ID G8F685_MACFA Unreviewed; 390 AA.
AC G8F685;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=EF-hand domain-containing protein {ECO:0000259|PROSITE:PS50222};
DE Flags: Fragment;
GN ORFNames=EGM_19393 {ECO:0000313|EMBL:EHH62799.1};
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 {ECO:0000313|Proteomes:UP000009130};
RN [1] {ECO:0000313|EMBL:EHH62799.1, ECO:0000313|Proteomes:UP000009130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH62799.1,
RC ECO:0000313|Proteomes:UP000009130};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
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; JH333776; EHH62799.1; -; Genomic_DNA.
DR AlphaFoldDB; G8F685; -.
DR Proteomes; UP000009130; 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 GO; GO:0071705; P:nitrogen compound transport; IEA:UniProt.
DR CDD; cd00051; EFh; 2.
DR Gene3D; 1.10.238.10; EF-hand; 1.
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:SF196; CALCIUM-BINDING MITOCHONDRIAL CARRIER PROTEIN SCAMC-3; 1.
DR PANTHER; PTHR24089; SOLUTE CARRIER FAMILY 25; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF00153; Mito_carr; 2.
DR PRINTS; PR00928; GRAVESDC.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50920; SOLCAR; 2.
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 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 26..61
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 62..97
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REPEAT 190..276
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 284..369
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHH62799.1"
FT NON_TER 390
FT /evidence="ECO:0000313|EMBL:EHH62799.1"
SQ SEQUENCE 390 AA; 44186 MW; 158A5E9D100D8E62 CRC64;
QGISSEGDAD PDGGLDLEEF SRYLQEREQR LLLMFHSLDR NQDGHIDVSE IQQSFRALGI
SITLEQAEKI LHSMDRDGTM TIDWQEWRDH FLLHSLENVE DVLYFWKHST LPSAGFSAWI
KDSTTERNRS KTTVFAGRGG SRLESQHFGR PRQADHEIRR LRPSWLTWVL DIGECLTVPD
EFSKQEKLTG MWWKQLVAGA VAGAVSRTGT APLDRLKVFM QVHASKTNRL NILGGLRSMV
LEGGIRSLWR GNGINVLKIA PESAIKFMAY EQIKRAILGQ QETLHVQERF VAGSLAGATA
QTIIYPMEVL KTRLTLRRTG QYKGLLDCAR RILEREGPRA FYRGYLPNVL GIIPYAGIDL
AVYEGWSVMA QSRLTATYTS WVQAILLPQS
//
