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 27-MAR-2024, entry version 218. 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 c; Xref=ChEBI:CHEBI:61717; CC Evidence={ECO:0000269|PubMed:28844695}; CC Note=Binds 1 heme c 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). Interacts with FLVCR2; this CC interaction occurs in the absence of heme and is disrupted upon heme CC binding. {ECO:0000250|UniProtKB:P00125, ECO:0000250|UniProtKB:Q9D0M3, 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 type 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/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 222. DR ComplexPortal; CPX-560; Mitochondrial respiratory chain complex III. DR IntAct; P08574; 44. 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; 9606-ENSP00000317159; -. DR PeptideAtlas; P08574; -. DR PRIDE; P08574; -. DR ProteomicsDB; 52124; -. DR Pumba; P08574; -. DR TopDownProteomics; P08574; -. DR Antibodypedia; 810; 440 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 AGR; HGNC:2579; -. 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; WVKKFKW; -. DR OrthoDB; 275461at2759; -. DR PhylomeDB; P08574; -. DR TreeFam; TF314799; -. DR BioCyc; MetaCyc:HS11349-MONOMER; -. 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; 415 hits in 1167 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 200 other cell types or tissues. 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; NAS: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; Cytochrome c-like domain; 1. DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 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; CYTOCHROME C1; 1. DR PANTHER; PTHR10266:SF3; CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL; 1. DR Pfam; PF02167; Cytochrom_C1; 1. DR PRINTS; PR00603; CYTOCHROMEC1. DR SUPFAM; SSF46626; Cytochrome c; 1. DR SUPFAM; SSF81496; Cytochrome c1 subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase), transmembrane anchor; 1. DR Genevisible; P08574; HS. 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 c" FT /ligand_id="ChEBI:CHEBI:61717" FT /note="covalent" FT /evidence="ECO:0000250|UniProtKB:P00125" FT BINDING 124 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /note="covalent" FT /evidence="ECO:0000250|UniProtKB:P00125" FT BINDING 125 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:0000269|PubMed:28844695, FT ECO:0007744|PDB:5XTE, ECO:0007744|PDB:5XTH" FT BINDING 244 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: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 //