CYC1A_ARATH
ID CYC1A_ARATH Reviewed; 307 AA.
AC Q9LK29; Q8LA08; Q940N2;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cytochrome c1 1, heme protein, mitochondrial;
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=CYC1-1; OrderedLocusNames=At3g27240; ORFNames=K17E12.6;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBUNIT.
RX PubMed=12970493; DOI=10.1104/pp.103.024620;
RA Eubel H., Jansch L., Braun H.P.;
RT "New insights into the respiratory chain of plant mitochondria.
RT Supercomplexes and a unique composition of complex II.";
RL Plant Physiol. 133:274-286(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [7]
RP SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, REVIEW,
RP AND NOMENCLATURE.
RX PubMed=18189341; DOI=10.1021/pr700595p;
RA Meyer E.H., Taylor N.L., Millar A.H.;
RT "Resolving and identifying protein components of plant mitochondrial
RT respiratory complexes using three dimensions of gel electrophoresis.";
RL J. Proteome Res. 7:786-794(2008).
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 -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC composed of 10 subunits. The complex is composed of 3 respiratory
CC subunits cytochrome b (MT-CYB), cytochrome c1 (CYC1-1 or CYC1-2) and
CC Rieske protein (UCR1-1 or UCR1-2), 2 core protein subunits MPPalpha1
CC (or MPPalpha2) and MPPB, and 5 low-molecular weight protein subunits
CC QCR7-1 (or QCR7-2), UCRQ-1 (or UCRQ-2), QCR9, UCRY and probably QCR6-1
CC (or QCR6-2) (PubMed:18189341). 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), resulting
CC in different assemblies (supercomplexes SCI(1)III(2) and SCI(2)III(4))
CC (PubMed:12970493). {ECO:0000269|PubMed:12970493,
CC ECO:0000269|PubMed:18189341}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:18189341}; Single-pass membrane protein
CC {ECO:0000269|PubMed:18189341}.
CC -!- PTM: Binds 1 heme c group covalently per subunit. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
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DR EMBL; AP000381; BAB02119.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77282.1; -; Genomic_DNA.
DR EMBL; AF458338; AAL51110.1; -; mRNA.
DR EMBL; AY054246; AAL06905.1; -; mRNA.
DR EMBL; AY088099; AAM65645.1; -; mRNA.
DR RefSeq; NP_189360.1; NM_113638.3.
DR AlphaFoldDB; Q9LK29; -.
DR SMR; Q9LK29; -.
DR BioGRID; 7673; 14.
DR IntAct; Q9LK29; 3.
DR STRING; 3702.AT3G27240.1; -.
DR MetOSite; Q9LK29; -.
DR PaxDb; Q9LK29; -.
DR PRIDE; Q9LK29; -.
DR ProteomicsDB; 222665; -.
DR EnsemblPlants; AT3G27240.1; AT3G27240.1; AT3G27240.
DR GeneID; 822343; -.
DR Gramene; AT3G27240.1; AT3G27240.1; AT3G27240.
DR KEGG; ath:AT3G27240; -.
DR Araport; AT3G27240; -.
DR TAIR; locus:2086553; AT3G27240.
DR eggNOG; KOG3052; Eukaryota.
DR HOGENOM; CLU_040334_0_0_1; -.
DR InParanoid; Q9LK29; -.
DR OMA; VCVFLKW; -.
DR OrthoDB; 923710at2759; -.
DR PhylomeDB; Q9LK29; -.
DR BioCyc; ARA:AT3G27240-MON; -.
DR BioCyc; MetaCyc:AT3G27240-MON; -.
DR PRO; PR:Q9LK29; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LK29; baseline and differential.
DR Genevisible; Q9LK29; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..64
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 65..307
FT /note="Cytochrome c1 1, heme protein, mitochondrial"
FT /id="PRO_0000428672"
FT TOPO_DOM 65..270
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P07143"
FT TRANSMEM 271..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..307
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P07143"
FT DOMAIN 90..246
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 103
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 106
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 107
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:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 226
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:0000255|PROSITE-ProRule:PRU00433"
FT CONFLICT 53
FT /note="T -> S (in Ref. 4; AAM65645)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="T -> A (in Ref. 3; AAL51110/AAL06905)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 307 AA; 33650 MW; D041537B37D84C03 CRC64;
MVGGGVIQQI LRRKLHSQSL ATPVLSWFSS KKAHEDAGSS GVRALALLGA GVTGLLSFST
VASADEAEHG LESPEYPWPH DGILSSYDHA SIRRGHQVYQ QVCASCHSMS LISYRDLVGV
AYTEEEAKAM AAEIEVVDGP NDEGEMFTRP GKLSDRFPQP YANESAARFA NGGAYPPDLS
LITKARHNGP NYVFALLTGY RDPPAGISIR EGLHYNPYFP GGAIAMPKML NDEAVEYEDG
VPATEAQMGK DIVSFLAWAA EPEMEERKLM GFKWIFLLSL ALLQAAYYRR LKWSVLKSRK
LVLDVVN
