SCMC2_RAT
ID SCMC2_RAT Reviewed; 469 AA.
AC Q8K3P6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Calcium-binding mitochondrial carrier protein SCaMC-2;
DE AltName: Full=Mitochondrial ATP-Mg/Pi carrier protein;
DE AltName: Full=Peroxisomal Ca(2+)-dependent solute carrier-like protein;
DE AltName: Full=Small calcium-binding mitochondrial carrier protein 2;
DE AltName: Full=Solute carrier family 25 member 25;
GN Name=Slc25a25; Synonyms=Mcsc, Pcscl, Scamc2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, CALCIUM-BINDING, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=Sprague-Dawley;
RX PubMed=12645546; DOI=10.1074/jbc.m208398200;
RA Mashima H., Ueda N., Ohno H., Suzuki J., Ohnishi H., Yasuda H.,
RA Tsuchida T., Kanamaru C., Makita N., Iiri T., Omata M., Kojima I.;
RT "A novel mitochondrial Ca2+-dependent solute carrier in the liver
RT identified by mRNA differential display.";
RL J. Biol. Chem. 278:9520-9527(2003).
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
CC {ECO:0000269|PubMed:12645546}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12645546}.
CC -!- TISSUE SPECIFICITY: Mainly present in the liver and the skeletal muscle
CC (at protein level). {ECO:0000269|PubMed:12645546}.
CC -!- DEVELOPMENTAL STAGE: In the liver, expression is higher in the adult
CC stage than in the fetal stage. {ECO:0000269|PubMed:12645546}.
CC -!- INDUCTION: Up-regulated in dexamethasone-treated cells before the
CC expression of albumin. {ECO:0000269|PubMed:12645546}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AY043169; AAL05592.1; -; mRNA.
DR RefSeq; NP_663710.1; NM_145677.1.
DR AlphaFoldDB; Q8K3P6; -.
DR SMR; Q8K3P6; -.
DR BioGRID; 251620; 1.
DR STRING; 10116.ENSRNOP00000020206; -.
DR iPTMnet; Q8K3P6; -.
DR PhosphoSitePlus; Q8K3P6; -.
DR jPOST; Q8K3P6; -.
DR PaxDb; Q8K3P6; -.
DR PRIDE; Q8K3P6; -.
DR GeneID; 246771; -.
DR KEGG; rno:246771; -.
DR UCSC; RGD:628666; rat.
DR CTD; 114789; -.
DR RGD; 628666; Slc25a25.
DR VEuPathDB; HostDB:ENSRNOG00000014338; -.
DR eggNOG; KOG0036; Eukaryota.
DR HOGENOM; CLU_015166_2_0_1; -.
DR InParanoid; Q8K3P6; -.
DR OMA; DIWMQEG; -.
DR OrthoDB; 442523at2759; -.
DR PRO; PR:Q8K3P6; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000014338; Expressed in liver and 20 other tissues.
DR Genevisible; Q8K3P6; RN.
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:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0005347; F:ATP transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0060612; P:adipose tissue development; ISO:RGD.
DR GO; GO:0046034; P:ATP metabolic process; ISO:RGD.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISO:RGD.
DR GO; GO:0043010; P:camera-type eye development; ISO:RGD.
DR GO; GO:0045333; P:cellular respiration; ISO:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0014823; P:response to activity; ISO:RGD.
DR GO; GO:0002021; P:response to dietary excess; ISO:RGD.
DR GO; GO:0032094; P:response to food; ISO:RGD.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
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; 1.
DR Pfam; PF13833; EF-hand_8; 1.
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; PS50222; EF_HAND_2; 3.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Calcium; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..469
FT /note="Calcium-binding mitochondrial carrier protein SCaMC-
FT 2"
FT /id="PRO_0000317604"
FT TOPO_DOM 1..189
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..207
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..244
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..264
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..287
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..301
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..337
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..357
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..380
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..398
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..437
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..457
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..469
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 47..80
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 78..113
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 114..149
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 184..270
FT /note="Solcar 1"
FT REPEAT 278..363
FT /note="Solcar 2"
FT REPEAT 375..463
FT /note="Solcar 3"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 52695 MW; 95E5DA46B9942992 CRC64;
MLCLCLYVPI AGEAQTEFQY FESKGLPTEL KSIFKLSVFI PSQEFSTYRQ WKQKIVQAGD
KDLDGQLDFE EFVHYLQDHE KKLRLVFKSL DKKNDGRIDA QEIMQSLRDL GVKISEQQAE
KILKSMDKNG TMTIDWNEWR DYHLLHPVEN IPEIILYWKH STIFDVGENL TVPDEFTVEE
RQTGMWWRHL VAGGGAGAVS RTCTAPLDRL KVLMQVHASR SNNMCIIGGF TQMIREGGAK
SLWRGNGINV LKIAPESAIK FMAYEQMKRL VGSDQETLRI HERLVAGSLA GAIAQSSIYP
MEVLKTRMAL RKTGQYSGML DCAKRILAKE GVAAFYKGYI PNMLGIIPYA GIDLAVYETL
KNTWLQRYAV NSADPGVFVL LACGTISSTC GQLASYPLAL VRTRMQAQAS IEGAPEVTMS
SLFKQILRTE GAFGLYRGLA PNFMKVIPAV SISYVVYENL KITLGVQSR
