CYC1B_ARATH
ID CYC1B_ARATH Reviewed; 307 AA.
AC Q9FKS5; F4KIR8; Q0WL66; Q0WNJ4; Q42065; Q94A63;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Cytochrome c1 2, heme protein, mitochondrial;
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;
GN Name=CYC1-2; OrderedLocusNames=At5g40810; ORFNames=MHK7.4;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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] (ISOFORM 1).
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-87 (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RA Hofte H.;
RT "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [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).
RN [8]
RP SUBCELLULAR LOCATION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18305213; DOI=10.1104/pp.107.111260;
RA Zsigmond L., Rigo G., Szarka A., Szekely G., Oetvoes K., Darula Z.,
RA Medzihradszky K.F., Koncz C., Koncz Z., Szabados L.;
RT "Arabidopsis PPR40 connects abiotic stress responses to mitochondrial
RT electron transport.";
RL Plant Physiol. 146:1721-1737(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, PubMed:18305213). The complex exists as
CC an obligatory dimer and forms supercomplexes (SCs) in the inner
CC mitochondrial membrane with NADH-ubiquinone oxidoreductase (complex I,
CC CI), resulting in different assemblies (supercomplexes SCI(1)III(2) and
CC SCI(2)III(4)) (PubMed:12970493). {ECO:0000269|PubMed:12970493,
CC ECO:0000269|PubMed:18189341, ECO:0000269|PubMed:18305213}.
CC -!- INTERACTION:
CC Q9FKS5; Q33884: CCMFN2; NbExp=4; IntAct=EBI-1777995, EBI-763400;
CC Q9FKS5; P99999: CYCS; Xeno; NbExp=2; IntAct=EBI-1777995, EBI-446479;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:18189341, ECO:0000269|PubMed:18305213}; Single-pass
CC membrane protein {ECO:0000269|PubMed:18189341,
CC ECO:0000269|PubMed:18305213}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FKS5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FKS5-2; Sequence=VSP_054178;
CC -!- PTM: Binds 1 heme c group covalently per subunit. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA81123.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB011477; BAB11343.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94597.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94598.1; -; Genomic_DNA.
DR EMBL; AY050340; AAK91357.1; -; mRNA.
DR EMBL; AY116937; AAM51571.1; -; mRNA.
DR EMBL; AK229445; BAF01305.1; -; mRNA.
DR EMBL; AK230342; BAF02141.1; -; mRNA.
DR EMBL; Z25972; CAA81123.1; ALT_INIT; mRNA.
DR RefSeq; NP_001154756.1; NM_001161284.1. [Q9FKS5-2]
DR RefSeq; NP_198897.1; NM_123446.5. [Q9FKS5-1]
DR AlphaFoldDB; Q9FKS5; -.
DR SMR; Q9FKS5; -.
DR BioGRID; 19332; 14.
DR IntAct; Q9FKS5; 4.
DR MINT; Q9FKS5; -.
DR STRING; 3702.AT5G40810.1; -.
DR PaxDb; Q9FKS5; -.
DR PRIDE; Q9FKS5; -.
DR ProteomicsDB; 220436; -. [Q9FKS5-1]
DR EnsemblPlants; AT5G40810.1; AT5G40810.1; AT5G40810. [Q9FKS5-1]
DR EnsemblPlants; AT5G40810.2; AT5G40810.2; AT5G40810. [Q9FKS5-2]
DR GeneID; 834081; -.
DR Gramene; AT5G40810.1; AT5G40810.1; AT5G40810. [Q9FKS5-1]
DR Gramene; AT5G40810.2; AT5G40810.2; AT5G40810. [Q9FKS5-2]
DR KEGG; ath:AT5G40810; -.
DR Araport; AT5G40810; -.
DR TAIR; locus:2164471; AT5G40810.
DR eggNOG; KOG3052; Eukaryota.
DR HOGENOM; CLU_040334_0_0_1; -.
DR InParanoid; Q9FKS5; -.
DR OMA; VWVKKFK; -.
DR PhylomeDB; Q9FKS5; -.
DR BioCyc; ARA:AT5G40810-MON; -.
DR BioCyc; MetaCyc:MONQT-2771; -.
DR PRO; PR:Q9FKS5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKS5; baseline and differential.
DR Genevisible; Q9FKS5; AT.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009536; C:plastid; 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 Alternative splicing; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Respiratory chain; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..64
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 65..307
FT /note="Cytochrome c1 2, heme protein, mitochondrial"
FT /id="PRO_0000428673"
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..197
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 VAR_SEQ 1..47
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_054178"
FT CONFLICT 83..87
FT /note="ILSSY -> HFSSS (in Ref. 5; CAA81123)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="N -> H (in Ref. 4; BAF01305)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="G -> C (in Ref. 3; AAK91357/AAM51571)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="S -> L (in Ref. 3; AAK91357/AAM51571)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 307 AA; 33690 MW; 3F807D081F788ED3 CRC64;
MVGGGVIRQL LRRKLHSQSV ATPVLSWLSS KKANEDAGSA GLRAFALMGA GITGLLSFST
VASADEAEHG LECPNYPWPH EGILSSYDHA SIRRGHQVYQ QVCASCHSMS LISYRDLVGV
AYTEEEAKAM AAEIEVVDGP NDEGEMFTRP GKLSDRLPEP YSNESAARFA NGGAYPPDLS
LVTKARHNGQ NYVFALLTGY RDPPAGISIR EGLHYNPYFP GGAIAMPKML NDEAVEYEDG
TPATEAQMGK DVVSFLSWAA EPEMEERKLM GFKWIFLLSL ALLQAAYYRR LKWSVLKSRK
LVLDVVN
