ID A0A091D9K1_FUKDA Unreviewed; 491 AA.
AC A0A091D9K1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Calcium-binding mitochondrial carrier protein SCaMC-3 {ECO:0000313|EMBL:KFO28794.1};
GN ORFNames=H920_09736 {ECO:0000313|EMBL:KFO28794.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO28794.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO28794.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO28794.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; KN122676; KFO28794.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091D9K1; -.
DR STRING; 885580.ENSFDAP00000008678; -.
DR eggNOG; KOG0036; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00051; EFh; 1.
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; PTHR24089:SF196; CALCIUM-BINDING MITOCHONDRIAL CARRIER PROTEIN SCAMC-3; 1.
DR PANTHER; PTHR24089; SOLUTE CARRIER FAMILY 25; 1.
DR Pfam; PF13405; EF-hand_6; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF00153; Mito_carr; 3.
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 Antiport {ECO:0000256|ARBA:ARBA00022449};
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:UP000028990};
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 31..66
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 100..135
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 136..171
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REPEAT 206..292
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 300..385
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 397..485
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REGION 62..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 491 AA; 55515 MW; 9CFF34B4E0E122C0 CRC64;
METCPCGCTT DWNIPVWYLY NTFLGLEHWL ENIPRWGRLF EELDRNKDGR VDVHELRQGL
ARLSGSDPDR GAQQDLSSQE AEVEASGGLD LEEFSRYLQE RERRLRLMFH SLDRNQDGHI
DVSEIQQSFR ALGISISLEQ VEKILHSMDR DGTMTIDWQE WRDHFLLHSL ENVEDVLYFW
KHSTVLDIGE CLMVPDEFSQ QEKLTGMWWK QLVAGAVAGA VSRTGTAPLD RLKVFMQVHA
SKTNRLNILG GLRSMVREGG VRSLWRGNGI NVLKIAPESA IKFMAYEQIK RAIRGQQDTL
HVQERFVAGS LAGATAQTVI YPMEVLKTRL TLRRTGQYNG LLDCARRILE QEGPRAFYRG
YLPNVLGIIP YAGIDLAVYE TLKNRWLQQC GRESANPGIL VLLACGTISS TCGQIASYPL
ALVRTRMQAQ ASLEGAQQLS MTGLLRHILA QEGVWGLYRG IAPNFMKVIP AVSLSYVVYE
NMKQALGVSS R
//
