CY12_SOLTU
ID CY12_SOLTU Reviewed; 260 AA.
AC P29610;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Cytochrome c1-2, heme protein, mitochondrial;
DE EC=7.1.1.8;
DE AltName: Full=Clone PC18I;
DE AltName: Full=Complex III subunit 4-2;
DE AltName: Full=Complex III subunit IV-2;
DE AltName: Full=Cytochrome b-c1 complex subunit 4-2;
DE AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome c1 subunit 2;
DE Short=Cytochrome c-1-2;
DE Flags: Precursor; Fragment;
GN Name=CYCL;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 18-37.
RC STRAIN=cv. Desiree; TISSUE=Green leaf;
RX PubMed=1310521; DOI=10.1007/bf00279794;
RA Braun H.P., Emmermann M., Kruft V., Schmitz U.K.;
RT "Cytochrome c1 from potato: a protein with a presequence for targeting to
RT the mitochondrial intermembrane space.";
RL Mol. Gen. Genet. 231:217-225(1992).
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:P07143};
CC Note=Binds 1 heme c group covalently per subunit.
CC {ECO:0000250|UniProtKB:P07143};
CC -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC composed of 3 respiratory subunits cytochrome b, cytochrome c1 and
CC Rieske protein, 2 core protein subunits, and additional low-molecular
CC weight protein subunits. The complex exists as an obligatory dimer and
CC forms supercomplexes (SCs) in the inner mitochondrial membrane with
CC cytochrome c oxidase (complex IV, CIV). {ECO:0000250|UniProtKB:P07143}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P07143}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P07143}.
CC -!- TISSUE SPECIFICITY: In all tissues analyzed.
CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
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DR AlphaFoldDB; P29610; -.
DR SMR; P29610; -.
DR STRING; 4113.PGSC0003DMT400052104; -.
DR PRIDE; P29610; -.
DR eggNOG; KOG3052; Eukaryota.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; P29610; baseline.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IBA:GO_Central.
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 Direct protein sequencing; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Respiratory chain; Transit peptide; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT <1..17
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1310521"
FT CHAIN 18..260
FT /note="Cytochrome c1-2, heme protein, mitochondrial"
FT /id="PRO_0000006558"
FT TOPO_DOM 18..221
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P07143"
FT TRANSMEM 222..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..260
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P07143"
FT DOMAIN 43..150
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 56
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07143"
FT BINDING 59
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07143"
FT BINDING 60
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:P07143"
FT BINDING 179
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:P07143"
FT NON_TER 1
SQ SEQUENCE 260 AA; 28592 MW; E39E2B84F3D7591A CRC64;
IGAGVSGLLG FATVASADEA EHGLECPSYP WPHAGILSSY DHASIRRGHQ VYQQVCASCH
SMSLVSYRDL VGVAYTEEEV KAMAAEIEVE DGPNDEGEMF TRPGKLSDRF PQPYPNEAAA
RFANGGAYPP DLSLITKARH NGQNYVFALL TAYRDPPAGV SIREGLHYNP YFPGGAIAMP
KMLNDGAVEY EDGVPATEAQ MGKDVVSFLT WAAEPEMEER KLMGFKWIFV LSLALLQAAY
YRRLRWSVLK SRKLVLDVVN
