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Database: UniProt
Entry: M3VW64_FELCA
LinkDB: M3VW64_FELCA
Original site: M3VW64_FELCA 
ID   M3VW64_FELCA            Unreviewed;       477 AA.
AC   M3VW64;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   24-JAN-2024, entry version 71.
DE   SubName: Full=Solute carrier family 25 member 24 {ECO:0000313|Ensembl:ENSFCAP00000001107.4};
GN   Name=SLC25A24 {ECO:0000313|Ensembl:ENSFCAP00000001107.4,
GN   ECO:0000313|VGNC:VGNC:65265};
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000001107.4, ECO:0000313|Proteomes:UP000011712};
RN   [1] {ECO:0000313|Ensembl:ENSFCAP00000001107.4, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001107.4,
RC   ECO:0000313|Proteomes:UP000011712};
RX   PubMed=17975172; DOI=10.1101/gr.6380007;
RA   Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA   Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA   Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA   Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA   Tesler G., O'Brien S.J.;
RT   "Initial sequence and comparative analysis of the cat genome.";
RL   Genome Res. 17:1675-1689(2007).
RN   [2] {ECO:0000313|Ensembl:ENSFCAP00000001107.4, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001107.4,
RC   ECO:0000313|Proteomes:UP000011712};
RA   Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT   "Sequence assembly of the Felis catus genome version 6.2.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSFCAP00000001107.4}
RP   IDENTIFICATION.
RC   STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001107.4};
RG   Ensembl;
RL   Submitted (SEP-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   EMBL; AANG04003279; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003990438.1; XM_003990389.4.
DR   AlphaFoldDB; M3VW64; -.
DR   STRING; 9685.ENSFCAP00000001107; -.
DR   PaxDb; 9685-ENSFCAP00000001107; -.
DR   Ensembl; ENSFCAT00000001193.6; ENSFCAP00000001107.4; ENSFCAG00000001193.6.
DR   GeneID; 101095354; -.
DR   KEGG; fca:101095354; -.
DR   CTD; 29957; -.
DR   VGNC; VGNC:65265; SLC25A24.
DR   eggNOG; KOG0036; Eukaryota.
DR   GeneTree; ENSGT00940000158786; -.
DR   HOGENOM; CLU_015166_2_0_1; -.
DR   InParanoid; M3VW64; -.
DR   OMA; GTFAHPY; -.
DR   OrthoDB; 1330359at2759; -.
DR   Proteomes; UP000011712; Chromosome C1.
DR   Bgee; ENSFCAG00000001193; Expressed in embryonic head and 10 other cell types or tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0140988; F:ADP:inorganic phosphate antiporter activity; IEA:Ensembl.
DR   GO; GO:0005347; F:ATP transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0140987; F:ATP:inorganic phosphate antiporter activity; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR   GO; GO:0015866; P:ADP transport; IBA:GO_Central.
DR   GO; GO:0015867; P:ATP transport; IBA:GO_Central.
DR   GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
DR   GO; GO:1990544; P:mitochondrial ATP transmembrane transport; IEA:Ensembl.
DR   GO; GO:0006839; P:mitochondrial transport; IEA:Ensembl.
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:UP000011712};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU00282};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000488}.
FT   DOMAIN          19..54
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          86..121
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          122..157
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REPEAT          192..278
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          286..371
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          383..471
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ   SEQUENCE   477 AA;  53182 MW;  112817B85DD5894A CRC64;
     MLRWLRGFVL PAAACQDAAP PTRFETLFQK LDRNGDGVVD IGELQEGLKG LGVALGQDGE
     EKILTTGDIN KDGKLDFEEF MQYLKDHEKK MKLAFKSLDK NNDGVIEASE IVQSLQTLGL
     TISEQQAELI LQSIDTDGTM TIDWNEWRDY FLFNPVTDIE EIIRFWKHST GIDIGDSLTI
     PDEFTEEEKK SGQWWRQLLA GGIAGAVSRT STAPLDRLKV MMQVHGSKSG KMNIYDGFRQ
     MVKEGGIRSL WRGNGTNVLK IAPETAVKFW SYEQYKKLLT VEGQKIGIFD RFISGSLAGA
     TAQTIIYPME VIKTRLAVGK TGQYYGIFDC AKKILKHEGV GAFYKGYIPN LLGIVPYAGI
     DLAVYELLKS YWLDNYAKDS VNPGVIVLLG CGIVSSTCGQ LASYPLALVK TRMQAQAMLE
     GTKQMNMVGL FRRIISKEGI PGLYRGITPN FMKVLPAVGI SYVVYENMKQ TLRVTQK
//
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