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ODC_PONAB
ID   ODC_PONAB               Reviewed;         299 AA.
AC   Q5RFB7;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Mitochondrial 2-oxodicarboxylate carrier;
DE   AltName: Full=Solute carrier family 25 member 21;
GN   Name=SLC25A21; Synonyms=ODC;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transports dicarboxylates across the inner membranes of
CC       mitochondria by a counter-exchange mechanism. Can transport 2-
CC       oxoadipate (2-oxohexanedioate), 2-oxoglutarate, adipate (hexanedioate),
CC       glutarate, and to a lesser extent, pimelate (heptanedioate), 2-
CC       oxopimelate (2-oxoheptanedioate), 2-aminoadipate (2-aminohexanedioate),
CC       oxaloacetate, and citrate. Plays a central role in catabolism of
CC       lysine, hydroxylysine, and tryptophan, by transporting common
CC       metabolite intermediates (such as 2-oxoadipate) into the mitochondria,
CC       where it is converted into acetyl-CoA and can enter the citric acid
CC       (TCA) cycle. {ECO:0000250|UniProtKB:Q9BQT8}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoadipate(in) + 2-oxoglutarate(out) = 2-oxoadipate(out) +
CC         2-oxoglutarate(in); Xref=Rhea:RHEA:71739, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:57499; Evidence={ECO:0000250|UniProtKB:Q9BQT8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate(out) + hexanedioate(in) = 2-oxoglutarate(in) +
CC         hexanedioate(out); Xref=Rhea:RHEA:71743, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:17128; Evidence={ECO:0000250|UniProtKB:Q9BQT8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate(out) + L-2-aminoadipate(in) = 2-
CC         oxoglutarate(in) + L-2-aminoadipate(out); Xref=Rhea:RHEA:71747,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:58672;
CC         Evidence={ECO:0000250|UniProtKB:Q9BQT8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate(out) + glutarate(in) = 2-oxoglutarate(in) +
CC         glutarate(out); Xref=Rhea:RHEA:71751, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:30921; Evidence={ECO:0000250|UniProtKB:Q9BQT8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate(out) + 2-oxoheptanedioate(in) = 2-
CC         oxoglutarate(in) + 2-oxoheptanedioate(out); Xref=Rhea:RHEA:71755,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:72701;
CC         Evidence={ECO:0000250|UniProtKB:Q9BQT8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate(out) + heptanedioate(in) = 2-oxoglutarate(in) +
CC         heptanedioate(out); Xref=Rhea:RHEA:71759, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:36165; Evidence={ECO:0000250|UniProtKB:Q9BQT8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate(out) + citrate(in) = 2-oxoglutarate(in) +
CC         citrate(out); Xref=Rhea:RHEA:71763, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:16947; Evidence={ECO:0000250|UniProtKB:Q9BQT8};
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; CR857243; CAH89540.1; -; mRNA.
DR   RefSeq; NP_001124669.1; NM_001131197.1.
DR   AlphaFoldDB; Q5RFB7; -.
DR   SMR; Q5RFB7; -.
DR   STRING; 9601.ENSPPYP00000006539; -.
DR   Ensembl; ENSPPYT00000033794; ENSPPYP00000024530; ENSPPYG00000005756.
DR   GeneID; 100171514; -.
DR   KEGG; pon:100171514; -.
DR   CTD; 89874; -.
DR   eggNOG; KOG0754; Eukaryota.
DR   GeneTree; ENSGT00730000111119; -.
DR   InParanoid; Q5RFB7; -.
DR   OMA; MLLVFDY; -.
DR   OrthoDB; 1236425at2759; -.
DR   TreeFam; TF314035; -.
DR   Proteomes; UP000001595; Chromosome 14.
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:0055085; P:transmembrane transport; IEA:InterPro.
DR   Gene3D; 1.50.40.10; -; 2.
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   Antiport; Lipid transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..299
FT                   /note="Mitochondrial 2-oxodicarboxylate carrier"
FT                   /id="PRO_0000090646"
FT   TRANSMEM        17..37
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..89
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          11..100
FT                   /note="Solcar 1"
FT   REPEAT          107..196
FT                   /note="Solcar 2"
FT   REPEAT          205..294
FT                   /note="Solcar 3"
SQ   SEQUENCE   299 AA;  33286 MW;  5BED9506E8F955D9 CRC64;
     MSAKPEVGLV REASRQIVAG GSAGLVEICL MHPLDVVKTR FQIQRCATDP NSYKSLVDSF
     RMIFQTERLF GFYKGILPPI LAETPKRAVK FFTFEQYKKL LGYVSLSPAL TFTIAGLGSG
     LTEAIVVNPF EVVKVGLQAN RNTFAKQPST VGYARQIIKK EGWGLQGLNK GLTATLGRHG
     VFNMVYFGFY YNVKNMIPVN KDPTLEFLRK FGIGLLSGTI ASVINIPFDV AKSRIQGPQP
     VPGEIKYRTC FKTMATVYQE EGILALYKGL LPKIMRLGPG GAVMLLVYEY TYSWLQENW
 
 
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