ID   C560_CHOCR              Reviewed;         127 AA.
AC   P48934;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Succinate dehydrogenase cytochrome b560 subunit;
DE   AltName: Full=Succinate dehydrogenase, subunit III;
GN   Name=SDH3; Synonyms=SDHC;
OS   Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa).
OG   Mitochondrion.
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC   Gigartinaceae; Chondrus.
OX   NCBI_TaxID=2769;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8821668; DOI=10.1007/bf02221585;
RA   Viehmann S., Richard O., Boyen C., Zetsche K.;
RT   "Genes for two subunits of succinate dehydrogenase form a cluster on the
RT   mitochondrial genome of Rhodophyta.";
RL   Curr. Genet. 29:199-201(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Apices;
RX   PubMed=7616569; DOI=10.1006/jmbi.1995.0392;
RA   Leblanc C., Boyen C., Richard O., Bonnard G., Grienenberger J.-M.,
RA   Kloareg B.;
RT   "Complete sequence of the mitochondrial DNA of the rhodophyte Chondrus
RT   crispus (Gigartinales). Gene content and genome organization.";
RL   J. Mol. Biol. 250:484-495(1995).
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; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC       Note=The heme is bound between the two transmembrane subunits.
CC       {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC   -!- SUBUNIT: Forms part of complex II containing four subunits: a 70 kDa
CC       flavoprotein (FP), a 27 kDa iron-sulfur protein (IP), a cytochrome B
CC       and a membrane-anchoring protein.
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; Z47547; CAA87612.1; -; Genomic_DNA.
DR   PIR; S59115; S59115.
DR   RefSeq; NP_062489.1; NC_001677.2.
DR   AlphaFoldDB; P48934; -.
DR   SMR; P48934; -.
DR   GeneID; 809393; -.
DR   KEGG; ccp:ChcroMp10; -.
DR   UniPathway; UPA00223; -.
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:0045281; C:succinate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000104; F:succinate dehydrogenase activity; IEA:InterPro.
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   PIRSF; PIRSF000178; SDH_cyt_b560; 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   3: Inferred from homology;
KW   Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Transmembrane; Transmembrane helix;
KW   Transport; Tricarboxylic acid cycle.
FT   CHAIN           1..127
FT                   /note="Succinate dehydrogenase cytochrome b560 subunit"
FT                   /id="PRO_0000203517"
FT   TRANSMEM        36..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         88
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_note="ligand shared with second transmembrane
FT                   subunit"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   127 AA;  15054 MW;  D3208940401974BF CRC64;
     MFIKFKISNR PIAPHLLVYT PQLSSLFSIW HRISGVGLAF FFTTFLIFIR IILSSNFACN
     LLTLISFEIS QWIIIYFNLF ILLFLFYHLF NGTRHIIWDF GFLLDIKYLS KFSLFLLVSL
     SLILIFQ