RES 453
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJS0"
FT MOD_RES 484
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9QXX4"
FT MOD_RES 484
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9QXX4"
FT MOD_RES 580
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXX4"
FT MOD_RES 661
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXX4"
SQ SEQUENCE 674 AA; 74003 MW; CD01541BE5AB0EFC CRC64;
MAAAKVALTK RADPAELRTI FLKYASIEKN GEFFTSPNDF VTRYLNIFGE SQPNPKTVEL
LSGVADQTKD GLISFQEFVA FESVLCAPDA LFMVAFQLFD KAGKGEVTFE DVKQVFGQTT
IHQHIPFNWD SEFVQLHFGK ERKRHLTYAE FTQFLLEIQL EHAKQAFVQR DNASTGRVTA
IDFRDIMVTI RPHVLTPFVE ECLVAAAGGT TSHQVSFSYF NGFNSLLNNM ELTRKIYSTL
AGNRKDVEVT KEEFVLAAQK FGQVTPMEVD ILFRLADLYE PRGRMTLADI ERIAPLEEGT
LPFNLAEAQR QKASGDSARP VLLQVAESAY RFGLGSVAGA VGATAVYPID LVKTRMQNQR
STGSFVGELM YKNSFDCFKK VLRYEGFFGL YRGLLPQLLG VAPEKAIKLT VNDFVRDKFM
HKDGSVPLAA EILAGGCAGG SQVIFTNPLE IVKIRLQVAG EITTGPRVSA LSVVRDLGFF
GIYKGAKACF LRDIPFSAIY FPCYAHARAS FANEDGQVSP GSLLLAGAIA GMPAASLVTP
ADVIKTRLQV AARAGQTTYS GVIDCFKKIL REEGPKALWK GAARVFRSSP QFGVTLLTYE
LLQRWFYIDF GGVKPMGSEP VPKSRINLPA PNPDHVGGYK LAVATFAGIE NKFGLYLPLF
KPSVPTSEAI GGGP
