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DHSD_PONAB
ID   DHSD_PONAB              Reviewed;         159 AA.
AC   Q5RC29;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial;
DE            Short=CybS;
DE   AltName: Full=CII-4;
DE   AltName: Full=QPs3;
DE   AltName: Full=Succinate dehydrogenase complex subunit D;
DE   AltName: Full=Succinate-ubiquinone oxidoreductase cytochrome b small subunit;
DE   AltName: Full=Succinate-ubiquinone reductase membrane anchor subunit;
DE   Flags: Precursor;
GN   Name=SDHD;
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: Membrane-anchoring subunit of succinate dehydrogenase (SDH)
CC       that is involved in complex II of the mitochondrial electron transport
CC       chain and is responsible for transferring electrons from succinate to
CC       ubiquinone (coenzyme Q). {ECO:0000250}.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC   -!- SUBUNIT: Component of complex II composed of four subunits: the
CC       flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a cytochrome
CC       b560 composed of SDHC and SDHD. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CybS family. {ECO:0000305}.
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DR   EMBL; CR858453; CAH90681.1; -; mRNA.
DR   RefSeq; NP_001125372.1; NM_001131900.1.
DR   AlphaFoldDB; Q5RC29; -.
DR   SMR; Q5RC29; -.
DR   STRING; 9601.ENSPPYP00000004440; -.
DR   Ensembl; ENSPPYT00000055581; ENSPPYP00000040446; ENSPPYG00000003876.
DR   GeneID; 100172275; -.
DR   KEGG; pon:100172275; -.
DR   CTD; 6392; -.
DR   eggNOG; KOG4097; Eukaryota.
DR   GeneTree; ENSGT00390000010003; -.
DR   HOGENOM; CLU_096618_1_1_1; -.
DR   InParanoid; Q5RC29; -.
DR   OMA; KLERLWA; -.
DR   OrthoDB; 1511215at2759; -.
DR   TreeFam; TF313310; -.
DR   UniPathway; UPA00223; -.
DR   Proteomes; UP000001595; Chromosome 11.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048039; F:ubiquinone binding; ISS:UniProtKB.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd03496; SQR_TypeC_CybS; 1.
DR   Gene3D; 1.20.1300.10; -; 1.
DR   InterPro; IPR007992; CybS.
DR   InterPro; IPR034804; SQR/QFR_C/D.
DR   PANTHER; PTHR13337; PTHR13337; 1.
DR   SUPFAM; SSF81343; SSF81343; 1.
PE   2: Evidence at transcript level;
KW   Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW   Transmembrane; Transmembrane helix; Transport; Tricarboxylic acid cycle.
FT   TRANSIT         1..56
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           57..159
FT                   /note="Succinate dehydrogenase [ubiquinone] cytochrome b
FT                   small subunit, mitochondrial"
FT                   /id="PRO_0000043355"
FT   TOPO_DOM        57..63
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        64..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        86..90
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        112..120
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        121..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        143..159
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_note="ligand shared with SDHC"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:A5GZW8"
FT   BINDING         114
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /ligand_note="ligand shared with IP/SDHB"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   159 AA;  17032 MW;  28C000B4BAA8C2F1 CRC64;
     MAVLWRLSAV CGAQGGRALL LRTPVVRPAH ISAFLQDRPI PEWCGVQHIH LSPGHHSGSK
     AASLHWTSER VVSVLLLGLL PAAYLNPCSA MDYSLAATLT LHGHWGLGQV VTDYVHGDAS
     QKAAKAGLLA LSALTFAGLC YFNYHDVGIC KAVAMLWKL
 
 
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