DHSD_CHOCR
ID DHSD_CHOCR Reviewed; 84 AA.
AC P54323;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Succinate dehydrogenase membrane anchor subunit;
DE AltName: Full=Succinate dehydrogenase, subunit IV;
GN Name=SDH4; Synonyms=SDHD;
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].
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 {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: Part of an enzyme complex containing four subunits: a
CC flavoprotein, an iron-sulfur protein, plus two membrane-anchoring
CC proteins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
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DR EMBL; Z47547; CAA87621.1; -; Genomic_DNA.
DR PIR; S59105; S59105.
DR RefSeq; NP_062495.1; NC_001677.2.
DR AlphaFoldDB; P54323; -.
DR SMR; P54323; -.
DR GeneID; 809388; -.
DR KEGG; ccp:ChcroMp16; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 SUPFAM; SSF81343; SSF81343; 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..84
FT /note="Succinate dehydrogenase membrane anchor subunit"
FT /id="PRO_0000158711"
FT TOPO_DOM 1..3
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..31
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..58
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..84
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT BINDING 37
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"
FT BINDING 49
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
SQ SEQUENCE 84 AA; 9906 MW; 321516D59F2C71BC CRC64;
MITFQWLIVR VVALFISLTI LIDIEMFVVM LSFLIIHISI GLKAIIHDYI HFQKIKLMLL
ILLRVSAIEI SRSFRTFYII IKNT
