ID Q6INL0_XENLA Unreviewed; 676 AA.
AC Q6INL0;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=LOC443574 protein {ECO:0000313|EMBL:AAH72270.1};
DE Flags: Fragment;
GN Name=LOC443574 {ECO:0000313|EMBL:AAH72270.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH72270.1};
RN [1] {ECO:0000313|EMBL:AAH72270.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart {ECO:0000313|EMBL:AAH72270.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00036383};
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:0000256|ARBA:ARBA00037019};
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:0000256|ARBA:ARBA00036177};
CC -!- SUBUNIT: Homodimer (via N-terminus). {ECO:0000256|ARBA:ARBA00038674}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004448}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000256|ARBA:ARBA00006375}.
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DR EMBL; BC072270; AAH72270.1; -; mRNA.
DR AlphaFoldDB; Q6INL0; -.
DR MaxQB; Q6INL0; -.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0043490; P:malate-aspartate shuttle; IEA:UniProt.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
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:SF7; CALCIUM-BINDING MITOCHONDRIAL CARRIER PROTEIN ARALAR1; 1.
DR PANTHER; PTHR45678; MITOCHONDRIAL 2-OXODICARBOXYLATE CARRIER 1-RELATED; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 2: Evidence at transcript level;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 161..196
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REPEAT 329..419
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 427..511
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 519..607
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAH72270.1"
SQ SEQUENCE 676 AA; 75039 MW; B5A8C1F3CCCFBF5A CRC64;
HHSSLSMAVK FTKRADPFEL KNIFLQYASV EKDGENYMTP SDFVQKYLGL HSDPHSNPMT
VELLGGVADQ TKDGLISFQE FLAFESVLCA PDAMFIVAYQ LFDKSGIAEV TFENVKEIFG
QTMIHHHIPF NWNCEFIRLH FGHNRKKNLS YLEFTEFLQE LQLEHARQAF AQKDKNKTGM
ISALDFSDIM VTIRSHMLTP FVEENLVSAA GGTISHQVSF SYFNAFNSLL NNMELVLKIY
STIAGSRKDL EVTKEEFAHA ANKFGQITPL EIDILFQLSD LFNATGRLML ADIERIAPLE
EGALPYNLAE LQRQQSYSDA GRPIWLQAAE SAYRFTLGSI AGAVGATAVY PIDLVKTRMQ
NQRSSFVGEL MYKNSFDCFK KVLRYEGFFG LYRGLLPQLV GVAPEKAIKL TVNDFVRDKF
TQKDGSIPLF AEIMAGGCAG GSQVIFTNPL EIVKIRLQVA GEITTGPKVR ALTVLRDLGF
FGLYKGAKAC FLRDIPFSGI YFPVYAHCKT MFADEHGHIG ALQLLTAGAV AGVPAASLVT
PADVIKTRLQ VAARAGQTTY TGVIDCFRKI LKEEGAKAFW KGAGARVFRS SPQFGVTLLT
YEMLQQWFYV DFGGIKPAGV EPSPKTRISD LPPANPDHIG GYRLATATFA GIENKFGLYL
PKFRSPEMAA PQPKPV
//
