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Protein

Succinate dehydrogenase cytochrome b560 subunit, mitochondrial

Gene

SDHC

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).1 Publication

Cofactori

hemeNote: The heme is bound between the two transmembrane subunits SDHC and SDHD.

Pathwayi: tricarboxylic acid cycle

This protein is involved in the pathway tricarboxylic acid cycle, which is part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi127 – 1271Iron (heme axial ligand); shared with SDHD

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport, Tricarboxylic acid cycle

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiR-SSC-71403. Citric acid cycle (TCA cycle).
UniPathwayiUPA00223.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
Alternative name(s):
Succinate-ubiquinone oxidoreductase cytochrome B large subunit
Short name:
CYBL
Gene namesi
Name:SDHC
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 4

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini30 – 6233Mitochondrial matrixCuratedAdd
BLAST
Transmembranei63 – 9230HelicalAdd
BLAST
Topological domaini93 – 11220Mitochondrial intermembraneCuratedAdd
BLAST
Transmembranei113 – 13725HelicalAdd
BLAST
Topological domaini138 – 1447Mitochondrial matrixCurated
Transmembranei145 – 16622HelicalAdd
BLAST
Topological domaini167 – 1693Mitochondrial intermembraneCurated

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2366564.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2929MitochondrionBy similarityAdd
BLAST
Chaini30 – 169140Succinate dehydrogenase cytochrome b560 subunit, mitochondrialPRO_0000391750Add
BLAST

Proteomic databases

PaxDbiD0VWV4.

Expressioni

Tissue specificityi

Detected in heart muscle (at protein level).1 Publication

Gene expression databases

GenevisibleiD0VWV4. SS.

Interactioni

Subunit structurei

Component of complex II composed of four subunits: the flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a cytochrome b560 composed of SDHC and SDHD.1 Publication

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000027481.

Structurei

Secondary structure

1
169
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi34 – 4613Combined sources
Turni47 – 493Combined sources
Turni56 – 583Combined sources
Helixi63 – 9129Combined sources
Beta strandi92 – 943Combined sources
Helixi96 – 1049Combined sources
Turni105 – 1073Combined sources
Helixi110 – 13829Combined sources
Turni139 – 1424Combined sources
Helixi145 – 16622Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZOYX-ray2.40C30-169[»]
1ZP0X-ray3.50C30-169[»]
3ABVX-ray3.24C30-169[»]
3AE1X-ray3.14C30-169[»]
3AE2X-ray3.10C30-169[»]
3AE3X-ray3.35C30-169[»]
3AE4X-ray2.91C30-169[»]
3AE5X-ray3.41C30-169[»]
3AE6X-ray3.40C30-169[»]
3AE7X-ray3.62C30-169[»]
3AE8X-ray3.40C30-169[»]
3AE9X-ray3.31C30-169[»]
3AEAX-ray3.39C30-169[»]
3AEBX-ray3.00C30-169[»]
3AECX-ray3.61C30-169[»]
3AEDX-ray3.52C30-169[»]
3AEEX-ray3.22C30-169[»]
3AEFX-ray2.80C30-169[»]
3AEGX-ray3.27C30-169[»]
3SFDX-ray2.61C30-169[»]
3SFEX-ray2.81C30-169[»]
4YTPX-ray3.10C1-169[»]
4YXDX-ray3.00C1-169[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiD0VWV4.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome b560 family.Curated

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0449. Eukaryota.
COG2009. LUCA.
GeneTreeiENSGT00390000000566.
InParanoidiD0VWV4.
KOiK00236.
OMAiFIAFDLA.
OrthoDBiEOG7SV0WV.
TreeFamiTF313317.

Family and domain databases

InterProiIPR018495. Succ_DH_cyt_bsu_CS.
IPR014314. Succ_DH_cytb556.
IPR000701. Succ_DH_Fumarate_Rdtase_TM-su.
[Graphical view]
PfamiPF01127. Sdh_cyt. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02970. succ_dehyd_cytB. 1 hit.
PROSITEiPS01000. SDH_CYT_1. 1 hit.
PS01001. SDH_CYT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

D0VWV4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALLLRHVG RHCLRAHLSP QLCIRNAVPL GTTAKEEMER FWNKNLGSNR
60 70 80 90 100
PLSPHITIYR WSLPMAMSIC HRGTGIALSA GVSLFGLSAL LLPGNFESHL
110 120 130 140 150
ELVKSLCLGP TLIYTAKFGI VFPLMYHTWN GIRHLIWDLG KGLTIPQLTQ
160
SGVVVLILTV LSSVGLAAM
Length:169
Mass (Da):18,518
Last modified:March 2, 2010 - v2
Checksum:i42EB611C1DCDF0A5
GO

Sequence databases

RefSeqiXP_003125707.2. XM_003125659.5.
UniGeneiSsc.23817.

Genome annotation databases

EnsembliENSSSCT00000029845; ENSSSCP00000027481; ENSSSCG00000030318.
GeneIDi100524676.
KEGGissc:100524676.

Cross-referencesi

Sequence databases

RefSeqiXP_003125707.2. XM_003125659.5.
UniGeneiSsc.23817.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZOYX-ray2.40C30-169[»]
1ZP0X-ray3.50C30-169[»]
3ABVX-ray3.24C30-169[»]
3AE1X-ray3.14C30-169[»]
3AE2X-ray3.10C30-169[»]
3AE3X-ray3.35C30-169[»]
3AE4X-ray2.91C30-169[»]
3AE5X-ray3.41C30-169[»]
3AE6X-ray3.40C30-169[»]
3AE7X-ray3.62C30-169[»]
3AE8X-ray3.40C30-169[»]
3AE9X-ray3.31C30-169[»]
3AEAX-ray3.39C30-169[»]
3AEBX-ray3.00C30-169[»]
3AECX-ray3.61C30-169[»]
3AEDX-ray3.52C30-169[»]
3AEEX-ray3.22C30-169[»]
3AEFX-ray2.80C30-169[»]
3AEGX-ray3.27C30-169[»]
3SFDX-ray2.61C30-169[»]
3SFEX-ray2.81C30-169[»]
4YTPX-ray3.10C1-169[»]
4YXDX-ray3.00C1-169[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000027481.

Chemistry

ChEMBLiCHEMBL2366564.

Proteomic databases

PaxDbiD0VWV4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000029845; ENSSSCP00000027481; ENSSSCG00000030318.
GeneIDi100524676.
KEGGissc:100524676.

Organism-specific databases

CTDi6391.

Phylogenomic databases

eggNOGiKOG0449. Eukaryota.
COG2009. LUCA.
GeneTreeiENSGT00390000000566.
InParanoidiD0VWV4.
KOiK00236.
OMAiFIAFDLA.
OrthoDBiEOG7SV0WV.
TreeFamiTF313317.

Enzyme and pathway databases

UniPathwayiUPA00223.
ReactomeiR-SSC-71403. Citric acid cycle (TCA cycle).

Miscellaneous databases

EvolutionaryTraceiD0VWV4.

Gene expression databases

GenevisibleiD0VWV4. SS.

Family and domain databases

InterProiIPR018495. Succ_DH_cyt_bsu_CS.
IPR014314. Succ_DH_cytb556.
IPR000701. Succ_DH_Fumarate_Rdtase_TM-su.
[Graphical view]
PfamiPF01127. Sdh_cyt. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02970. succ_dehyd_cytB. 1 hit.
PROSITEiPS01000. SDH_CYT_1. 1 hit.
PS01001. SDH_CYT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Preliminary molecular characterization and crystallization of mitochondrial respiratory complex II from porcine heart."
    Huo X., Su D., Wang A., Zhai Y., Xu J., Li X., Bartlam M., Sun F., Rao Z.
    FEBS J. 274:1524-1529(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Heart.
  2. "Crystal structure of mitochondrial respiratory membrane protein complex II."
    Sun F., Huo X., Zhai Y., Wang A., Xu J., Su D., Bartlam M., Rao Z.
    Cell 121:1043-1057(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 30-169 IN COMPLEX WITH HEME, SUBUNIT, MEMBRANE TOPOLOGY.

Entry informationi

Entry nameiC560_PIG
AccessioniPrimary (citable) accession number: D0VWV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: March 2, 2010
Last modified: April 13, 2016
This is version 50 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.