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SCMC2_BOVIN
ID   SCMC2_BOVIN             Reviewed;         469 AA.
AC   Q0V7M4; Q32PJ0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Calcium-binding mitochondrial carrier protein SCaMC-2;
DE   AltName: Full=Small calcium-binding mitochondrial carrier protein 2;
DE   AltName: Full=Solute carrier family 25 member 25;
GN   Name=SLC25A25; Synonyms=SCAMC2;
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].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2005) 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; BT026546; ABH06333.1; -; mRNA.
DR   EMBL; BC108098; AAI08099.1; -; mRNA.
DR   RefSeq; NP_001033234.1; NM_001038145.2.
DR   AlphaFoldDB; Q0V7M4; -.
DR   SMR; Q0V7M4; -.
DR   STRING; 9913.ENSBTAP00000015802; -.
DR   PaxDb; Q0V7M4; -.
DR   PRIDE; Q0V7M4; -.
DR   GeneID; 527786; -.
DR   KEGG; bta:527786; -.
DR   CTD; 114789; -.
DR   eggNOG; KOG0036; Eukaryota.
DR   HOGENOM; CLU_015166_2_0_1; -.
DR   InParanoid; Q0V7M4; -.
DR   OrthoDB; 442523at2759; -.
DR   TreeFam; TF313492; -.
DR   Proteomes; UP000009136; Unplaced.
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; 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   2: Evidence at transcript 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_0000317601"
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"
FT   CONFLICT        273
FT                   /note="S -> R (in Ref. 2; AAI08099)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        306
FT                   /note="T -> A (in Ref. 2; AAI08099)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        378
FT                   /note="F -> C (in Ref. 2; AAI08099)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   469 AA;  52769 MW;  CF76F06BFA976B3F CRC64;
     MLCLCLYVPL IGEAQTEFQY FESKGLPAEL KSIFKLSVFI PSQEFSTYRQ WKQKIVQAGD
     KDLDGQLDFE EFVHYLQDHE KKLRLVFKSL DKKNDGRIDA QEIMQSLRDL GVKISEQQAE
     KILKSMDKNG TMTIDWNEWR DYHLLHPVEN IPEIILYWKH STIFDVGENL TVPDEFTVEE
     RQTGMWWRHL VAGGGAGAVS RTCTAPLDRL KVLMQVHASR SNNMCIVGGF TQMIREGGAR
     SLWRGNGINV LKIAPESAIK FMAYEQIKRL IGSDQETLRI HERLVAGSLA GAIAQSSIYP
     MEVLKTRMAL RKTGQYSGML DCARKILARE GMAAFYKGYV PNMLGIIPYA GIDLAVYETL
     KNAWLQRYAV NSADPGVFVL LACGTMSSTC GQLASYPLAL VRTRMQAQAS MEGAPEVTMS
     SLFKQILRTE GAFGLYRGLA PNFMKVIPAV SISYVVYENL KITLGVQSR
 
 
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