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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_HUMAN               Reviewed;         325 AA.
P08574; Q5U062; Q6FHS7;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 3.
28-FEB-2018, entry version 180.
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;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-76 AND VAL-89.
PubMed=2836796; DOI=10.1093/nar/16.8.3577;
Nishikimi M., Ohta S., Suzuki H., Tanaka T., Kikkawa F., Tanaka M.,
Kagawa Y., Ozawa T.;
"Nucleotide sequence of a cDNA encoding the precursor to human
cytochrome c1.";
Nucleic Acids Res. 16:3577-3577(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-76.
PubMed=2536365;
Suzuki H., Hosokawa Y., Nishikimi M., Ozawa T.;
"Structural organization of the human mitochondrial cytochrome c1
gene.";
J. Biol. Chem. 264:1368-1374(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-76.
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-76.
NIEHS SNPs program;
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-76.
TISSUE=Brain, Lung, and Skin;
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 99-325.
PubMed=3036122; DOI=10.1016/0006-291X(87)91283-6;
Nishikimi M., Suzuki H., Ohta S., Sakurai T., Shimomura Y., Tanaka M.,
Kagawa Y., Ozawa T.;
"Isolation of a cDNA clone for human cytochrome c1 from a lambda gt11
expression library.";
Biochem. Biophys. Res. Commun. 145:34-39(1987).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-84, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[13]
VARIANT VAL-89.
PubMed=10453733; DOI=10.1007/s004390050988;
Valnot I., Kassis J., Chretien D., de Lonlay P., Parfait B.,
Munnich A., Kachaner J., Rustin P., Roetig A.;
"A mitochondrial cytochrome b mutation but no mutations of nuclearly
encoded subunits in ubiquinol cytochrome c reductase (complex III)
deficiency.";
Hum. Genet. 104:460-466(1999).
[14]
VARIANTS MC3DN6 CYS-96 AND PHE-215.
PubMed=23910460; DOI=10.1016/j.ajhg.2013.06.015;
Gaignard P., Menezes M., Schiff M., Bayot A., Rak M.,
Ogier de Baulny H., Su C.H., Gilleron M., Lombes A., Abida H.,
Tzagoloff A., Riley L., Cooper S.T., Mina K., Sivadorai P.,
Davis M.R., Allcock R.J., Kresoje N., Laing N.G., Thorburn D.R.,
Slama A., Christodoulou J., Rustin P.;
"Mutations in CYC1, encoding cytochrome c1 subunit of respiratory
chain complex III, cause insulin-responsive hyperglycemia.";
Am. J. Hum. Genet. 93:384-389(2013).
-!- 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.
-!- 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).
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass
membrane protein; Intermembrane side.
-!- PTM: Binds 1 heme group per subunit.
-!- DISEASE: Mitochondrial complex III deficiency, nuclear 6 (MC3DN6)
[MIM:615453]: An autosomal recessive disorder caused by
mitochondrial dysfunction. It is characterized by onset in early
childhood of episodic acute lactic acidosis, ketoacidosis, and
insulin-responsive hyperglycemia, usually associated with
infection. Laboratory studies show decreased activity of
mitochondrial complex III. Psychomotor development is normal.
{ECO:0000269|PubMed:23910460}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cyc1/";
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EMBL; M16597; AAA35730.1; -; mRNA.
EMBL; J04444; AAA52135.1; -; Genomic_DNA.
EMBL; CR541674; CAG46475.1; -; mRNA.
EMBL; BT019798; AAV38601.1; -; mRNA.
EMBL; DQ300360; ABB96244.1; -; Genomic_DNA.
EMBL; AC104592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001006; AAH01006.1; -; mRNA.
EMBL; BC015616; AAH15616.1; -; mRNA.
EMBL; BC020566; AAH20566.1; -; mRNA.
EMBL; X06994; CAA30052.1; -; mRNA.
CCDS; CCDS6415.1; -.
PIR; A31481; S00680.
RefSeq; NP_001907.2; NM_001916.4.
UniGene; Hs.289271; -.
PDB; 5XTE; EM; 3.40 A; H/U=85-325.
PDB; 5XTH; EM; 3.90 A; AH/AU=85-325.
PDB; 5XTI; EM; 17.40 A; AH/AU=85-325.
PDBsum; 5XTE; -.
PDBsum; 5XTH; -.
PDBsum; 5XTI; -.
ProteinModelPortal; P08574; -.
SMR; P08574; -.
BioGrid; 107917; 83.
IntAct; P08574; 12.
MINT; P08574; -.
STRING; 9606.ENSP00000317159; -.
DrugBank; DB08453; 2-NONYL-4-HYDROXYQUINOLINE N-OXIDE.
DrugBank; DB07778; FAMOXADONE.
DrugBank; DB07401; METHYL (2Z)-2-(2-{[6-(2-CYANOPHENOXY)PYRIMIDIN-4-YL]OXY}PHENYL)-3-METHOXYACRYLATE.
DrugBank; DB08330; METHYL (2Z)-3-METHOXY-2-{2-[(E)-2-PHENYLVINYL]PHENYL}ACRYLATE.
DrugBank; DB08690; UBIQUINONE-2.
iPTMnet; P08574; -.
PhosphoSitePlus; P08574; -.
SwissPalm; P08574; -.
BioMuta; CYC1; -.
DMDM; 311033458; -.
EPD; P08574; -.
MaxQB; P08574; -.
PaxDb; P08574; -.
PeptideAtlas; P08574; -.
PRIDE; P08574; -.
TopDownProteomics; P08574; -.
DNASU; 1537; -.
Ensembl; ENST00000318911; ENSP00000317159; ENSG00000179091.
GeneID; 1537; -.
KEGG; hsa:1537; -.
UCSC; uc003zaz.6; human.
CTD; 1537; -.
DisGeNET; 1537; -.
EuPathDB; HostDB:ENSG00000179091.4; -.
GeneCards; CYC1; -.
HGNC; HGNC:2579; CYC1.
HPA; HPA001247; -.
MalaCards; CYC1; -.
MIM; 123980; gene.
MIM; 615453; phenotype.
neXtProt; NX_P08574; -.
OpenTargets; ENSG00000179091; -.
Orphanet; 1460; Isolated CoQ-cytochrome C reductase deficiency.
PharmGKB; PA27077; -.
eggNOG; KOG3052; Eukaryota.
eggNOG; COG2857; LUCA.
GeneTree; ENSGT00390000012445; -.
HOGENOM; HOG000003867; -.
HOVERGEN; HBG001239; -.
InParanoid; P08574; -.
KO; K00413; -.
OMA; SRKIAYR; -.
OrthoDB; EOG091G0FT2; -.
PhylomeDB; P08574; -.
TreeFam; TF314799; -.
Reactome; R-HSA-1268020; Mitochondrial protein import.
Reactome; R-HSA-611105; Respiratory electron transport.
ChiTaRS; CYC1; human.
GeneWiki; CYC1; -.
GenomeRNAi; 1537; -.
PRO; PR:P08574; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000179091; -.
CleanEx; HS_CYC1; -.
Genevisible; P08574; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
GO; GO:0005750; C:mitochondrial respiratory chain complex III; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; TAS:ProtInc.
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; IEA:Ensembl.
Gene3D; 1.10.760.10; -; 1.
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.
1: Evidence at protein level;
3D-structure; Complete proteome; Disease mutation; Electron transport;
Heme; Iron; Membrane; Metal-binding; Mitochondrion;
Mitochondrion inner membrane; Phosphoprotein; Polymorphism;
Primary mitochondrial disease; Reference proteome; Respiratory chain;
Transit peptide; Transmembrane; Transmembrane helix; Transport.
TRANSIT 1 84 Mitochondrion.
{ECO:0000244|PubMed:25944712}.
CHAIN 85 325 Cytochrome c1, heme protein,
mitochondrial.
/FTId=PRO_0000006554.
TRANSMEM 292 306 Helical; Note=Anchors to the membrane.
{ECO:0000255}.
DOMAIN 108 209 Cytochrome c.
METAL 125 125 Iron (heme axial ligand).
METAL 244 244 Iron (heme axial ligand). {ECO:0000250}.
BINDING 121 121 Heme (covalent).
BINDING 124 124 Heme (covalent).
MOD_RES 182 182 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 76 76 M -> V (in dbSNP:rs7820984).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2536365,
ECO:0000269|PubMed:2836796,
ECO:0000269|Ref.3, ECO:0000269|Ref.5}.
/FTId=VAR_025163.
VARIANT 89 89 L -> V. {ECO:0000269|PubMed:10453733,
ECO:0000269|PubMed:2836796}.
/FTId=VAR_013631.
VARIANT 96 96 W -> C (in MC3DN6; dbSNP:rs587777041).
{ECO:0000269|PubMed:23910460}.
/FTId=VAR_070847.
VARIANT 215 215 L -> F (in MC3DN6; dbSNP:rs587777042).
{ECO:0000269|PubMed:23910460}.
/FTId=VAR_070848.
HELIX 97 99 {ECO:0000244|PDB:5XTE}.
STRAND 100 102 {ECO:0000244|PDB:5XTE}.
HELIX 107 117 {ECO:0000244|PDB:5XTE}.
TURN 118 123 {ECO:0000244|PDB:5XTE}.
STRAND 131 134 {ECO:0000244|PDB:5XTE}.
HELIX 135 138 {ECO:0000244|PDB:5XTE}.
HELIX 142 149 {ECO:0000244|PDB:5XTE}.
STRAND 159 162 {ECO:0000244|PDB:5XTE}.
STRAND 178 181 {ECO:0000244|PDB:5XTE}.
HELIX 182 187 {ECO:0000244|PDB:5XTE}.
TURN 188 191 {ECO:0000244|PDB:5XTE}.
HELIX 200 203 {ECO:0000244|PDB:5XTE}.
TURN 205 207 {ECO:0000244|PDB:5XTE}.
HELIX 208 216 {ECO:0000244|PDB:5XTE}.
STRAND 242 244 {ECO:0000244|PDB:5XTE}.
HELIX 263 278 {ECO:0000244|PDB:5XTE}.
HELIX 282 315 {ECO:0000244|PDB:5XTE}.
SEQUENCE 325 AA; 35422 MW; CC8EA2E60E96BBDC CRC64;
MAAAAASLRG VVLGPRGAGL PGARARGLLC SARPGQLPLR TPQAVALSSK SGLSRGRKVM
LSALGMLAAG GAGLAMALHS AVSASDLELH PPSYPWSHRG LLSSLDHTSI RRGFQVYKQV
CASCHSMDFV AYRHLVGVCY TEDEAKELAA EVEVQDGPNE DGEMFMRPGK LFDYFPKPYP
NSEAARAANN GALPPDLSYI VRARHGGEDY VFSLLTGYCE PPTGVSLREG LYFNPYFPGQ
AIAMAPPIYT DVLEFDDGTP ATMSQIAKDV CTFLRWASEP EHDHRKRMGL KMLMMMALLV
PLVYTIKRHK WSVLKSRKLA YRPPK


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