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

 CY1_MOUSE               Reviewed;         325 AA.
Q9D0M3; Q3TDC5; Q3UAN2; Q63ZW4; Q9DCG0;
11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
12-SEP-2018, entry version 151.
RecName: Full=Cytochrome c1, heme protein, mitochondrial;
AltName: Full=Complex III subunit 4;
AltName: Full=Complex III subunit IV;
AltName: Full=Cytochrome b-c1 complex subunit 4;
AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome c1 subunit;
Short=Cytochrome c-1;
Flags: Precursor;
Name=Cyc1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Embryo, and Kidney;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Jaw;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 100-111; 134-202; 269-285 AND 292-307, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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 bc1 complex contains 11 subunits: 3 respiratory
subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core
proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight
proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9,
UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass
membrane protein; Intermembrane side.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9D0M3-1; Sequence=Displayed;
Name=2;
IsoId=Q9D0M3-2; Sequence=VSP_025056;
-!- PTM: Binds 1 heme group per subunit.
-!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH82790.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AK002815; BAB22380.1; -; mRNA.
EMBL; AK011288; BAB27518.1; -; mRNA.
EMBL; AK151299; BAE30282.1; -; mRNA.
EMBL; AK170272; BAE41677.1; -; mRNA.
EMBL; BC005620; AAH05620.1; -; mRNA.
EMBL; BC082790; AAH82790.1; ALT_INIT; mRNA.
CCDS; CCDS27567.1; -. [Q9D0M3-1]
RefSeq; NP_079843.1; NM_025567.2. [Q9D0M3-1]
UniGene; Mm.29196; -.
ProteinModelPortal; Q9D0M3; -.
SMR; Q9D0M3; -.
BioGrid; 211479; 2.
ComplexPortal; CPX-563; Mitochondrial respiratory chain complex III.
CORUM; Q9D0M3; -.
IntAct; Q9D0M3; 18.
MINT; Q9D0M3; -.
STRING; 10090.ENSMUSP00000023210; -.
iPTMnet; Q9D0M3; -.
PhosphoSitePlus; Q9D0M3; -.
SwissPalm; Q9D0M3; -.
PaxDb; Q9D0M3; -.
PeptideAtlas; Q9D0M3; -.
PRIDE; Q9D0M3; -.
TopDownProteomics; Q9D0M3-1; -. [Q9D0M3-1]
Ensembl; ENSMUST00000023210; ENSMUSP00000023210; ENSMUSG00000022551. [Q9D0M3-1]
GeneID; 66445; -.
KEGG; mmu:66445; -.
UCSC; uc007wjs.1; mouse. [Q9D0M3-1]
CTD; 1537; -.
MGI; MGI:1913695; Cyc1.
eggNOG; KOG3052; Eukaryota.
eggNOG; COG2857; LUCA.
GeneTree; ENSGT00390000012445; -.
HOGENOM; HOG000003867; -.
HOVERGEN; HBG001239; -.
InParanoid; Q9D0M3; -.
KO; K00413; -.
OMA; SRKIAYR; -.
OrthoDB; EOG091G0FT2; -.
PhylomeDB; Q9D0M3; -.
TreeFam; TF314799; -.
PRO; PR:Q9D0M3; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000022551; Expressed in 297 organ(s), highest expression level in diaphragm.
CleanEx; MM_CYC1; -.
Genevisible; Q9D0M3; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
GO; GO:0005750; C:mitochondrial respiratory chain complex III; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; IBA:GO_Central.
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.
GO; GO:0033762; P:response to glucagon; ISO:MGI.
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; Direct protein sequencing;
Electron transport; Heme; Iron; Membrane; Metal-binding;
Mitochondrion; Mitochondrion inner membrane; Reference proteome;
Respiratory chain; Transit peptide; Transmembrane;
Transmembrane helix; Transport.
TRANSIT 1 84 Mitochondrion. {ECO:0000250}.
CHAIN 85 325 Cytochrome c1, heme protein,
mitochondrial.
/FTId=PRO_0000006555.
TRANSMEM 292 306 Helical; Note=Anchors to the membrane.
{ECO:0000255}.
DOMAIN 108 209 Cytochrome c. {ECO:0000255|PROSITE-
ProRule:PRU00433}.
METAL 125 125 Iron (heme axial ligand).
METAL 244 244 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00433}.
BINDING 121 121 Heme (covalent).
BINDING 124 124 Heme (covalent).
VAR_SEQ 1 59 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_025056.
CONFLICT 44 44 A -> R (in Ref. 1; BAB22380).
{ECO:0000305}.
CONFLICT 318 318 K -> R (in Ref. 1; BAB22380).
{ECO:0000305}.
SEQUENCE 325 AA; 35328 MW; 5F7DD8B78677E9BF CRC64;
MAAAAASLRR TVLGPRGVGL PGASAPGLLG GARSRQLPLR TPQAVSLSSK SGPSRGRKVM
LSALGMLAAG GAGLAVALHS AVSASDLELH PPSYPWSHRG LLSSLDHTSI RRGFQVYKQV
CSSCHSMDYV AYRHLVGVCY TEEEAKALAE EVEVQDGPND DGEMFMRPGK LSDYFPKPYP
NPEAARAANN GALPPDLSYI VRARHGGEDY VFSLLTGYCE PPTGVSLREG LYFNPYFPGQ
AIGMAPPIYT EVLEYDDGTP ATMSQVAKDV ATFLRWASEP EHDHRKRMGL KMLLMMGLLL
PLTYAMKRHK WSVLKSRKLA YRPPK


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