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DIC_CAEEL
ID   DIC_CAEEL               Reviewed;         290 AA.
AC   G5EE96;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Mitochondrial dicarboxylate carrier;
DE            Short=DIC;
DE   AltName: Full=Solute carrier family 25 member 10 homolog;
GN   Name=slc-25a10 {ECO:0000312|WormBase:K11G12.5};
GN   ORFNames=K11G12.5 {ECO:0000312|WormBase:K11G12.5};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7803813; DOI=10.3109/10425179409020854;
RA   Runswick M.J., Philippides A., Lauria G., Walker J.E.;
RT   "Extension of the mitochondrial transporter super-family: sequences of five
RT   members from the nematode worm, Caenorhabditis elegans.";
RL   DNA Seq. 4:281-291(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   FUNCTION, AND TRANSPORT ACTIVITY.
RX   PubMed=9733776; DOI=10.1074/jbc.273.38.24754;
RA   Fiermonte G., Palmieri L., Dolce V., Lasorsa F.M., Palmieri F.,
RA   Runswick M.J., Walker J.E.;
RT   "The sequence, bacterial expression, and functional reconstitution of the
RT   rat mitochondrial dicarboxylate transporter cloned via distant homologs in
RT   yeast and Caenorhabditis elegans.";
RL   J. Biol. Chem. 273:24754-24759(1998).
CC   -!- FUNCTION: Catalyzes the electroneutral exchange or flux of
CC       physiologically important metabolites such as dicarboxylates (malonate,
CC       malate, succinate), inorganic sulfur-containing anions, and phosphate,
CC       across mitochondrial inner membrane (PubMed:9733776). Plays an
CC       important role in gluconeogenesis, fatty acid metabolism, urea
CC       synthesis, and sulfur metabolism, by supplying the substrates for the
CC       different metabolic processes (By similarity).
CC       {ECO:0000250|UniProtKB:Q9QZD8, ECO:0000269|PubMed:9733776}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate(in) + phosphate(out) = (S)-malate(out) +
CC         phosphate(in); Xref=Rhea:RHEA:71607, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:43474; Evidence={ECO:0000269|PubMed:9733776};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate(in) + malonate(out) = (S)-malate(out) +
CC         malonate(in); Xref=Rhea:RHEA:71611, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:15792; Evidence={ECO:0000269|PubMed:9733776};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate(in) + succinate(out) = (S)-malate(out) +
CC         succinate(in); Xref=Rhea:RHEA:29327, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:30031; Evidence={ECO:0000269|PubMed:9733776};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate(in) + sulfate(out) = (S)-malate(out) + sulfate(in);
CC         Xref=Rhea:RHEA:71615, ChEBI:CHEBI:15589, ChEBI:CHEBI:16189;
CC         Evidence={ECO:0000269|PubMed:9733776};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate(in) + 2 thiosulfate(out) = (S)-malate(out) + 2
CC         thiosulfate(in); Xref=Rhea:RHEA:71619, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:33542; Evidence={ECO:0000269|PubMed:9733776};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=malonate(out) + phosphate(in) = malonate(in) + phosphate(out);
CC         Xref=Rhea:RHEA:71623, ChEBI:CHEBI:15792, ChEBI:CHEBI:43474;
CC         Evidence={ECO:0000269|PubMed:9733776};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate(in) + succinate(out) = phosphate(out) +
CC         succinate(in); Xref=Rhea:RHEA:71627, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:43474; Evidence={ECO:0000269|PubMed:9733776};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate(in) + sulfate(out) = phosphate(out) + sulfate(in);
CC         Xref=Rhea:RHEA:71631, ChEBI:CHEBI:16189, ChEBI:CHEBI:43474;
CC         Evidence={ECO:0000269|PubMed:9733776};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate(in) + 2 thiosulfate(out) = phosphate(out) + 2
CC         thiosulfate(in); Xref=Rhea:RHEA:71635, ChEBI:CHEBI:33542,
CC         ChEBI:CHEBI:43474; Evidence={ECO:0000269|PubMed:9733776};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=malonate(out) + succinate(in) = malonate(in) + succinate(out);
CC         Xref=Rhea:RHEA:71667, ChEBI:CHEBI:15792, ChEBI:CHEBI:30031;
CC         Evidence={ECO:0000250|UniProtKB:Q9QZD8};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q9QZD8}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000305}.
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DR   EMBL; X76114; CAA53720.1; -; mRNA.
DR   EMBL; BX284606; CCD70797.1; -; Genomic_DNA.
DR   PIR; S44091; S44091.
DR   RefSeq; NP_509133.1; NM_076732.5.
DR   SMR; G5EE96; -.
DR   STRING; 6239.K11G12.5; -.
DR   EnsemblMetazoa; K11G12.5.1; K11G12.5.1; WBGene00019656.
DR   GeneID; 180940; -.
DR   KEGG; cel:CELE_K11G12.5; -.
DR   CTD; 180940; -.
DR   WormBase; K11G12.5; CE02827; WBGene00019656; slc-25A10.
DR   eggNOG; KOG0759; Eukaryota.
DR   GeneTree; ENSGT00940000156783; -.
DR   HOGENOM; CLU_015166_14_1_1; -.
DR   OMA; FGAYEVG; -.
DR   OrthoDB; 984118at2759; -.
DR   Reactome; R-CEL-1614517; Sulfide oxidation to sulfate.
DR   Reactome; R-CEL-428643; Organic anion transporters.
DR   Reactome; R-CEL-70263; Gluconeogenesis.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00019656; Expressed in larva and 4 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0015297; F:antiporter activity; IBA:GO_Central.
DR   GO; GO:0015140; F:malate transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015131; F:oxaloacetate transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015141; F:succinate transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015116; F:sulfate transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015117; F:thiosulfate transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0071423; P:malate transmembrane transport; IBA:GO_Central.
DR   GO; GO:0015729; P:oxaloacetate transport; IBA:GO_Central.
DR   GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0071422; P:succinate transmembrane transport; IBA:GO_Central.
DR   GO; GO:0008272; P:sulfate transport; IBA:GO_Central.
DR   GO; GO:0015709; P:thiosulfate transport; IBA:GO_Central.
DR   Gene3D; 1.50.40.10; -; 1.
DR   InterPro; IPR002067; Mit_carrier.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00926; MITOCARRIER.
DR   SUPFAM; SSF103506; SSF103506; 1.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   2: Evidence at transcript level;
KW   Acetylation; Antiport; Lipid transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..290
FT                   /note="Mitochondrial dicarboxylate carrier"
FT                   /id="PRO_0000456254"
FT   TRANSMEM        12..32
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        65..84
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..182
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        203..223
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        256..276
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          6..90
FT                   /note="Solcar 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT   REPEAT          101..188
FT                   /note="Solcar 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT   REPEAT          197..281
FT                   /note="Solcar 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT   MOD_RES         159
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QZD8"
SQ   SEQUENCE   290 AA;  32022 MW;  850BAF3CF11D9AFF CRC64;
     MAEDKTKRLG RWYFGGVAGA MAACCTHPLD LLKVQLQTQQ QGKLTIGQLS LKIYKNDGIL
     AFYNGVSASV LRQLTYSTTR FGIYETVKKQ LPQDQPLPFY QKALLAGFAG ACGGMVGTPG
     DLVNVRMQND SKLPLEQRRN YKHALDGLVR ITREEGFMKM FNGATMATSR AILMTIGQLS
     FYDQIKQTLI SSGVAEDNLQ THFASSISAA SVATVMTQPL DVMKTRMMNA APGEFKGILD
     CFMFTAKLGP MGFFKGFIPA WARLAPHTVL TFIFFEQLRL KFGYAPPVKA
 
 
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