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C560_DICDI
ID   C560_DICDI              Reviewed;         192 AA.
AC   Q8T2T5; Q554F4;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Succinate dehydrogenase cytochrome b560 subunit, mitochondrial;
DE   Flags: Precursor;
GN   Name=sdhC; ORFNames=DDB_G0275115;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:D0VWV4};
CC       Note=The heme b is bound between the two transmembrane cytochrome b560
CC       subunits. {ECO:0000250|UniProtKB:D0VWV4};
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 cytochrome b560 family. {ECO:0000305}.
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DR   EMBL; AAFI02000013; EAL69838.1; -; Genomic_DNA.
DR   RefSeq; XP_643757.1; XM_638665.1.
DR   AlphaFoldDB; Q8T2T5; -.
DR   SMR; Q8T2T5; -.
DR   STRING; 44689.DDB0231385; -.
DR   PaxDb; Q8T2T5; -.
DR   PRIDE; Q8T2T5; -.
DR   EnsemblProtists; EAL69838; EAL69838; DDB_G0275115.
DR   GeneID; 8619802; -.
DR   KEGG; ddi:DDB_G0275115; -.
DR   dictyBase; DDB_G0275115; sdhC.
DR   eggNOG; KOG0449; Eukaryota.
DR   HOGENOM; CLU_1417530_0_0_1; -.
DR   InParanoid; Q8T2T5; -.
DR   OMA; MIGRTIL; -.
DR   PhylomeDB; Q8T2T5; -.
DR   Reactome; R-DDI-71403; Citric acid cycle (TCA cycle).
DR   UniPathway; UPA00223; -.
DR   PRO; PR:Q8T2T5; -.
DR   Proteomes; UP000002195; Chromosome 2.
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:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000104; F:succinate dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.20.1300.10; -; 1.
DR   InterPro; IPR034804; SQR/QFR_C/D.
DR   InterPro; IPR014314; Succ_DH_cytb556.
DR   InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR   PANTHER; PTHR10978; PTHR10978; 1.
DR   Pfam; PF01127; Sdh_cyt; 1.
DR   SUPFAM; SSF81343; SSF81343; 1.
DR   TIGRFAMs; TIGR02970; succ_dehyd_cytB; 1.
PE   3: Inferred from homology;
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..27
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..192
FT                   /note="Succinate dehydrogenase cytochrome b560 subunit,
FT                   mitochondrial"
FT                   /id="PRO_0000327439"
FT   TOPO_DOM        48..83
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        84..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        114..131
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        132..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        157..164
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        165..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        187..189
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   BINDING         146
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_note="ligand shared with sdhd"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWV4"
SQ   SEQUENCE   192 AA;  21379 MW;  668B337821B289EC CRC64;
     MFGRTLNTFT SRNAPLVRNF DKFIVNNTLT SKNIYLSQTN TTNTPLSYST QAKKPFTITE
     KRIDELKTPY QPTSPHLTIY KFPLPAVMSI MHRATGICLA LGITGLAGVT LFAPHDAIHY
     IQLLHTQYPA LVYPAKFAVA LPLTYHFCTG VRHIIWDETV KGLSISQIES SGKVLLAVVA
     VLSTIFTFVS FK
 
 
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