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C560_PIG
ID   C560_PIG                Reviewed;         169 AA.
AC   D0VWV4;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 2.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Succinate dehydrogenase cytochrome b560 subunit, mitochondrial;
DE   AltName: Full=Succinate-ubiquinone oxidoreductase cytochrome B large subunit;
DE            Short=CYBL;
DE   Flags: Precursor;
GN   Name=SDHC;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Heart;
RX   PubMed=17480203; DOI=10.1111/j.1742-4658.2007.05698.x;
RA   Huo X., Su D., Wang A., Zhai Y., Xu J., Li X., Bartlam M., Sun F., Rao Z.;
RT   "Preliminary molecular characterization and crystallization of
RT   mitochondrial respiratory complex II from porcine heart.";
RL   FEBS J. 274:1524-1529(2007).
RN   [2] {ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0}
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 30-169 IN COMPLEXES WITH HEME,
RP   SUBUNIT, AND MEMBRANE TOPOLOGY.
RX   PubMed=15989954; DOI=10.1016/j.cell.2005.05.025;
RA   Sun F., Huo X., Zhai Y., Wang A., Xu J., Su D., Bartlam M., Rao Z.;
RT   "Crystal structure of mitochondrial respiratory membrane protein complex
RT   II.";
RL   Cell 121:1043-1057(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:0000269|PubMed:17480203}.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000269|PubMed:15989954};
CC       Note=The heme b is bound between the two transmembrane subunits SDHC
CC       and SDHD. {ECO:0000269|PubMed:15989954};
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:0000269|PubMed:15989954}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:17480203}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:17480203}.
CC   -!- TISSUE SPECIFICITY: Detected in heart muscle (at protein level).
CC       {ECO:0000269|PubMed:17480203}.
CC   -!- SIMILARITY: Belongs to the cytochrome b560 family. {ECO:0000305}.
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DR   RefSeq; XP_003125707.2; XM_003125659.5.
DR   PDB; 1ZOY; X-ray; 2.40 A; C=30-169.
DR   PDB; 1ZP0; X-ray; 3.50 A; C=30-169.
DR   PDB; 3ABV; X-ray; 3.24 A; C=30-169.
DR   PDB; 3AE1; X-ray; 3.14 A; C=30-169.
DR   PDB; 3AE2; X-ray; 3.10 A; C=30-169.
DR   PDB; 3AE3; X-ray; 3.35 A; C=30-169.
DR   PDB; 3AE4; X-ray; 2.91 A; C=30-169.
DR   PDB; 3AE5; X-ray; 3.41 A; C=30-169.
DR   PDB; 3AE6; X-ray; 3.40 A; C=30-169.
DR   PDB; 3AE7; X-ray; 3.62 A; C=30-169.
DR   PDB; 3AE8; X-ray; 3.40 A; C=30-169.
DR   PDB; 3AE9; X-ray; 3.31 A; C=30-169.
DR   PDB; 3AEA; X-ray; 3.39 A; C=30-169.
DR   PDB; 3AEB; X-ray; 3.00 A; C=30-169.
DR   PDB; 3AEC; X-ray; 3.61 A; C=30-169.
DR   PDB; 3AED; X-ray; 3.52 A; C=30-169.
DR   PDB; 3AEE; X-ray; 3.22 A; C=30-169.
DR   PDB; 3AEF; X-ray; 2.80 A; C=30-169.
DR   PDB; 3AEG; X-ray; 3.27 A; C=30-169.
DR   PDB; 3SFD; X-ray; 2.61 A; C=30-169.
DR   PDB; 3SFE; X-ray; 2.81 A; C=30-169.
DR   PDB; 4YTP; X-ray; 3.10 A; C=1-169.
DR   PDB; 4YXD; X-ray; 3.00 A; C=1-169.
DR   PDBsum; 1ZOY; -.
DR   PDBsum; 1ZP0; -.
DR   PDBsum; 3ABV; -.
DR   PDBsum; 3AE1; -.
DR   PDBsum; 3AE2; -.
DR   PDBsum; 3AE3; -.
DR   PDBsum; 3AE4; -.
DR   PDBsum; 3AE5; -.
DR   PDBsum; 3AE6; -.
DR   PDBsum; 3AE7; -.
DR   PDBsum; 3AE8; -.
DR   PDBsum; 3AE9; -.
DR   PDBsum; 3AEA; -.
DR   PDBsum; 3AEB; -.
DR   PDBsum; 3AEC; -.
DR   PDBsum; 3AED; -.
DR   PDBsum; 3AEE; -.
DR   PDBsum; 3AEF; -.
DR   PDBsum; 3AEG; -.
DR   PDBsum; 3SFD; -.
DR   PDBsum; 3SFE; -.
DR   PDBsum; 4YTP; -.
DR   PDBsum; 4YXD; -.
DR   AlphaFoldDB; D0VWV4; -.
DR   SMR; D0VWV4; -.
DR   STRING; 9823.ENSSSCP00000027481; -.
DR   BindingDB; D0VWV4; -.
DR   ChEMBL; CHEMBL2366564; -.
DR   PaxDb; D0VWV4; -.
DR   PeptideAtlas; D0VWV4; -.
DR   PRIDE; D0VWV4; -.
DR   Ensembl; ENSSSCT00000045783; ENSSSCP00000053659; ENSSSCG00000030318.
DR   Ensembl; ENSSSCT00015011874; ENSSSCP00015004688; ENSSSCG00015008931.
DR   Ensembl; ENSSSCT00025006739; ENSSSCP00025002788; ENSSSCG00025004969.
DR   Ensembl; ENSSSCT00030039217; ENSSSCP00030018057; ENSSSCG00030028035.
DR   Ensembl; ENSSSCT00035098999; ENSSSCP00035041870; ENSSSCG00035073083.
DR   Ensembl; ENSSSCT00040078450; ENSSSCP00040033836; ENSSSCG00040057801.
DR   Ensembl; ENSSSCT00045057057; ENSSSCP00045039867; ENSSSCG00045033311.
DR   Ensembl; ENSSSCT00050043755; ENSSSCP00050018047; ENSSSCG00050032579.
DR   Ensembl; ENSSSCT00055004386; ENSSSCP00055003368; ENSSSCG00055002313.
DR   Ensembl; ENSSSCT00060069080; ENSSSCP00060029719; ENSSSCG00060050777.
DR   Ensembl; ENSSSCT00065037789; ENSSSCP00065015918; ENSSSCG00065028024.
DR   Ensembl; ENSSSCT00070050221; ENSSSCP00070042436; ENSSSCG00070025122.
DR   GeneID; 100524676; -.
DR   KEGG; ssc:100524676; -.
DR   CTD; 6391; -.
DR   VGNC; VGNC:98852; SDHC.
DR   eggNOG; KOG0449; Eukaryota.
DR   GeneTree; ENSGT00390000000566; -.
DR   HOGENOM; CLU_094691_1_1_1; -.
DR   InParanoid; D0VWV4; -.
DR   OMA; IPGGIPC; -.
DR   OrthoDB; 1443173at2759; -.
DR   TreeFam; TF313317; -.
DR   UniPathway; UPA00223; -.
DR   EvolutionaryTrace; D0VWV4; -.
DR   Proteomes; UP000008227; Chromosome 4.
DR   Proteomes; UP000314985; Chromosome 4.
DR   Bgee; ENSSSCG00000030318; Expressed in metanephros cortex and 45 other tissues.
DR   ExpressionAtlas; D0VWV4; baseline and differential.
DR   Genevisible; D0VWV4; SS.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IDA:UniProtKB.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IDA: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; IPR018495; Succ_DH_cyt_bsu_CS.
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.
DR   PROSITE; PS01000; SDH_CYT_1; 1.
DR   PROSITE; PS01001; SDH_CYT_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transit peptide; Transmembrane; Transmembrane helix; Transport;
KW   Tricarboxylic acid cycle.
FT   TRANSIT         1..29
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           30..169
FT                   /note="Succinate dehydrogenase cytochrome b560 subunit,
FT                   mitochondrial"
FT                   /id="PRO_0000391750"
FT   TOPO_DOM        30..62
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        63..92
FT                   /note="Helical"
FT   TOPO_DOM        93..112
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        113..137
FT                   /note="Helical"
FT   TOPO_DOM        138..144
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        145..166
FT                   /note="Helical"
FT   TOPO_DOM        167..169
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
FT   BINDING         127
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:0000269|PubMed:15989954,
FT                   ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0"
FT   HELIX           34..46
FT                   /evidence="ECO:0007829|PDB:1ZOY"
FT   TURN            47..49
FT                   /evidence="ECO:0007829|PDB:3AEA"
FT   TURN            56..58
FT                   /evidence="ECO:0007829|PDB:1ZOY"
FT   HELIX           63..91
FT                   /evidence="ECO:0007829|PDB:1ZOY"
FT   STRAND          92..94
FT                   /evidence="ECO:0007829|PDB:3AEF"
FT   HELIX           96..104
FT                   /evidence="ECO:0007829|PDB:1ZOY"
FT   TURN            105..107
FT                   /evidence="ECO:0007829|PDB:1ZOY"
FT   HELIX           110..138
FT                   /evidence="ECO:0007829|PDB:1ZOY"
FT   TURN            139..142
FT                   /evidence="ECO:0007829|PDB:3SFD"
FT   HELIX           145..166
FT                   /evidence="ECO:0007829|PDB:1ZOY"
SQ   SEQUENCE   169 AA;  18518 MW;  42EB611C1DCDF0A5 CRC64;
     MAALLLRHVG RHCLRAHLSP QLCIRNAVPL GTTAKEEMER FWNKNLGSNR PLSPHITIYR
     WSLPMAMSIC HRGTGIALSA GVSLFGLSAL LLPGNFESHL ELVKSLCLGP TLIYTAKFGI
     VFPLMYHTWN GIRHLIWDLG KGLTIPQLTQ SGVVVLILTV LSSVGLAAM
 
 
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