ID   C560_MARPO              Reviewed;         137 AA.
AC   P35721;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Succinate dehydrogenase cytochrome b560 subunit;
DE   AltName: Full=Succinate dehydrogenase, subunit III;
GN   Name=SDH3; Synonyms=SDHC, YMF24;
OS   Marchantia polymorpha (Liverwort) (Marchantia aquatica).
OG   Mitochondrion.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=3197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1731062; DOI=10.1016/0022-2836(92)90708-r;
RA   Oda K., Yamato K., Ohta E., Nakamura Y., Takemura M., Nozato N., Akashi K.,
RA   Kanegae T., Ogura Y., Kohchi T., Ohyama K.;
RT   "Gene organization deduced from the complete sequence of liverwort
RT   Marchantia polymorpha mitochondrial DNA. A primitive form of plant
RT   mitochondrial genome.";
RL   J. Mol. Biol. 223:1-7(1992).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M68929; AAC09406.1; -; Genomic_DNA.
DR   PIR; S25968; S25968.
DR   RefSeq; NP_054409.1; NC_001660.1.
DR   AlphaFoldDB; P35721; -.
DR   SMR; P35721; -.
DR   GeneID; 2948414; -.
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..137
FT                   /note="Succinate dehydrogenase cytochrome b560 subunit"
FT                   /id="PRO_0000203519"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         85
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   137 AA;  16173 MW;  812131C4325A82C8 CRC64;
     MKINRPLSPH LTIYKPQLTS TFSIFHRISG AFLATMVLFS ILFFKIGDLS LTFYHFYQYF
     FFLTFYLNWF IISLVNFTLL ALCYHMSNGV RHLLWDLGFF LELSKVYTSG IIMLFCAAFL
     ALLNIIRQHW SNGQIPY