CYB5_HUMAN
ID CYB5_HUMAN Reviewed; 134 AA.
AC P00167; A8MV91; F8WEU4; Q6IB14;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Cytochrome b5;
DE AltName: Full=Microsomal cytochrome b5 type A;
DE Short=MCB5;
GN Name=CYB5A; Synonyms=CYB5;
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] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=3178851; DOI=10.1016/s0006-291x(88)80881-7;
RA Yoo M., Steggles A.W.;
RT "The complete nucleotide sequence of human liver cytochrome b5 mRNA.";
RL Biochem. Biophys. Res. Commun. 156:576-580(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Erythrocyte;
RX PubMed=1712589; DOI=10.1016/0006-291x(91)91776-9;
RA Giordano S.J., Steggles A.W.;
RT "The human liver and reticulocyte cytochrome b5 mRNAs are products from a
RT single gene.";
RL Biochem. Biophys. Res. Commun. 178:38-44(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7733981; DOI=10.1006/bbrc.1995.1582;
RA Li X.R., Giordano S.J., Yoo M., Steggles A.W.;
RT "The isolation and characterization of the human cytochrome b5 gene.";
RL Biochem. Biophys. Res. Commun. 209:894-900(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Pancreas;
RA Melton D., Brown J., Kenty G., Permutt A., Lee C., Kaestner K.,
RA Lemishka I., Scearce M., Brestelli J., Gradwohl G., Clifton S., Hillier L.,
RA Marra M., Pape D., Wylie T., Martin J., Blistain A., Schmitt A.,
RA Theising B., Ritter E., Ronko I., Bennett J., Cardenas M., Gibbons M.,
RA McCann R., Cole R., Tsagareishvili R., Williams T., Jackson Y., Bowers Y.;
RT "Endocrine pancreas consortium.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [9]
RP PROTEIN SEQUENCE OF 2-98.
RC TISSUE=Erythrocyte;
RX PubMed=4030743; DOI=10.1093/oxfordjournals.jbchem.a135224;
RA Abe K., Kimura S., Kizawa R., Anan F.K., Sugita Y.;
RT "Amino acid sequences of cytochrome b5 from human, porcine, and bovine
RT erythrocytes and comparison with liver microsomal cytochrome b5.";
RL J. Biochem. 97:1659-1668(1985).
RN [10]
RP PROTEIN SEQUENCE OF 2-91.
RX PubMed=4993957; DOI=10.1016/s0021-9258(18)62368-3;
RA Nobrega F.G., Ozols J.;
RT "Amino acid sequences of tryptic peptides of cytochromes b5 from microsomes
RT of human, monkey, porcine, and chicken liver.";
RL J. Biol. Chem. 246:1706-1717(1971).
RN [11]
RP PROTEIN SEQUENCE OF 2-91.
RX PubMed=5062820; DOI=10.1016/s0021-9258(19)45520-8;
RA Ozols J.;
RT "Cytochrome b5 from a normal human liver. Isolation and the partial amino
RT acid sequence.";
RL J. Biol. Chem. 247:2242-2245(1972).
RN [12]
RP PROTEIN SEQUENCE OF 2-91.
RX PubMed=4770377;
RA Rashid M.A., Hagihara B., Kobayashi M., Tani S., Tsugita A.;
RT "Structural studies of cytochrome b5. 3. Sequential studies on human liver
RT cytochrome b5.";
RL J. Biochem. 74:985-1002(1973).
RN [13]
RP PROTEIN SEQUENCE OF 2-36 AND 84-134, CLEAVAGE OF INITIATOR METHIONINE, AND
RP ACETYLATION AT ALA-2.
RX PubMed=2752049; DOI=10.1016/0167-4838(89)90143-x;
RA Ozols J.;
RT "Structure of cytochrome b5 and its topology in the microsomal membrane.";
RL Biochim. Biophys. Acta 997:121-130(1989).
RN [14]
RP INVOLVEMENT IN METAG.
RX PubMed=8168836; DOI=10.1007/bf00202825;
RA Giordano S.J., Kaftory A., Steggles A.W.;
RT "A splicing mutation in the cytochrome b5 gene from a patient with
RT congenital methemoglobinemia and pseudohermaphrodism.";
RL Hum. Genet. 93:568-570(1994).
RN [15]
RP INVOLVEMENT IN METAG, AND VARIANT METAG 27-TRP--ASP-134 DEL.
RX PubMed=20080843; DOI=10.1210/jc.2008-1745;
RA Kok R.C., Timmerman M.A., Wolffenbuttel K.P., Drop S.L., de Jong F.H.;
RT "Isolated 17,20-lyase deficiency due to the cytochrome b5 mutation W27X.";
RL J. Clin. Endocrinol. Metab. 95:994-999(2010).
RN [16]
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 [17]
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 [18]
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 [19]
RP VARIANT METAG LEU-44.
RX PubMed=22170710; DOI=10.1210/jc.2011-2413;
RA Idkowiak J., Randell T., Dhir V., Patel P., Shackleton C.H., Taylor N.F.,
RA Krone N., Arlt W.;
RT "A missense mutation in the human cytochrome B5 gene causes 46,XY disorder
RT of sex development due to true isolated 17,20 lyase deficiency.";
RL J. Clin. Endocrinol. Metab. 97:E465-E475(2012).
CC -!- FUNCTION: Cytochrome b5 is a membrane-bound hemoprotein functioning as
CC an electron carrier for several membrane-bound oxygenases.
CC -!- INTERACTION:
CC P00167; P28799: GRN; NbExp=3; IntAct=EBI-1047284, EBI-747754;
CC P00167; O60333-2: KIF1B; NbExp=3; IntAct=EBI-1047284, EBI-10975473;
CC P00167; D3DTS7: PMP22; NbExp=3; IntAct=EBI-1047284, EBI-25882629;
CC P00167; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-1047284, EBI-396669;
CC P00167; O76024: WFS1; NbExp=3; IntAct=EBI-1047284, EBI-720609;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane;
CC Single-pass membrane protein; Cytoplasmic side. Microsome membrane;
CC Single-pass membrane protein; Cytoplasmic side.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Liver, Membrane-bound;
CC IsoId=P00167-1; Sequence=Displayed;
CC Name=2; Synonyms=Erythrocyte, Cytoplasmic;
CC IsoId=P00167-2; Sequence=VSP_001240, VSP_001241;
CC Name=3;
CC IsoId=P00167-3; Sequence=VSP_045367;
CC -!- DISEASE: Methemoglobinemia and ambiguous genitalia (METAG)
CC [MIM:250790]: An autosomal recessive disorder characterized by sex
CC steroid deficiency but normal glucocorticoid and mineralocorticoid
CC reserve, male undermasculinization, absent or disturbed pubertal
CC development, decreased levels of erythrocyte cytochrome B5, and
CC excessive amounts of methemoglobin in blood cells resulting in cyanosis
CC and hypoxia. {ECO:0000269|PubMed:20080843, ECO:0000269|PubMed:22170710,
CC ECO:0000269|PubMed:8168836}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA63169.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M22865; AAA35729.1; -; mRNA.
DR EMBL; M60174; AAA52165.1; -; mRNA.
DR EMBL; L39945; AAA63169.1; ALT_SEQ; Genomic_DNA.
DR EMBL; L39792; AAA63169.1; JOINED; Genomic_DNA.
DR EMBL; L39941; AAA63169.1; JOINED; Genomic_DNA.
DR EMBL; L39942; AAA63169.1; JOINED; Genomic_DNA.
DR EMBL; L39943; AAA63169.1; JOINED; Genomic_DNA.
DR EMBL; L39944; AAA63169.1; JOINED; Genomic_DNA.
DR EMBL; CA771478; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CR456990; CAG33271.1; -; mRNA.
DR EMBL; AC090398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471117; EAW66544.1; -; Genomic_DNA.
DR EMBL; BC015182; AAH15182.1; -; mRNA.
DR CCDS; CCDS12004.1; -. [P00167-1]
DR CCDS; CCDS12005.1; -. [P00167-2]
DR CCDS; CCDS54188.1; -. [P00167-3]
DR PIR; A28936; CBHU5.
DR PIR; JN0075; CBHU5E.
DR RefSeq; NP_001177736.1; NM_001190807.2. [P00167-3]
DR RefSeq; NP_001905.1; NM_001914.3. [P00167-2]
DR RefSeq; NP_683725.1; NM_148923.3. [P00167-1]
DR RefSeq; XP_011524137.1; XM_011525835.2. [P00167-2]
DR PDB; 2I96; NMR; -; A=1-108.
DR PDBsum; 2I96; -.
DR AlphaFoldDB; P00167; -.
DR SMR; P00167; -.
DR BioGRID; 107908; 125.
DR IntAct; P00167; 22.
DR STRING; 9606.ENSP00000341625; -.
DR ChEMBL; CHEMBL6170; -.
DR DrugBank; DB14526; Chromic citrate.
DR DrugBank; DB14527; Chromic nitrate.
DR DrugBank; DB11136; Chromium.
DR DrugBank; DB14528; Chromium gluconate.
DR DrugBank; DB14529; Chromium nicotinate.
DR DrugBank; DB14530; Chromous sulfate.
DR DrugBank; DB04009; Dimethyl Propionate Ester Heme.
DR iPTMnet; P00167; -.
DR PhosphoSitePlus; P00167; -.
DR BioMuta; CYB5A; -.
DR DMDM; 117809; -.
DR EPD; P00167; -.
DR jPOST; P00167; -.
DR MassIVE; P00167; -.
DR MaxQB; P00167; -.
DR PaxDb; P00167; -.
DR PeptideAtlas; P00167; -.
DR PRIDE; P00167; -.
DR ProteomicsDB; 31960; -.
DR ProteomicsDB; 51226; -. [P00167-1]
DR ProteomicsDB; 51227; -. [P00167-2]
DR TopDownProteomics; P00167-1; -. [P00167-1]
DR TopDownProteomics; P00167-3; -. [P00167-3]
DR Antibodypedia; 23308; 373 antibodies from 31 providers.
DR DNASU; 1528; -.
DR Ensembl; ENST00000340533.9; ENSP00000341625.4; ENSG00000166347.19. [P00167-1]
DR Ensembl; ENST00000397914.4; ENSP00000381011.4; ENSG00000166347.19. [P00167-3]
DR Ensembl; ENST00000494131.6; ENSP00000436461.2; ENSG00000166347.19. [P00167-2]
DR GeneID; 1528; -.
DR KEGG; hsa:1528; -.
DR MANE-Select; ENST00000340533.9; ENSP00000341625.4; NM_148923.4; NP_683725.1.
DR UCSC; uc002llh.4; human. [P00167-1]
DR CTD; 1528; -.
DR DisGeNET; 1528; -.
DR GeneCards; CYB5A; -.
DR HGNC; HGNC:2570; CYB5A.
DR HPA; ENSG00000166347; Tissue enhanced (kidney, liver).
DR MalaCards; CYB5A; -.
DR MIM; 250790; phenotype.
DR MIM; 613218; gene.
DR neXtProt; NX_P00167; -.
DR OpenTargets; ENSG00000166347; -.
DR Orphanet; 90796; 46,XY disorder of sex development due to isolated 17,20-lyase deficiency.
DR Orphanet; 621; Hereditary methemoglobinemia.
DR PharmGKB; PA27068; -.
DR VEuPathDB; HostDB:ENSG00000166347; -.
DR eggNOG; KOG0537; Eukaryota.
DR GeneTree; ENSGT00940000156770; -.
DR HOGENOM; CLU_102602_4_2_1; -.
DR InParanoid; P00167; -.
DR OMA; YRFYFTQ; -.
DR OrthoDB; 1566561at2759; -.
DR PhylomeDB; P00167; -.
DR TreeFam; TF314537; -.
DR BioCyc; MetaCyc:ENSG00000166347-MON; -.
DR PathwayCommons; P00167; -.
DR Reactome; R-HSA-196836; Vitamin C (ascorbate) metabolism.
DR Reactome; R-HSA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane. [P00167-1]
DR SignaLink; P00167; -.
DR BioGRID-ORCS; 1528; 11 hits in 1086 CRISPR screens.
DR ChiTaRS; CYB5A; human.
DR EvolutionaryTrace; P00167; -.
DR GeneWiki; Cytochrome_b5,_type_A; -.
DR GenomeRNAi; 1528; -.
DR Pharos; P00167; Tbio.
DR PRO; PR:P00167; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; P00167; protein.
DR Bgee; ENSG00000166347; Expressed in nephron tubule and 207 other tissues.
DR ExpressionAtlas; P00167; baseline and differential.
DR Genevisible; P00167; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; TAS:ProtInc.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR Pfam; PF00173; Cyt-b5; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Disease variant; Electron transport;
KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2752049,
FT ECO:0000269|PubMed:4030743, ECO:0000269|PubMed:4770377,
FT ECO:0000269|PubMed:4993957, ECO:0000269|PubMed:5062820"
FT CHAIN 2..134
FT /note="Cytochrome b5"
FT /id="PRO_0000166010"
FT TRANSMEM 109..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 9..85
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 44
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 BINDING 68
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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:2752049"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56395"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56395"
FT VAR_SEQ 86..95
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_045367"
FT VAR_SEQ 98
FT /note="T -> P (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1712589"
FT /id="VSP_001240"
FT VAR_SEQ 99..134
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1712589"
FT /id="VSP_001241"
FT VARIANT 27..134
FT /note="Missing (in METAG)"
FT /evidence="ECO:0000269|PubMed:20080843"
FT /id="VAR_080833"
FT VARIANT 44
FT /note="H -> L (in METAG; dbSNP:rs1555688659)"
FT /evidence="ECO:0000269|PubMed:22170710"
FT /id="VAR_080834"
FT CONFLICT 2..4
FT /note="Missing (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 4
FT /note="Q -> E (in Ref. 13; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 15..18
FT /note="EEIQ -> QEIE (in Ref. 10; AA sequence, 11; AA
FT sequence and 12; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="Missing (in Ref. 12; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="R -> W (in Ref. 4; CA771478)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="N -> D (in Ref. 10; AA sequence, 11; AA sequence and
FT 12; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 89..91
FT /note="RPK -> KPR (in Ref. 9; AA sequence, 10; AA sequence,
FT 11; AA sequence and 12; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="A -> V (in Ref. 13; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2I96"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:2I96"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:2I96"
FT STRAND 25..36
FT /evidence="ECO:0007829|PDB:2I96"
FT TURN 38..43
FT /evidence="ECO:0007829|PDB:2I96"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:2I96"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:2I96"
FT HELIX 61..65
FT /evidence="ECO:0007829|PDB:2I96"
FT HELIX 70..75
FT /evidence="ECO:0007829|PDB:2I96"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:2I96"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:2I96"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:2I96"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:2I96"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:2I96"
SQ SEQUENCE 134 AA; 15330 MW; B6AD2AB747555048 CRC64;
MAEQSDEAVK YYTLEEIQKH NHSKSTWLIL HHKVYDLTKF LEEHPGGEEV LREQAGGDAT
ENFEDVGHST DAREMSKTFI IGELHPDDRP KLNKPPETLI TTIDSSSSWW TNWVIPAISA
VAVALMYRLY MAED
