CY1_MOUSE
ID CY1_MOUSE Reviewed; 325 AA.
AC Q9D0M3; Q3TDC5; Q3UAN2; Q63ZW4; Q9DCG0;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Cytochrome c1, heme protein, mitochondrial;
DE EC=7.1.1.8;
DE AltName: Full=Complex III subunit 4;
DE AltName: Full=Complex III subunit IV;
DE AltName: Full=Cytochrome b-c1 complex subunit 4;
DE AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome c1 subunit;
DE Short=Cytochrome c-1;
DE Flags: Precursor;
GN Name=Cyc1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Embryo, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Jaw;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 100-111; 134-202; 269-285 AND 292-307, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP SUBUNIT.
RX PubMed=19026783; DOI=10.1016/j.molcel.2008.10.021;
RA Acin-Perez R., Fernandez-Silva P., Peleato M.L., Perez-Martos A.,
RA Enriquez J.A.;
RT "Respiratory active mitochondrial supercomplexes.";
RL Mol. Cell 32:529-539(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a
CC multisubunit transmembrane complex that is part of the mitochondrial
CC electron transport chain which drives oxidative phosphorylation. The
CC respiratory chain contains 3 multisubunit complexes succinate
CC dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase
CC (complex IV, CIV), that cooperate to transfer electrons derived from
CC NADH and succinate to molecular oxygen, creating an electrochemical
CC gradient over the inner membrane that drives transmembrane transport
CC and the ATP synthase. The cytochrome b-c1 complex catalyzes electron
CC transfer from ubiquinol to cytochrome c, linking this redox reaction to
CC translocation of protons across the mitochondrial inner membrane, with
CC protons being carried across the membrane as hydrogens on the quinol.
CC In the process called Q cycle, 2 protons are consumed from the matrix,
CC 4 protons are released into the intermembrane space and 2 electrons are
CC passed to cytochrome c. Cytochrome c1 is a catalytic core subunit
CC containing a c-type heme. It transfers electrons from the [2Fe-2S]
CC iron-sulfur cluster of the Rieske protein to cytochrome c.
CC {ECO:0000250|UniProtKB:P07143}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2
CC Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:132124; EC=7.1.1.8;
CC Evidence={ECO:0000250|UniProtKB:P07143};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000250|UniProtKB:P00125};
CC Note=Binds 1 heme c group covalently per subunit.
CC {ECO:0000250|UniProtKB:P00125};
CC -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC composed of 11 subunits. The complex is composed of 3 respiratory
CC subunits cytochrome b, cytochrome c1 and Rieske protein UQCRFS1, 2 core
CC protein subunits UQCRC1/QCR1 and UQCRC2/QCR2, and 6 low-molecular
CC weight protein subunits UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8,
CC UQCR10/QCR9, UQCR11/QCR10 and subunit 9, the cleavage product of Rieske
CC protein UQCRFS1 (By similarity). The complex exists as an obligatory
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC cytochrome c oxidase (complex IV, CIV), resulting in different
CC assemblies (supercomplex SCI(1)III(2)IV(1) and megacomplex
CC MCI(2)III(2)IV(2)) (PubMed:19026783). {ECO:0000250|UniProtKB:P00125,
CC ECO:0000269|PubMed:19026783}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P07143}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P07143}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D0M3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D0M3-2; Sequence=VSP_025056;
CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH82790.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK002815; BAB22380.1; -; mRNA.
DR EMBL; AK011288; BAB27518.1; -; mRNA.
DR EMBL; AK151299; BAE30282.1; -; mRNA.
DR EMBL; AK170272; BAE41677.1; -; mRNA.
DR EMBL; BC005620; AAH05620.1; -; mRNA.
DR EMBL; BC082790; AAH82790.1; ALT_INIT; mRNA.
DR CCDS; CCDS27567.1; -. [Q9D0M3-1]
DR RefSeq; NP_079843.1; NM_025567.2. [Q9D0M3-1]
DR PDB; 7O37; EM; 3.20 A; D/O=85-325.
DR PDB; 7O3C; EM; 3.30 A; D/O=85-325.
DR PDB; 7O3E; EM; 3.60 A; D/O=85-325.
DR PDB; 7O3H; EM; 2.60 A; D/O=85-325.
DR PDBsum; 7O37; -.
DR PDBsum; 7O3C; -.
DR PDBsum; 7O3E; -.
DR PDBsum; 7O3H; -.
DR AlphaFoldDB; Q9D0M3; -.
DR SMR; Q9D0M3; -.
DR BioGRID; 211479; 81.
DR ComplexPortal; CPX-563; Mitochondrial respiratory chain complex III.
DR CORUM; Q9D0M3; -.
DR IntAct; Q9D0M3; 16.
DR MINT; Q9D0M3; -.
DR STRING; 10090.ENSMUSP00000023210; -.
DR iPTMnet; Q9D0M3; -.
DR PhosphoSitePlus; Q9D0M3; -.
DR SwissPalm; Q9D0M3; -.
DR EPD; Q9D0M3; -.
DR jPOST; Q9D0M3; -.
DR MaxQB; Q9D0M3; -.
DR PaxDb; Q9D0M3; -.
DR PeptideAtlas; Q9D0M3; -.
DR PRIDE; Q9D0M3; -.
DR ProteomicsDB; 283990; -. [Q9D0M3-1]
DR ProteomicsDB; 283991; -. [Q9D0M3-2]
DR TopDownProteomics; Q9D0M3-1; -. [Q9D0M3-1]
DR Antibodypedia; 810; 401 antibodies from 33 providers.
DR DNASU; 66445; -.
DR Ensembl; ENSMUST00000023210; ENSMUSP00000023210; ENSMUSG00000022551. [Q9D0M3-1]
DR GeneID; 66445; -.
DR KEGG; mmu:66445; -.
DR UCSC; uc007wjs.1; mouse. [Q9D0M3-1]
DR CTD; 1537; -.
DR MGI; MGI:1913695; Cyc1.
DR VEuPathDB; HostDB:ENSMUSG00000022551; -.
DR eggNOG; KOG3052; Eukaryota.
DR GeneTree; ENSGT00390000012445; -.
DR HOGENOM; CLU_040334_1_0_1; -.
DR InParanoid; Q9D0M3; -.
DR OMA; VWVKKFK; -.
DR OrthoDB; 923710at2759; -.
DR PhylomeDB; Q9D0M3; -.
DR TreeFam; TF314799; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR BioGRID-ORCS; 66445; 28 hits in 78 CRISPR screens.
DR ChiTaRS; Cyc1; mouse.
DR PRO; PR:Q9D0M3; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9D0M3; protein.
DR Bgee; ENSMUSG00000022551; Expressed in ileal epithelium and 266 other tissues.
DR ExpressionAtlas; Q9D0M3; baseline and differential.
DR Genevisible; Q9D0M3; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0045333; P:cellular respiration; IC:ComplexPortal.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR GO; GO:0033762; P:response to glucagon; ISO:MGI.
DR Gene3D; 1.10.760.10; -; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR002326; Cyt_c1.
DR InterPro; IPR021157; Cyt_c1_TM_anchor_C.
DR PANTHER; PTHR10266; PTHR10266; 1.
DR Pfam; PF02167; Cytochrom_C1; 1.
DR PRINTS; PR00603; CYTOCHROMEC1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR SUPFAM; SSF81496; SSF81496; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW Transit peptide; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..84
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 85..325
FT /note="Cytochrome c1, heme protein, mitochondrial"
FT /id="PRO_0000006555"
FT TOPO_DOM 85..281
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00125"
FT TRANSMEM 282..315
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00125"
FT TOPO_DOM 316..325
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00125"
FT DOMAIN 108..209
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 121
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P00125"
FT BINDING 124
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P00125"
FT BINDING 125
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P00125"
FT BINDING 244
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P00125"
FT VAR_SEQ 1..59
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_025056"
FT CONFLICT 44
FT /note="A -> R (in Ref. 1; BAB22380)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="K -> R (in Ref. 1; BAB22380)"
FT /evidence="ECO:0000305"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:7O3H"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 142..150
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:7O3H"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:7O3H"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:7O3H"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 208..215
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 263..278
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 282..312
FT /evidence="ECO:0007829|PDB:7O3H"
FT TURN 313..316
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:7O3H"
SQ SEQUENCE 325 AA; 35328 MW; 5F7DD8B78677E9BF CRC64;
MAAAAASLRR TVLGPRGVGL PGASAPGLLG GARSRQLPLR TPQAVSLSSK SGPSRGRKVM
LSALGMLAAG GAGLAVALHS AVSASDLELH PPSYPWSHRG LLSSLDHTSI RRGFQVYKQV
CSSCHSMDYV AYRHLVGVCY TEEEAKALAE EVEVQDGPND DGEMFMRPGK LSDYFPKPYP
NPEAARAANN GALPPDLSYI VRARHGGEDY VFSLLTGYCE PPTGVSLREG LYFNPYFPGQ
AIGMAPPIYT EVLEYDDGTP ATMSQVAKDV ATFLRWASEP EHDHRKRMGL KMLLMMGLLL
PLTYAMKRHK WSVLKSRKLA YRPPK
