CY1_BOVIN
ID CY1_BOVIN Reviewed; 325 AA.
AC P00125; Q2TBM2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 168.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 85-325.
RC TISSUE=Heart;
RX PubMed=6286615; DOI=10.1016/s0021-9258(18)34074-2;
RA Wakabayashi S., Matsubara H., Kim C.H., King T.E.;
RT "Structural studies of bovine heart cytochrome c1.";
RL J. Biol. Chem. 257:9335-9344(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-194.
RC STRAIN=Holstein-Friesian;
RA Band M., Ron M.;
RT "Partial genomic sequence of the bovine cytochrome c1 gene.";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 85-321.
RX PubMed=9204897; DOI=10.1126/science.277.5322.60;
RA Xia D., Yu C.A., Kim H., Xia J.Z., Kachurin A.M., Zhang L., Yu L.,
RA Deisenhofer J.;
RT "Crystal structure of the cytochrome bc1 complex from bovine heart
RT mitochondria.";
RL Science 277:60-66(1997).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 85-321 IN COMPLEX WITH HEME.
RX PubMed=9651245; DOI=10.1126/science.281.5373.64;
RA Iwata S., Lee J.W., Okada K., Lee J.K., Iwata M., Rasmussen B., Link T.A.,
RA Ramaswamy S., Jap B.K.;
RT "Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1
RT complex.";
RL Science 281:64-71(1998).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
RX PubMed=12269811; DOI=10.1021/bi026252p;
RA Gao X., Wen X., Yu C., Esser L., Tsao S., Quinn B., Zhang L., Yu L.,
RA Xia D.;
RT "The crystal structure of mitochondrial cytochrome bc1 in complex with
RT famoxadone: the role of aromatic-aromatic interaction in inhibition.";
RL Biochemistry 41:11692-11702(2002).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS).
RX PubMed=15312779; DOI=10.1016/j.jmb.2004.05.065;
RA Esser L., Quinn B., Li Y.F., Zhang M., Elberry M., Yu L., Yu C.A., Xia D.;
RT "Crystallographic studies of quinol oxidation site inhibitors: a modified
RT classification of inhibitors for the cytochrome bc(1) complex.";
RL J. Mol. Biol. 341:281-302(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=16024040; DOI=10.1016/j.jmb.2005.05.053;
RA Huang L.S., Cobessi D., Tung E.Y., Berry E.A.;
RT "Binding of the respiratory chain inhibitor antimycin to the mitochondrial
RT bc1 complex: a new crystal structure reveals an altered intramolecular
RT hydrogen-bonding pattern.";
RL J. Mol. Biol. 351:573-597(2005).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS).
RX PubMed=16924113; DOI=10.1073/pnas.0601149103;
RA Esser L., Gong X., Yang S., Yu L., Yu C.A., Xia D.;
RT "Surface-modulated motion switch: capture and release of iron-sulfur
RT protein in the cytochrome bc1 complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13045-13050(2006).
RN [10]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.10 ANGSTROMS), AND SUBUNIT.
RX PubMed=27830641; DOI=10.7554/elife.21290;
RA Sousa J.S., Mills D.J., Vonck J., Kuehlbrandt W.;
RT "Functional asymmetry and electron flow in the bovine respirasome.";
RL Elife 5:0-0(2016).
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:0000269|PubMed:9651245};
CC Note=Binds 1 heme c group covalently per subunit.
CC {ECO:0000269|PubMed:9651245};
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 (PubMed:9651245). 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:27830641). {ECO:0000269|PubMed:27830641,
CC ECO:0000269|PubMed:9651245}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P07143}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P07143}.
CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
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DR EMBL; BC109917; AAI09918.1; -; mRNA.
DR EMBL; U97172; AAB57834.1; -; Genomic_DNA.
DR PIR; A00118; CCBO1.
DR RefSeq; NP_001033179.1; NM_001038090.2.
DR PDB; 1BCC; X-ray; 3.16 A; D=85-325.
DR PDB; 1BE3; X-ray; 3.00 A; D=85-325.
DR PDB; 1BGY; X-ray; 3.00 A; D/P=85-325.
DR PDB; 1L0L; X-ray; 2.35 A; D=85-325.
DR PDB; 1L0N; X-ray; 2.60 A; D=85-325.
DR PDB; 1NTK; X-ray; 2.60 A; D=85-325.
DR PDB; 1NTM; X-ray; 2.40 A; D=85-325.
DR PDB; 1NTZ; X-ray; 2.60 A; D=85-325.
DR PDB; 1NU1; X-ray; 3.20 A; D=85-325.
DR PDB; 1PP9; X-ray; 2.10 A; D/Q=85-325.
DR PDB; 1PPJ; X-ray; 2.10 A; D/Q=85-325.
DR PDB; 1QCR; X-ray; 2.70 A; D=251-325.
DR PDB; 1SQB; X-ray; 2.69 A; D=85-325.
DR PDB; 1SQP; X-ray; 2.70 A; D=85-325.
DR PDB; 1SQQ; X-ray; 3.00 A; D=85-325.
DR PDB; 1SQV; X-ray; 2.85 A; D=85-325.
DR PDB; 1SQX; X-ray; 2.60 A; D=85-325.
DR PDB; 2A06; X-ray; 2.10 A; D/Q=85-325.
DR PDB; 2BCC; X-ray; 3.50 A; D=85-325.
DR PDB; 2FYU; X-ray; 2.26 A; D=85-325.
DR PDB; 2YBB; EM; 19.00 A; D/d=85-325.
DR PDB; 3BCC; X-ray; 3.70 A; D=85-325.
DR PDB; 4D6T; X-ray; 3.57 A; D/Q=61-325.
DR PDB; 4D6U; X-ray; 4.09 A; D/Q=1-325.
DR PDB; 5GPN; EM; 5.40 A; D/P=85-325.
DR PDB; 5KLV; X-ray; 2.65 A; D=85-325.
DR PDB; 5LUF; EM; 9.10 A; d/p=85-325.
DR PDB; 5NMI; X-ray; 3.50 A; D/Q=86-325.
DR PDB; 5OKD; X-ray; 3.10 A; D=1-325.
DR PDB; 6FO0; EM; 4.10 A; D/Q=1-325.
DR PDB; 6FO2; EM; 4.40 A; D/Q=1-325.
DR PDB; 6FO6; EM; 4.10 A; D/Q=1-325.
DR PDB; 6HAW; X-ray; 3.45 A; D=86-324.
DR PDB; 6NHG; X-ray; 2.80 A; D=85-325.
DR PDB; 6XVF; X-ray; 3.50 A; D=86-324.
DR PDB; 6ZFS; X-ray; 3.50 A; D=86-324.
DR PDB; 6ZFT; X-ray; 3.30 A; D=86-324.
DR PDB; 6ZFU; X-ray; 3.50 A; D=86-324.
DR PDBsum; 1BCC; -.
DR PDBsum; 1BE3; -.
DR PDBsum; 1BGY; -.
DR PDBsum; 1L0L; -.
DR PDBsum; 1L0N; -.
DR PDBsum; 1NTK; -.
DR PDBsum; 1NTM; -.
DR PDBsum; 1NTZ; -.
DR PDBsum; 1NU1; -.
DR PDBsum; 1PP9; -.
DR PDBsum; 1PPJ; -.
DR PDBsum; 1QCR; -.
DR PDBsum; 1SQB; -.
DR PDBsum; 1SQP; -.
DR PDBsum; 1SQQ; -.
DR PDBsum; 1SQV; -.
DR PDBsum; 1SQX; -.
DR PDBsum; 2A06; -.
DR PDBsum; 2BCC; -.
DR PDBsum; 2FYU; -.
DR PDBsum; 2YBB; -.
DR PDBsum; 3BCC; -.
DR PDBsum; 4D6T; -.
DR PDBsum; 4D6U; -.
DR PDBsum; 5GPN; -.
DR PDBsum; 5KLV; -.
DR PDBsum; 5LUF; -.
DR PDBsum; 5NMI; -.
DR PDBsum; 5OKD; -.
DR PDBsum; 6FO0; -.
DR PDBsum; 6FO2; -.
DR PDBsum; 6FO6; -.
DR PDBsum; 6HAW; -.
DR PDBsum; 6NHG; -.
DR PDBsum; 6XVF; -.
DR PDBsum; 6ZFS; -.
DR PDBsum; 6ZFT; -.
DR PDBsum; 6ZFU; -.
DR AlphaFoldDB; P00125; -.
DR SMR; P00125; -.
DR CORUM; P00125; -.
DR DIP; DIP-38976N; -.
DR IntAct; P00125; 10.
DR STRING; 9913.ENSBTAP00000016224; -.
DR TCDB; 3.D.3.2.1; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
DR PaxDb; P00125; -.
DR PeptideAtlas; P00125; -.
DR PRIDE; P00125; -.
DR Ensembl; ENSBTAT00000016224; ENSBTAP00000016224; ENSBTAG00000012232.
DR GeneID; 512500; -.
DR KEGG; bta:512500; -.
DR CTD; 1537; -.
DR VEuPathDB; HostDB:ENSBTAG00000012232; -.
DR VGNC; VGNC:50266; CYC1.
DR eggNOG; KOG3052; Eukaryota.
DR GeneTree; ENSGT00390000012445; -.
DR HOGENOM; CLU_040334_1_0_1; -.
DR InParanoid; P00125; -.
DR OMA; VWVKKFK; -.
DR OrthoDB; 923710at2759; -.
DR TreeFam; TF314799; -.
DR EvolutionaryTrace; P00125; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000012232; Expressed in cardiac ventricle and 106 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:AgBase.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISS:AgBase.
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:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
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; Direct protein sequencing; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Respiratory chain; Transit peptide; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..84
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:6286615"
FT CHAIN 85..325
FT /note="Cytochrome c1, heme protein, mitochondrial"
FT /id="PRO_0000108416"
FT TOPO_DOM 85..281
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:9651245"
FT TRANSMEM 282..315
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:9651245"
FT TOPO_DOM 316..325
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:9651245"
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:0000269|PubMed:9651245,
FT ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY"
FT BINDING 124
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9651245,
FT ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY"
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:0000269|PubMed:9651245,
FT ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY"
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:0000269|PubMed:9651245,
FT ECO:0007744|PDB:1BE3"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1L0L"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:1NTK"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:1PP9"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 142..150
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:1PP9"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:1L0L"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:2FYU"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:1PP9"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:2FYU"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:1SQQ"
FT HELIX 207..215
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:2FYU"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:2FYU"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:2FYU"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:1SQP"
FT HELIX 263..278
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 282..315
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:1PP9"
SQ SEQUENCE 325 AA; 35297 MW; 588ED1DEFEAABD6D CRC64;
MAAAAATLRG AMVGPRGAGL PGARARGLLC GARPGQLPLR TPQAVSLSSK SGLSRGRKVI
LSALGMLAAG GAGLAVALHS AVSASDLELH PPSYPWSHRG LLSSLDHTSI RRGFQVYKQV
CSSCHSMDYV AYRHLVGVCY TEDEAKALAE EVEVQDGPNE DGEMFMRPGK LSDYFPKPYP
NPEAARAANN GALPPDLSYI VRARHGGEDY VFSLLTGYCE PPTGVSLREG LYFNPYFPGQ
AIGMAPPIYN EVLEFDDGTP ATMSQVAKDV CTFLRWAAEP EHDHRKRMGL KMLLMMGLLL
PLVYAMKRHK WSVLKSRKLA YRPPK
