SCMC1_RABIT
ID SCMC1_RABIT Reviewed; 475 AA.
AC O18757;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Calcium-binding mitochondrial carrier protein SCaMC-1;
DE AltName: Full=Peroxisomal Ca(2+)-dependent solute carrier;
DE AltName: Full=Small calcium-binding mitochondrial carrier protein 1;
DE AltName: Full=Solute carrier family 25 member 24;
GN Name=SLC25A24; Synonyms=EFINAL, SCAMC1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, CALCIUM-BINDING, TISSUE
RP SPECIFICITY, AND TOPOLOGY.
RC TISSUE=Small intestine;
RX PubMed=9238007; DOI=10.1073/pnas.94.16.8509;
RA Weber F.E., Minestrini G., Dyer J.H., Werder M., Boffelli D., Compassi S.,
RA Wehrli E., Thomas R.M., Schulthess G., Hauser H.;
RT "Molecular cloning of a peroxisomal Ca2+-dependent member of the
RT mitochondrial carrier superfamily.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8509-8514(1997).
CC -!- FUNCTION: Calcium-dependent mitochondrial solute carrier. Mediates the
CC reversible, electroneutral exchange of Mg-ATP or Mg-ADP against
CC phosphate ions, catalyzing the net uptake or efflux of adenine
CC nucleotides across the mitochondrial inner membrane. Nucleotide
CC transport is inactive when cytosolic calcium levels are low, and is
CC activated by an increase in cytosolic calcium levels. May play a role
CC in protecting cells against oxidative stress-induced cell death,
CC probably by promoting the formation of calcium-phosphate precipitates
CC in the mitochondrial matrix, and thereby buffering calcium levels in
CC the mitochondrial matrix (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Peroxisome
CC {ECO:0000269|PubMed:9238007}. Note=According to PubMed:9238007, it is
CC mainly found in peroxisomes while low levels are present in
CC mitochondrion. The relevance of such results remain unclear in vivo.
CC -!- TISSUE SPECIFICITY: Mainly expressed in colon. Also expressed in the
CC small intestine proximal to the ileum. Weakly expressed in kidney but
CC not in the liver. {ECO:0000269|PubMed:9238007}.
CC -!- DOMAIN: The N-terminal domain can bind calcium and regulates the ATP
CC carrier activity of the transmembrane domain. The apo form of the N-
CC terminal domain is intrinsically disordered and binds to the
CC transmembrane domain, leading to inhibition of the ATP carrier
CC activity. Calcium binding leads to a major conformation change and
CC abolishes the interaction with the transmembrane domain and the
CC inhibition of the ATP carrier activity (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AF004161; AAB69156.1; -; mRNA.
DR PIR; T50686; T50686.
DR RefSeq; NP_001076246.1; NM_001082777.1.
DR AlphaFoldDB; O18757; -.
DR SMR; O18757; -.
DR STRING; 9986.ENSOCUP00000011022; -.
DR PRIDE; O18757; -.
DR GeneID; 100009567; -.
DR KEGG; ocu:100009567; -.
DR CTD; 29957; -.
DR eggNOG; KOG0036; Eukaryota.
DR InParanoid; O18757; -.
DR OrthoDB; 442523at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0005347; F:ATP transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0015867; P:ATP transport; ISS:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0006839; P:mitochondrial transport; ISS:UniProtKB.
DR GO; GO:0010941; P:regulation of cell death; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Acetylation; Calcium; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Peroxisome; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..475
FT /note="Calcium-binding mitochondrial carrier protein SCaMC-
FT 1"
FT /id="PRO_0000317596"
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..250
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..270
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..293
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..307
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..343
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..363
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..386
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..404
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..443
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..463
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..475
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 55..88
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..276
FT /note="Solcar 1"
FT REPEAT 284..369
FT /note="Solcar 2"
FT REPEAT 381..469
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 BINDING 135
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000305"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000305"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000305"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000305"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000305"
FT MOD_RES 318
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMD8"
FT MOD_RES 318
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMD8"
FT MOD_RES 334
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6NUK1"
FT MOD_RES 435
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q6NUK1"
FT MOD_RES 435
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMD8"
SQ SEQUENCE 475 AA; 53006 MW; E779D43F7C758269 CRC64;
MLRWLRGFVL PTAACQGAEP PTRYETLFQA LDRNGDGVVD IRELQEGLKS LGIPLGQDAE
EKIFTTGDVN KDGKLDFEEF MKYLKDHEKK MKLAFKSLDK NNDGKIEASE IVQSLQTLGL
TISEQQAELI LQSIDADGTM TVDWNEWRDY FLFNPVADIE EIIRFWKHST GIDIGDSLTI
PDEFTEEERK SGQWWRQLLA GGIAGAVSRT STAPLDRLKV MMQVHGSKSM NIFGGFRQMI
KEGGVRSLWR GNGTNVIKIA PETAVKFWVY EQYKKLLTEE GQKIGTFERF ISGSMAGATA
QTFIYPMEVM KTRLAVGKTG QYSGIYDCAK KILKYEGFGA FYKGYVPNLL GIIPYAGIDL
AVYELLKSHW LDNFAKDSVN PGVLVLLGCG ALSSTCGQLA SYPLALVRTR MQAQAMLEGA
PQLNMVGLFR RIISKEGLPG LYRGITPNFM KVLPAVGISY VVYENMKQTL GVTQK
