SCMC1_BOVIN
ID SCMC1_BOVIN Reviewed; 477 AA.
AC A5PJZ1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Calcium-binding mitochondrial carrier protein SCaMC-1;
DE AltName: Full=Small calcium-binding mitochondrial carrier protein 1;
DE AltName: Full=Solute carrier family 25 member 24;
GN Name=SLC25A24; Synonyms=SCAMC1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Calcium-dependent mitochondrial solute carrier. Mitochondrial
CC solute carriers shuttle metabolites, nucleotides, and cofactors through
CC the mitochondrial inner membrane. May act as a ATP-Mg/Pi exchanger that
CC mediates the transport of Mg-ATP in exchange for phosphate, catalyzing
CC the net uptake or efflux of adenine nucleotides into or from the
CC mitochondria (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; BC142292; AAI42293.1; -; mRNA.
DR RefSeq; NP_001092536.1; NM_001099066.1.
DR AlphaFoldDB; A5PJZ1; -.
DR SMR; A5PJZ1; -.
DR STRING; 9913.ENSBTAP00000004885; -.
DR PaxDb; A5PJZ1; -.
DR PeptideAtlas; A5PJZ1; -.
DR PRIDE; A5PJZ1; -.
DR Ensembl; ENSBTAT00000004885; ENSBTAP00000004885; ENSBTAG00000003752.
DR GeneID; 534742; -.
DR KEGG; bta:534742; -.
DR CTD; 29957; -.
DR VEuPathDB; HostDB:ENSBTAG00000003752; -.
DR VGNC; VGNC:55682; SLC25A24.
DR eggNOG; KOG0036; Eukaryota.
DR GeneTree; ENSGT00940000158786; -.
DR HOGENOM; CLU_015166_2_0_1; -.
DR InParanoid; A5PJZ1; -.
DR OMA; LGIFPYA; -.
DR OrthoDB; 442523at2759; -.
DR TreeFam; TF313492; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000003752; Expressed in abomasum and 107 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005347; F:ATP transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR Gene3D; 1.50.40.10; -; 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; Graves_DC.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
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; SSF103506; SSF103506; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 4.
DR PROSITE; PS50920; SOLCAR; 3.
PE 2: Evidence at transcript level;
KW Acetylation; Calcium; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..477
FT /note="Calcium-binding mitochondrial carrier protein SCaMC-
FT 1"
FT /id="PRO_0000317593"
FT TOPO_DOM 1..197
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..215
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..252
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..272
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..295
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..309
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..345
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..365
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..388
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..406
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..445
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..465
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..477
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 19..54
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 61..85
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 86..121
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 122..157
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 192..278
FT /note="Solcar 1"
FT REPEAT 286..371
FT /note="Solcar 2"
FT REPEAT 383..471
FT /note="Solcar 3"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 99
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 101
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 320
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMD8"
FT MOD_RES 320
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMD8"
FT MOD_RES 336
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6NUK1"
FT MOD_RES 437
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q6NUK1"
FT MOD_RES 437
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMD8"
SQ SEQUENCE 477 AA; 53285 MW; A3B7F5F083BE8631 CRC64;
MLRWLRGFVL PTAACQDVEP PTRYETLFQK LDRNGDGVVD ISELQEGLKS LGIPLGQDAE
EKIFTTGDVN KDGKLDFEEF MKYLKDHEKK MKLAFKSLDK NNDGKIEASE IVQSLQILGL
TISEQQAELI LQSIDADGTM TVDWNEWRDY FLFNPVTDIE EIIRFWKHST GIDIGDSLTI
PDEFTEDEKK SGQWWRQLLA GGVAGAVSRT STAPLDRLKV MMQVHGSKSA KMNIYGGFQQ
MVKEGGIRSL WRGNGTNVIK IAPETAVKFW AYEQYKKLLT EEGQKIGTFE RFVSGSMAGA
TAQTFIYPME VLKTRLAVGK TGQYSGMFDC AKKILKYEGM GAFYKGYVPN LLGIIPYAGI
DLAVYELLKS HWLDNFAKDS VNPGVMVLLG CGALSSTCGQ LASYPLALVR TRMQAQAMIE
KSPQLNMVGL FRRILSKEGL PGLYRGITPN FMKVLPAVGI SYVVYENMKQ TLGVTQK
