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Cytochrome c1 2, heme protein, mitochondrial (Complex III subunit 4-2) (Complex III subunit IV-2) (Cytochrome b-c1 complex subunit 4-2) (Ubiquinol-cytochrome-c reductase complex cytochrome c1 subunit 2) (Cytochrome c-1 2)

 CYC1B_ARATH             Reviewed;         307 AA.
Q9FKS5; F4KIR8; Q0WL66; Q0WNJ4; Q42065; Q94A63;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
07-NOV-2018, entry version 107.
RecName: Full=Cytochrome c1 2, heme protein, mitochondrial;
AltName: Full=Complex III subunit 4-2;
AltName: Full=Complex III subunit IV-2;
AltName: Full=Cytochrome b-c1 complex subunit 4-2;
AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome c1 subunit 2;
Short=Cytochrome c-1 2;
Flags: Precursor;
Name=CYC12; OrderedLocusNames=At5g40810; ORFNames=MHK7.4;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9679202; DOI=10.1093/dnares/5.2.131;
Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
features of the regions of 1,381,565 bp covered by twenty one
physically assigned P1 and TAC clones.";
DNA Res. 5:131-145(1998).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-87 (ISOFORM 1).
STRAIN=cv. Columbia; TISSUE=Seedling;
Hofte H.;
"The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
[6]
REVIEW.
PubMed=12970493; DOI=10.1104/pp.103.024620;
Eubel H., Jansch L., Braun H.P.;
"New insights into the respiratory chain of plant mitochondria.
Supercomplexes and a unique composition of complex II.";
Plant Physiol. 133:274-286(2003).
[7]
SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY,
REVIEW, AND NOMENCLATURE.
PubMed=18189341; DOI=10.1021/pr700595p;
Meyer E.H., Taylor N.L., Millar A.H.;
"Resolving and identifying protein components of plant mitochondrial
respiratory complexes using three dimensions of gel electrophoresis.";
J. Proteome Res. 7:786-794(2008).
[8]
SUBCELLULAR LOCATION, SUBUNIT, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=18305213; DOI=10.1104/pp.107.111260;
Zsigmond L., Rigo G., Szarka A., Szekely G., Oetvoes K., Darula Z.,
Medzihradszky K.F., Koncz C., Koncz Z., Szabados L.;
"Arabidopsis PPR40 connects abiotic stress responses to mitochondrial
electron transport.";
Plant Physiol. 146:1721-1737(2008).
-!- FUNCTION: This is the heme-containing component of the cytochrome
b-c1 complex, which accepts electrons from Rieske protein and
transfers electrons to cytochrome c in the mitochondrial
respiratory chain. {ECO:0000250}.
-!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
cytochrome c1 and the Rieske protein. Associated to the
mitochondrial respiratory chain complex III.
{ECO:0000269|PubMed:18189341, ECO:0000269|PubMed:18305213}.
-!- INTERACTION:
Q33884:CCMFN2; NbExp=4; IntAct=EBI-1777995, EBI-763400;
P99999:CYCS (xeno); NbExp=2; IntAct=EBI-1777995, EBI-446479;
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:18189341, ECO:0000269|PubMed:18305213};
Single-pass membrane protein {ECO:0000269|PubMed:18189341,
ECO:0000269|PubMed:18305213}; Intermembrane side
{ECO:0000269|PubMed:18189341, ECO:0000269|PubMed:18305213}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9FKS5-1; Sequence=Displayed;
Name=2;
IsoId=Q9FKS5-2; Sequence=VSP_054178;
Note=Derived from EST data. No experimental confirmation
available.;
-!- PTM: Binds 1 heme group per subunit. {ECO:0000250}.
-!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA81123.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB011477; BAB11343.1; -; Genomic_DNA.
EMBL; CP002688; AED94597.1; -; Genomic_DNA.
EMBL; CP002688; AED94598.1; -; Genomic_DNA.
EMBL; AY050340; AAK91357.1; -; mRNA.
EMBL; AY116937; AAM51571.1; -; mRNA.
EMBL; AK229445; BAF01305.1; -; mRNA.
EMBL; AK230342; BAF02141.1; -; mRNA.
EMBL; Z25972; CAA81123.1; ALT_INIT; mRNA.
RefSeq; NP_001154756.1; NM_001161284.1. [Q9FKS5-2]
RefSeq; NP_198897.1; NM_123446.5. [Q9FKS5-1]
UniGene; At.23244; -.
UniGene; At.75407; -.
ProteinModelPortal; Q9FKS5; -.
BioGrid; 19332; 1.
IntAct; Q9FKS5; 4.
MINT; Q9FKS5; -.
STRING; 3702.AT5G40810.1; -.
PaxDb; Q9FKS5; -.
PRIDE; Q9FKS5; -.
EnsemblPlants; AT5G40810.1; AT5G40810.1; AT5G40810. [Q9FKS5-1]
EnsemblPlants; AT5G40810.2; AT5G40810.2; AT5G40810. [Q9FKS5-2]
GeneID; 834081; -.
Gramene; AT5G40810.1; AT5G40810.1; AT5G40810. [Q9FKS5-1]
Gramene; AT5G40810.2; AT5G40810.2; AT5G40810. [Q9FKS5-2]
KEGG; ath:AT5G40810; -.
Araport; AT5G40810; -.
TAIR; locus:2164471; AT5G40810.
eggNOG; KOG3052; Eukaryota.
eggNOG; COG2857; LUCA.
HOGENOM; HOG000003867; -.
InParanoid; Q9FKS5; -.
KO; K00413; -.
OMA; SRKIAYR; -.
OrthoDB; EOG09360JHE; -.
PhylomeDB; Q9FKS5; -.
PRO; PR:Q9FKS5; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FKS5; baseline and differential.
Genevisible; Q9FKS5; AT.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005750; C:mitochondrial respiratory chain complex III; IDA:TAIR.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0045153; F:electron transporter, transferring electrons within CoQH2-cytochrome c reductase complex activity; IBA:GO_Central.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IBA:GO_Central.
GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
Gene3D; 1.10.760.10; -; 1.
InterPro; IPR009056; Cyt_c-like_dom.
InterPro; IPR036909; Cyt_c-like_dom_sf.
InterPro; IPR002326; Cyt_c1.
InterPro; IPR021157; Cyt_c1_TM_anchor_C.
PANTHER; PTHR10266; PTHR10266; 1.
Pfam; PF02167; Cytochrom_C1; 1.
PRINTS; PR00603; CYTOCHROMEC1.
SUPFAM; SSF46626; SSF46626; 1.
SUPFAM; SSF81496; SSF81496; 1.
PROSITE; PS51007; CYTC; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Electron transport; Heme;
Iron; Membrane; Metal-binding; Mitochondrion;
Mitochondrion inner membrane; Reference proteome; Respiratory chain;
Transit peptide; Transmembrane; Transmembrane helix; Transport.
TRANSIT 1 64 Mitochondrion. {ECO:0000255}.
CHAIN 65 307 Cytochrome c1 2, heme protein,
mitochondrial.
/FTId=PRO_0000428673.
TRANSMEM 268 288 Helical; Note=Anchors to the membrane.
{ECO:0000255}.
DOMAIN 90 197 Cytochrome c. {ECO:0000255|PROSITE-
ProRule:PRU00433}.
METAL 107 107 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00433}.
METAL 226 226 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00433}.
BINDING 103 103 Heme (covalent). {ECO:0000255|PROSITE-
ProRule:PRU00433}.
BINDING 106 106 Heme (covalent). {ECO:0000255|PROSITE-
ProRule:PRU00433}.
VAR_SEQ 1 47 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_054178.
CONFLICT 83 87 ILSSY -> HFSSS (in Ref. 5; CAA81123).
{ECO:0000305}.
CONFLICT 141 141 N -> H (in Ref. 4; BAF01305).
{ECO:0000305}.
CONFLICT 144 144 G -> C (in Ref. 3; AAK91357/AAM51571).
{ECO:0000305}.
CONFLICT 162 162 S -> L (in Ref. 3; AAK91357/AAM51571).
{ECO:0000305}.
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


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