ID A0A5F8HJ05_MONDO Unreviewed; 116 AA. AC A0A5F8HJ05; DT 11-DEC-2019, integrated into UniProtKB/TrEMBL. DT 11-DEC-2019, sequence version 1. DT 14-DEC-2022, entry version 13. DE RecName: Full=Succinate dehydrogenase cytochrome b560 subunit, mitochondrial {ECO:0000256|ARBA:ARBA00014631}; GN Name=SDHC {ECO:0000313|Ensembl:ENSMODP00000059834.1}; OS Monodelphis domestica (Gray short-tailed opossum). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Metatheria; Didelphimorphia; Didelphidae; Monodelphis. OX NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000059834.1, ECO:0000313|Proteomes:UP000002280}; RN [1] {ECO:0000313|Ensembl:ENSMODP00000059834.1, ECO:0000313|Proteomes:UP000002280} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17495919; DOI=10.1038/nature05805; RA Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S., RA Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M., RA Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V., RA Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E., RA Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A., RA Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S., RA Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E., RA Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K., RA VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C., RA Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J., RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P., RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A., RA Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M., RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K., RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J., RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A., RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R., RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L., RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C., RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L., RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F., RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T., RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J., RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S., RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I., RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., RA Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M., RA Samollow P.B., Lander E.S., Lindblad-Toh K.; RT "Genome of the marsupial Monodelphis domestica reveals innovation in non- RT coding sequences."; RL Nature 447:167-177(2007). RN [2] {ECO:0000313|Ensembl:ENSMODP00000059834.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. 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:0000256|ARBA:ARBA00002027}. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|PIRSR:PIRSR000178-1}; CC Note=The heme is bound between the two transmembrane subunits. CC {ECO:0000256|PIRSR:PIRSR000178-1}; 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:0000256|ARBA:ARBA00011758}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the cytochrome b560 family. CC {ECO:0000256|ARBA:ARBA00007244}. 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 AlphaFoldDB; A0A5F8HJ05; -. DR Ensembl; ENSMODT00000053401.1; ENSMODP00000059834.1; ENSMODG00000005031.4. DR GeneTree; ENSGT00390000000566; -. DR Proteomes; UP000002280; Chromosome 2. DR Bgee; ENSMODG00000005031; Expressed in skeletal muscle tissue and 21 other tissues. 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:InterPro. 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; SUCCINATE DEHYDROGENASE CYTOCHROME B560 SUBUNIT; 1. DR Pfam; PF01127; Sdh_cyt; 1. DR PIRSF; PIRSF000178; SDH_cyt_b560; 1. DR SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 1. DR TIGRFAMs; TIGR02970; succ_dehyd_cytB; 1. DR PROSITE; PS01001; SDH_CYT_2; 1. PE 3: Inferred from homology; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000178-1}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000178-1}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR000178-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002280}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1..15 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 16..116 FT /note="Succinate dehydrogenase cytochrome b560 subunit, FT mitochondrial" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5023848941" FT TRANSMEM 25..43 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 96..115 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT BINDING 74 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:0000256|PIRSR:PIRSR000178-1" SQ SEQUENCE 116 AA; 12265 MW; 44736453E7A2895F CRC64; MAALLLSWSL PMAMSICHRA SGIALSAGVS LFGLAALLLP GNFESHVELL KSLSLGPALI HTAKFALVSP LMYHTWNGIR HLTWDLGMGL KIPQLYQSGV VVLALTVLSS IGLAAM //