ID H2VC65_TAKRU Unreviewed; 478 AA.
AC H2VC65;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Solute carrier family 25 member 24 {ECO:0000313|Ensembl:ENSTRUP00000046808.3};
GN Name=slc25a24 {ECO:0000313|Ensembl:ENSTRUP00000046808.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000046808.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000046808.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000046808.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-AMP(in) + ADP(out) + H(+)(out) = 3'-AMP(out) + ADP(in) +
CC H(+)(in); Xref=Rhea:RHEA:73679, ChEBI:CHEBI:15378, ChEBI:CHEBI:60880,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-AMP(out) + phosphate(in) = 3'-AMP(in) + phosphate(out);
CC Xref=Rhea:RHEA:73691, ChEBI:CHEBI:43474, ChEBI:CHEBI:60880;
CC Evidence={ECO:0000256|ARBA:ARBA00036289};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP(out) + ATP(in) + H(+)(out) + Mg(2+)(in) = ADP(in) +
CC ATP(out) + H(+)(in) + Mg(2+)(out); Xref=Rhea:RHEA:73659,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18420, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036612};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP(out) + H(+)(out) + phosphate(in) = ADP(in) + H(+)(in) +
CC phosphate(out); Xref=Rhea:RHEA:65844, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00036415};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP(out) + dADP(in) = ADP(in) + dADP(out);
CC Xref=Rhea:RHEA:72855, ChEBI:CHEBI:57667, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00036435};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP(out) + dAMP(in) + H(+)(out) = ADP(in) + dAMP(out) +
CC H(+)(in); Xref=Rhea:RHEA:73675, ChEBI:CHEBI:15378, ChEBI:CHEBI:58245,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036316};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP(out) + diphosphate(in) = ADP(in) + diphosphate(out);
CC Xref=Rhea:RHEA:73671, ChEBI:CHEBI:33019, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00036630};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP(out) + phosphate(in) = AMP(in) + phosphate(out);
CC Xref=Rhea:RHEA:70259, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000256|ARBA:ARBA00036908};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP(out) + 2 H(+)(out) + phosphate(in) = ATP(in) + 2 H(+)(in)
CC + phosphate(out); Xref=Rhea:RHEA:72035, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474;
CC Evidence={ECO:0000256|ARBA:ARBA00036970};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP(out) + Mg(2+)(out) + phosphate(in) = ATP(in) + Mg(2+)(in)
CC + phosphate(out); Xref=Rhea:RHEA:65840, ChEBI:CHEBI:18420,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474;
CC Evidence={ECO:0000256|ARBA:ARBA00034993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dADP(out) + H(+)(out) + phosphate(in) = dADP(in) + H(+)(in) +
CC phosphate(out); Xref=Rhea:RHEA:73695, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57667;
CC Evidence={ECO:0000256|ARBA:ARBA00036766};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dAMP(out) + phosphate(in) = dAMP(in) + phosphate(out);
CC Xref=Rhea:RHEA:73687, ChEBI:CHEBI:43474, ChEBI:CHEBI:58245;
CC Evidence={ECO:0000256|ARBA:ARBA00036282};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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, ECO:0000256|RuleBase:RU000488}.
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DR AlphaFoldDB; H2VC65; -.
DR STRING; 31033.ENSTRUP00000046808; -.
DR Ensembl; ENSTRUT00000046966.3; ENSTRUP00000046808.3; ENSTRUG00000018295.3.
DR GeneTree; ENSGT00940000164927; -.
DR HOGENOM; CLU_015166_2_0_1; -.
DR OMA; SGQWWKQ; -.
DR Proteomes; UP000005226; Chromosome 20.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
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; IPR002167; GDC-like.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR PANTHER; PTHR24089:SF262; CALCIUM-BINDING MITOCHONDRIAL CARRIER PROTEIN SCAMC-1; 1.
DR PANTHER; PTHR24089; SOLUTE CARRIER FAMILY 25; 1.
DR Pfam; PF13499; EF-hand_7; 2.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00928; GRAVESDC.
DR PRINTS; PR00926; MITOCARRIER.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS50920; SOLCAR; 3.
PE 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000488}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..478
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025439503"
FT DOMAIN 21..56
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 88..123
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 124..159
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REPEAT 194..280
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 288..373
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 385..473
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 478 AA; 53183 MW; F47A1291A4B79ACC CRC64;
VFLWFKSLLF FPHCRCAASQ DGPKTYEELF AKLDANKDGK VDVSELRAGL AAMGIKSGKG
AAQKIISSGD KDEDEGLDFS EFSKYLKEHE KKLKLTFKSL DKNNDGRIDH TEIKQSLADL
GLDISKEEAE KILQSIDVDG TMTVDWNEWR EHFLFNPATN LQEIIRYWKH STVLDIGESL
AIPDEFTEEE KTSGLWWKQL SAGAMAGAVS RTGTAPLDRM KVFMQVHATK SNKISLSGGF
KQMLKEGGVT SLWRGNGINV LKIAPETAIK FMAYEQYKKL LSSEPGKVRT HERFMAGSLA
GATAQTAIYP MEVLKTRLTL RKTGQYSGMF DCAKKILKNE GVKAFYKGYI PNILGIIPYA
GIDLAIYESL KNLWLSKYAK DTANPGILVL LGCGTISSSC GQVASYPLAL IRTRMQAQAS
IEGSKQMSMS QIAKKILEKE GFFGLYRGIL PNFMKVIPAV SISYVVYENM RYSLGIQK
//
