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   27-MAR-2024, entry version 229.
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; 144.
DR   IntAct; P00167; 23.
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   GlyGen; P00167; 1 site, 1 O-linked glycan (1 site).
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; 9606-ENSP00000341625; -.
DR   PeptideAtlas; P00167; -.
DR   ProteomicsDB; 31960; -.
DR   ProteomicsDB; 51226; -. [P00167-1]
DR   ProteomicsDB; 51227; -. [P00167-2]
DR   Pumba; P00167; -.
DR   TopDownProteomics; P00167-1; -. [P00167-1]
DR   TopDownProteomics; P00167-3; -. [P00167-3]
DR   Antibodypedia; 23308; 406 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   AGR; HGNC:2570; -.
DR   CTD; 1528; -.
DR   DisGeNET; 1528; -.
DR   GeneCards; CYB5A; -.
DR   HGNC; HGNC:2570; CYB5A.
DR   HPA; ENSG00000166347; Tissue enhanced (liver).
DR   MalaCards; CYB5A; -.
DR   MIM; 250790; phenotype.
DR   MIM; 613218; gene.
DR   neXtProt; NX_P00167; -.
DR   OpenTargets; ENSG00000166347; -.
DR   Orphanet; 90796; 46,XY difference 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; FLNWILP; -.
DR   OrthoDB; 2712490at2759; -.
DR   PhylomeDB; P00167; -.
DR   TreeFam; TF314537; -.
DR   BioCyc; MetaCyc:ENSG00000166347-MONOMER; -.
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; 18 hits in 1167 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 209 other cell types or tissues.
DR   ExpressionAtlas; P00167; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
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; IBA:GO_Central.
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; Cytochrome b5-like heme/steroid binding domain; 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   PANTHER; PTHR19359; CYTOCHROME B5; 1.
DR   PANTHER; PTHR19359:SF126; CYTOCHROME B5; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   PRINTS; PR00363; CYTOCHROMEB5.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR   Genevisible; P00167; HS.
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
//