CY11_SOLTU
ID CY11_SOLTU Reviewed; 320 AA.
AC P25076; Q41207;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Cytochrome c1-1, heme protein, mitochondrial;
DE EC=7.1.1.8;
DE AltName: Full=Complex III subunit 4-1;
DE AltName: Full=Complex III subunit IV-1;
DE AltName: Full=Cytochrome b-c1 complex subunit 4-1;
DE AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome c1 subunit 1;
DE Short=Cytochrome c-1-1;
DE Flags: Precursor;
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].
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Desiree;
RX PubMed=8221935; DOI=10.1007/bf00351800;
RA Wegener S., Schmitz U.K.;
RT "The presequence of cytochrome c1 from potato mitochondria is encoded on
RT four exons.";
RL Curr. Genet. 24:256-259(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44;
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
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 EMBL; X62124; CAA44055.1; -; mRNA.
DR EMBL; S66866; AAB28813.2; -; Genomic_DNA.
DR PIR; S20014; S20014.
DR RefSeq; NP_001275377.1; NM_001288448.1.
DR AlphaFoldDB; P25076; -.
DR SMR; P25076; -.
DR STRING; 4113.PGSC0003DMT400073387; -.
DR PRIDE; P25076; -.
DR GeneID; 102589911; -.
DR KEGG; sot:102589911; -.
DR eggNOG; KOG3052; Eukaryota.
DR InParanoid; P25076; -.
DR OrthoDB; 923710at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; P25076; baseline and differential.
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:0070469; C:respirasome; IEA:UniProtKB-KW.
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 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 2: Evidence at transcript level;
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..77
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 78..320
FT /note="Cytochrome c1-1, heme protein, mitochondrial"
FT /id="PRO_0000006557"
FT TOPO_DOM 78..280
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P07143"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..320
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P07143"
FT DOMAIN 103..210
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 116
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07143"
FT BINDING 119
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07143"
FT BINDING 120
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 239
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 CONFLICT 88
FT /note="N -> S (in Ref. 2; AAB28813)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="A -> G (in Ref. 2; AAB28813)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 35159 MW; 19E05BF0C9EC78E3 CRC64;
MSLGKKIRIG FDGFGRINRF ITRGAAQRND SKLPSRNDAL KHGLDGLGSA GSKSFRALAA
IGAGVSGLLS FATIAYSDEA EHGLECPNYP WPHEGILSSY DHASIRRGHQ VYQQVCASCH
SMSLISYRDL VGVAYTEEET KAMAAEIEVV DGPNDEGEMF TRPGKLSDRF PQPYANEAAA
RFANGGAYPP DLSLITKARH NGQNYVFALL TAYRDPPAGV SIREGLHYNP YFPGGAIAMP
KMLNDGAVEY EDGIPATEAQ MGKDVVSFLS WAAEPEMEER KLMGFKWIFV LSLALLQAAY
YRRLRWSVLK SRKLVLDVVN
