CY1_HUMAN
ID CY1_HUMAN Reviewed; 325 AA.
AC P08574; Q5U062; Q6FHS7;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Cytochrome c1, heme protein, mitochondrial;
DE EC=7.1.1.8;
DE AltName: Full=Complex III subunit 4;
DE AltName: Full=Complex III subunit IV;
DE AltName: Full=Cytochrome b-c1 complex subunit 4;
DE AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome c1 subunit;
DE Short=Cytochrome c-1;
DE Flags: Precursor;
GN Name=CYC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-76 AND VAL-89.
RX PubMed=2836796; DOI=10.1093/nar/16.8.3577;
RA Nishikimi M., Ohta S., Suzuki H., Tanaka T., Kikkawa F., Tanaka M.,
RA Kagawa Y., Ozawa T.;
RT "Nucleotide sequence of a cDNA encoding the precursor to human cytochrome
RT c1.";
RL Nucleic Acids Res. 16:3577-3577(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-76.
RX PubMed=2536365; DOI=10.1016/s0021-9258(18)94196-7;
RA Suzuki H., Hosokawa Y., Nishikimi M., Ozawa T.;
RT "Structural organization of the human mitochondrial cytochrome c1 gene.";
RL J. Biol. Chem. 264:1368-1374(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-76.
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-76.
RG NIEHS SNPs program;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-76.
RC TISSUE=Brain, Lung, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 99-325.
RX PubMed=3036122; DOI=10.1016/0006-291x(87)91283-6;
RA Nishikimi M., Suzuki H., Ohta S., Sakurai T., Shimomura Y., Tanaka M.,
RA Kagawa Y., Ozawa T.;
RT "Isolation of a cDNA clone for human cytochrome c1 from a lambda gt11
RT expression library.";
RL Biochem. Biophys. Res. Commun. 145:34-39(1987).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-84, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), AND SUBUNIT.
RX PubMed=28844695; DOI=10.1016/j.cell.2017.07.050;
RA Guo R., Zong S., Wu M., Gu J., Yang M.;
RT "Architecture of human mitochondrial respiratory megacomplex I2III2IV2.";
RL Cell 170:1247-1257(2017).
RN [14]
RP VARIANT VAL-89.
RX PubMed=10453733; DOI=10.1007/s004390050988;
RA Valnot I., Kassis J., Chretien D., de Lonlay P., Parfait B., Munnich A.,
RA Kachaner J., Rustin P., Roetig A.;
RT "A mitochondrial cytochrome b mutation but no mutations of nuclearly
RT encoded subunits in ubiquinol cytochrome c reductase (complex III)
RT deficiency.";
RL Hum. Genet. 104:460-466(1999).
RN [15]
RP VARIANTS MC3DN6 CYS-96 AND PHE-215.
RX PubMed=23910460; DOI=10.1016/j.ajhg.2013.06.015;
RA Gaignard P., Menezes M., Schiff M., Bayot A., Rak M., Ogier de Baulny H.,
RA Su C.H., Gilleron M., Lombes A., Abida H., Tzagoloff A., Riley L.,
RA Cooper S.T., Mina K., Sivadorai P., Davis M.R., Allcock R.J., Kresoje N.,
RA Laing N.G., Thorburn D.R., Slama A., Christodoulou J., Rustin P.;
RT "Mutations in CYC1, encoding cytochrome c1 subunit of respiratory chain
RT complex III, cause insulin-responsive hyperglycemia.";
RL Am. J. Hum. Genet. 93:384-389(2013).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2
CC Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:132124; EC=7.1.1.8;
CC Evidence={ECO:0000250|UniProtKB:P07143};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:28844695};
CC Note=Binds 1 heme group covalently per subunit.
CC {ECO:0000269|PubMed:28844695};
CC -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC composed of 11 subunits. The complex is composed of 3 respiratory
CC subunits cytochrome b, cytochrome c1 and Rieske protein UQCRFS1, 2 core
CC protein subunits UQCRC1/QCR1 and UQCRC2/QCR2, and 6 low-molecular
CC weight protein subunits UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8,
CC UQCR10/QCR9, UQCR11/QCR10 and subunit 9, the cleavage product of Rieske
CC protein UQCRFS1 (By similarity). 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) and
CC cytochrome c oxidase (complex IV, CIV), resulting in different
CC assemblies (supercomplex SCI(1)III(2)IV(1) and megacomplex
CC MCI(2)III(2)IV(2)) (PubMed:28844695). {ECO:0000250|UniProtKB:P00125,
CC ECO:0000269|PubMed:28844695}.
CC -!- INTERACTION:
CC P08574; Q8IWZ3-3: ANKHD1; NbExp=3; IntAct=EBI-1224514, EBI-25833200;
CC P08574; P42858: HTT; NbExp=7; IntAct=EBI-1224514, EBI-466029;
CC P08574; Q16342: PDCD2; NbExp=3; IntAct=EBI-1224514, EBI-359462;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P07143}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P07143}.
CC -!- DISEASE: Mitochondrial complex III deficiency, nuclear 6 (MC3DN6)
CC [MIM:615453]: An autosomal recessive disorder caused by mitochondrial
CC dysfunction. It is characterized by onset in early childhood of
CC episodic acute lactic acidosis, ketoacidosis, and insulin-responsive
CC hyperglycemia, usually associated with infection. Laboratory studies
CC show decreased activity of mitochondrial complex III. Psychomotor
CC development is normal. {ECO:0000269|PubMed:23910460}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/cyc1/";
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DR EMBL; M16597; AAA35730.1; -; mRNA.
DR EMBL; J04444; AAA52135.1; -; Genomic_DNA.
DR EMBL; CR541674; CAG46475.1; -; mRNA.
DR EMBL; BT019798; AAV38601.1; -; mRNA.
DR EMBL; DQ300360; ABB96244.1; -; Genomic_DNA.
DR EMBL; AC104592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001006; AAH01006.1; -; mRNA.
DR EMBL; BC015616; AAH15616.1; -; mRNA.
DR EMBL; BC020566; AAH20566.1; -; mRNA.
DR EMBL; X06994; CAA30052.1; -; mRNA.
DR CCDS; CCDS6415.1; -.
DR PIR; A31481; S00680.
DR RefSeq; NP_001907.2; NM_001916.4.
DR PDB; 5XTE; EM; 3.40 A; H/U=85-325.
DR PDB; 5XTH; EM; 3.90 A; AH/AU=85-325.
DR PDB; 5XTI; EM; 17.40 A; AH/AU=85-325.
DR PDBsum; 5XTE; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; P08574; -.
DR SMR; P08574; -.
DR BioGRID; 107917; 205.
DR ComplexPortal; CPX-560; Mitochondrial respiratory chain complex III.
DR IntAct; P08574; 42.
DR MINT; P08574; -.
DR STRING; 9606.ENSP00000317159; -.
DR ChEMBL; CHEMBL4105975; -.
DR DrugBank; DB07763; (5S)-3-ANILINO-5-(2,4-DIFLUOROPHENYL)-5-METHYL-1,3-OXAZOLIDINE-2,4-DIONE.
DR DrugBank; DB07778; (S)-famoxadone.
DR DrugBank; DB04141; 2-Hexyloxy-6-Hydroxymethyl-Tetrahydro-Pyran-3,4,5-Triol.
DR DrugBank; DB08453; 2-Nonyl-4-quinolinol 1-oxide.
DR DrugBank; DB07636; 5-Heptyl-6-hydroxy-1,3-benzothiazole-4,7-dione.
DR DrugBank; DB04799; 6-Hydroxy-5-undecyl-4,7-benzothiazoledione.
DR DrugBank; DB07401; Azoxystrobin.
DR DrugBank; DB08330; METHYL (2Z)-3-METHOXY-2-{2-[(E)-2-PHENYLVINYL]PHENYL}ACRYLATE.
DR DrugBank; DB08690; Ubiquinone Q2.
DR GlyGen; P08574; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P08574; -.
DR PhosphoSitePlus; P08574; -.
DR SwissPalm; P08574; -.
DR BioMuta; CYC1; -.
DR DMDM; 311033458; -.
DR CPTAC; CPTAC-490; -.
DR CPTAC; CPTAC-491; -.
DR EPD; P08574; -.
DR jPOST; P08574; -.
DR MassIVE; P08574; -.
DR MaxQB; P08574; -.
DR PaxDb; P08574; -.
DR PeptideAtlas; P08574; -.
DR PRIDE; P08574; -.
DR ProteomicsDB; 52124; -.
DR TopDownProteomics; P08574; -.
DR Antibodypedia; 810; 401 antibodies from 33 providers.
DR DNASU; 1537; -.
DR Ensembl; ENST00000318911.5; ENSP00000317159.4; ENSG00000179091.5.
DR GeneID; 1537; -.
DR KEGG; hsa:1537; -.
DR MANE-Select; ENST00000318911.5; ENSP00000317159.4; NM_001916.5; NP_001907.3.
DR UCSC; uc003zaz.6; human.
DR CTD; 1537; -.
DR DisGeNET; 1537; -.
DR GeneCards; CYC1; -.
DR HGNC; HGNC:2579; CYC1.
DR HPA; ENSG00000179091; Tissue enhanced (skeletal muscle, tongue).
DR MalaCards; CYC1; -.
DR MIM; 123980; gene.
DR MIM; 615453; phenotype.
DR neXtProt; NX_P08574; -.
DR OpenTargets; ENSG00000179091; -.
DR Orphanet; 1460; Isolated complex III deficiency.
DR PharmGKB; PA27077; -.
DR VEuPathDB; HostDB:ENSG00000179091; -.
DR eggNOG; KOG3052; Eukaryota.
DR GeneTree; ENSGT00390000012445; -.
DR HOGENOM; CLU_040334_1_0_1; -.
DR InParanoid; P08574; -.
DR OMA; VWVKKFK; -.
DR OrthoDB; 923710at2759; -.
DR PhylomeDB; P08574; -.
DR TreeFam; TF314799; -.
DR BioCyc; MetaCyc:HS11349-MON; -.
DR PathwayCommons; P08574; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR SignaLink; P08574; -.
DR SIGNOR; P08574; -.
DR BioGRID-ORCS; 1537; 382 hits in 1086 CRISPR screens.
DR ChiTaRS; CYC1; human.
DR GeneWiki; CYC1; -.
DR GenomeRNAi; 1537; -.
DR Pharos; P08574; Tchem.
DR PRO; PR:P08574; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P08574; protein.
DR Bgee; ENSG00000179091; Expressed in apex of heart and 198 other tissues.
DR Genevisible; P08574; HS.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IPI:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0045333; P:cellular respiration; IC:ComplexPortal.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR GO; GO:0033762; P:response to glucagon; IEA:Ensembl.
DR Gene3D; 1.10.760.10; -; 1.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Disease variant; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Primary mitochondrial disease; Reference proteome; Respiratory chain;
KW Transit peptide; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..84
FT /note="Mitochondrion"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 85..325
FT /note="Cytochrome c1, heme protein, mitochondrial"
FT /id="PRO_0000006554"
FT TOPO_DOM 85..281
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:28844695"
FT TRANSMEM 282..315
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28844695"
FT TOPO_DOM 316..325
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:28844695"
FT DOMAIN 108..209
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 121
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P00125"
FT BINDING 124
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P00125"
FT BINDING 125
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:28844695,
FT ECO:0007744|PDB:5XTE, ECO:0007744|PDB:5XTH"
FT BINDING 244
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:28844695,
FT ECO:0007744|PDB:5XTH"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 76
FT /note="M -> V (in dbSNP:rs7820984)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2536365, ECO:0000269|PubMed:2836796,
FT ECO:0000269|Ref.3, ECO:0000269|Ref.5"
FT /id="VAR_025163"
FT VARIANT 89
FT /note="L -> V"
FT /evidence="ECO:0000269|PubMed:10453733,
FT ECO:0000269|PubMed:2836796"
FT /id="VAR_013631"
FT VARIANT 96
FT /note="W -> C (in MC3DN6; dbSNP:rs587777041)"
FT /evidence="ECO:0000269|PubMed:23910460"
FT /id="VAR_070847"
FT VARIANT 215
FT /note="L -> F (in MC3DN6; dbSNP:rs587777042)"
FT /evidence="ECO:0000269|PubMed:23910460"
FT /id="VAR_070848"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 107..117
FT /evidence="ECO:0007829|PDB:5XTE"
FT TURN 118..123
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 182..187
FT /evidence="ECO:0007829|PDB:5XTE"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:5XTE"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 263..278
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 282..315
FT /evidence="ECO:0007829|PDB:5XTE"
SQ 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
