ID NB5R4_HUMAN Reviewed; 521 AA. AC Q7L1T6; B1AEM2; Q5TGI9; Q9NUE4; Q9UHI9; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2005, sequence version 1. DT 27-MAR-2024, entry version 153. DE RecName: Full=Cytochrome b5 reductase 4 {ECO:0000305}; DE EC=1.6.2.2 {ECO:0000305|PubMed:10611283}; DE AltName: Full=Flavohemoprotein b5/b5R; DE Short=b5+b5R; DE AltName: Full=N-terminal cytochrome b5 and cytochrome b5 oxidoreductase domain-containing protein; DE AltName: Full=cb5/cb5R; GN Name=CYB5R4 {ECO:0000312|HGNC:HGNC:20147}; Synonyms=NCB5OR; 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 [GENOMIC DNA], AND VARIANTS HIS-140; ALA-267 AND RP SER-316. RG SeattleSNPs variation discovery resource; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-521, CATALYTIC ACTIVITY, SUBCELLULAR RP LOCATION, HEME-BINDING, FAD-BINDING, AND TISSUE SPECIFICITY. RX PubMed=10611283; DOI=10.1073/pnas.96.26.14742; RA Zhu H., Qiu H., Yoon H.-W., Huang S., Bunn H.F.; RT "Identification of a cytochrome b-type NAD(P)H oxidoreductase ubiquitously RT expressed in human cells."; RL Proc. Natl. Acad. Sci. U.S.A. 96:14742-14747(1999). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 51-137, AND HEME-BINDING SITES. RX PubMed=20630863; DOI=10.1074/jbc.m110.120329; RA Deng B., Parthasarathy S., Wang W., Gibney B.R., Battaile K.P., Lovell S., RA Benson D.R., Zhu H.; RT "Study of the individual cytochrome b5 and cytochrome b5 reductase domains RT of Ncb5or reveals a unique heme pocket and a possible role of the CS RT domain."; RL J. Biol. Chem. 285:30181-30191(2010). RN [7] RP VARIANTS ARG-187 AND ARG-223. RX PubMed=15504981; DOI=10.2337/diabetes.53.11.2992; RA Andersen G., Wegner L., Rose C.S., Xie J., Zhu H., Larade K., Johansen A., RA Ek J., Lauenborg J., Drivsholm T., Borch-Johnsen K., Damm P., Hansen T., RA Bunn H.F., Pedersen O.; RT "Variation in NCB5OR: studies of relationships to type 2 diabetes, RT maturity-onset diabetes of the young, and gestational diabetes mellitus."; RL Diabetes 53:2992-2997(2004). RN [8] RP SUBCELLULAR LOCATION. RX PubMed=15131110; DOI=10.1074/jbc.m402664200; RA Zhu H., Larade K., Jackson T.A., Xie J., Ladoux A., Acker H., RA Berchner-Pfannschmidt U., Fandrey J., Cross A.R., Lukat-Rodgers G.S., RA Rodgers K.R., Bunn H.F.; RT "NCB5OR is a novel soluble NAD(P)H reductase localized in the endoplasmic RT reticulum."; RL J. Biol. Chem. 279:30316-30325(2004). RN [9] RP VARIANTS [LARGE SCALE ANALYSIS] TYR-371 AND MET-390. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: NADH-cytochrome b5 reductase involved in endoplasmic CC reticulum stress response pathway. Plays a critical role in protecting CC pancreatic beta-cells against oxidant stress, possibly by protecting CC the cell from excess buildup of reactive oxygen species (ROS). Reduces CC a variety of substrates in vitro, such as cytochrome c, feericyanide CC and methemoglobin. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + CC H(+) + NAD(+); Xref=Rhea:RHEA:46680, Rhea:RHEA-COMP:10438, Rhea:RHEA- CC COMP:10439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.2.2; CC Evidence={ECO:0000305|PubMed:10611283}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000269|PubMed:10611283}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=25 mM for O(2); CC Redox potential: CC E(0) is -108 mV.; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum CC {ECO:0000269|PubMed:10611283, ECO:0000269|PubMed:15131110}. CC Note=Soluble protein. CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10611283}. CC -!- POLYMORPHISM: Variants Arg-187 and Arg-223 do not influence the CC pathogenesis of non-autoimmune diabetes. {ECO:0000269|PubMed:15504981}. CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome CC reductase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF04812.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/cyb5r4/"; 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; EU448291; ACA06109.1; -; Genomic_DNA. DR EMBL; AL034347; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL139232; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC025380; AAH25380.2; -; mRNA. DR EMBL; AF169803; AAF04812.1; ALT_INIT; mRNA. DR CCDS; CCDS5000.2; -. DR RefSeq; NP_057314.2; NM_016230.3. DR PDB; 3LF5; X-ray; 1.25 A; A/B=51-137. DR PDB; 6MV1; X-ray; 2.15 A; A=164-521. DR PDB; 6MV2; X-ray; 2.05 A; A=164-521. DR PDBsum; 3LF5; -. DR PDBsum; 6MV1; -. DR PDBsum; 6MV2; -. DR AlphaFoldDB; Q7L1T6; -. DR SMR; Q7L1T6; -. DR BioGRID; 119347; 19. DR IntAct; Q7L1T6; 1. DR STRING; 9606.ENSP00000358695; -. DR iPTMnet; Q7L1T6; -. DR PhosphoSitePlus; Q7L1T6; -. DR BioMuta; CYB5R4; -. DR EPD; Q7L1T6; -. DR jPOST; Q7L1T6; -. DR MassIVE; Q7L1T6; -. DR MaxQB; Q7L1T6; -. DR PaxDb; 9606-ENSP00000358695; -. DR PeptideAtlas; Q7L1T6; -. DR ProteomicsDB; 68750; -. DR Pumba; Q7L1T6; -. DR TopDownProteomics; Q7L1T6; -. DR Antibodypedia; 18533; 178 antibodies from 30 providers. DR DNASU; 51167; -. DR Ensembl; ENST00000369681.10; ENSP00000358695.3; ENSG00000065615.14. DR GeneID; 51167; -. DR KEGG; hsa:51167; -. DR MANE-Select; ENST00000369681.10; ENSP00000358695.3; NM_016230.4; NP_057314.2. DR UCSC; uc003pkf.4; human. DR AGR; HGNC:20147; -. DR CTD; 51167; -. DR DisGeNET; 51167; -. DR GeneCards; CYB5R4; -. DR HGNC; HGNC:20147; CYB5R4. DR HPA; ENSG00000065615; Low tissue specificity. DR MIM; 608343; gene. DR neXtProt; NX_Q7L1T6; -. DR OpenTargets; ENSG00000065615; -. DR PharmGKB; PA134904907; -. DR VEuPathDB; HostDB:ENSG00000065615; -. DR eggNOG; KOG0534; Eukaryota. DR eggNOG; KOG0536; Eukaryota. DR GeneTree; ENSGT00940000155536; -. DR HOGENOM; CLU_003827_0_2_1; -. DR InParanoid; Q7L1T6; -. DR OMA; WIRLCNS; -. DR OrthoDB; 163533at2759; -. DR PhylomeDB; Q7L1T6; -. DR TreeFam; TF313874; -. DR BRENDA; 1.6.2.2; 2681. DR PathwayCommons; Q7L1T6; -. DR Reactome; R-HSA-1237044; Erythrocytes take up carbon dioxide and release oxygen. DR SignaLink; Q7L1T6; -. DR BioGRID-ORCS; 51167; 212 hits in 1163 CRISPR screens. DR ChiTaRS; CYB5R4; human. DR EvolutionaryTrace; Q7L1T6; -. DR GeneWiki; CYB5R4; -. DR GenomeRNAi; 51167; -. DR Pharos; Q7L1T6; Tbio. DR PRO; PR:Q7L1T6; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q7L1T6; Protein. DR Bgee; ENSG00000065615; Expressed in monocyte and 181 other cell types or tissues. DR ExpressionAtlas; Q7L1T6; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IDA:UniProtKB. DR GO; GO:0020037; F:heme binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IDA:UniProtKB. DR GO; GO:0016653; F:oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor; IDA:UniProtKB. DR GO; GO:0015701; P:bicarbonate transport; TAS:Reactome. DR GO; GO:0048468; P:cell development; ISS:UniProtKB. DR GO; GO:0003032; P:detection of oxygen; NAS:UniProtKB. DR GO; GO:0006091; P:generation of precursor metabolites and energy; IDA:UniProtKB. DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB. DR GO; GO:0030073; P:insulin secretion; ISS:UniProtKB. DR GO; GO:0072593; P:reactive oxygen species metabolic process; IDA:UniProtKB. DR GO; GO:0046677; P:response to antibiotic; ISS:UniProtKB. DR GO; GO:0006801; P:superoxide metabolic process; IDA:UniProtKB. DR CDD; cd06183; cyt_b5_reduct_like; 1. DR CDD; cd06490; p23_NCB5OR; 1. DR Gene3D; 2.60.40.790; -; 1. DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1. DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1. DR Gene3D; 2.40.30.10; Translation factors; 1. DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom. DR InterPro; IPR007052; CS_dom. 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 InterPro; IPR017927; FAD-bd_FR_type. DR InterPro; IPR039261; FNR_nucleotide-bd. DR InterPro; IPR008978; HSP20-like_chaperone. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR037908; p23_NCB5OR. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR PANTHER; PTHR46237:SF1; CYTOCHROME B5 REDUCTASE 4; 1. DR PANTHER; PTHR46237; CYTOCHROME B5 REDUCTASE 4 FAMILY MEMBER; 1. DR Pfam; PF04969; CS; 1. DR Pfam; PF00173; Cyt-b5; 1. DR Pfam; PF00970; FAD_binding_6; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PRINTS; PR00406; CYTB5RDTASE. DR PRINTS; PR00363; CYTOCHROMEB5. DR SMART; SM01117; Cyt-b5; 1. DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1. DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1. DR SUPFAM; SSF49764; HSP20-like chaperones; 1. DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1. DR PROSITE; PS51203; CS; 1. DR PROSITE; PS00191; CYTOCHROME_B5_1; 1. DR PROSITE; PS50255; CYTOCHROME_B5_2; 1. DR PROSITE; PS51384; FAD_FR; 1. DR Genevisible; Q7L1T6; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Endoplasmic reticulum; FAD; Flavoprotein; Heme; KW Iron; Metal-binding; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1..521 FT /note="Cytochrome b5 reductase 4" FT /id="PRO_0000287556" FT DOMAIN 54..130 FT /note="Cytochrome b5 heme-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279" FT DOMAIN 165..256 FT /note="CS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547" FT DOMAIN 273..385 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716" FT REGION 1..27 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..21 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 89 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 112 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 365..380 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT BINDING 392..424 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT VARIANT 140 FT /note="R -> H (in dbSNP:rs61762820)" FT /evidence="ECO:0000269|Ref.1" FT /id="VAR_047967" FT VARIANT 187 FT /note="Q -> R (in dbSNP:rs143478181)" FT /evidence="ECO:0000269|PubMed:15504981" FT /id="VAR_032323" FT VARIANT 223 FT /note="H -> R (in dbSNP:rs141290525)" FT /evidence="ECO:0000269|PubMed:15504981" FT /id="VAR_032324" FT VARIANT 267 FT /note="P -> A (in dbSNP:rs61382555)" FT /evidence="ECO:0000269|Ref.1" FT /id="VAR_047968" FT VARIANT 282 FT /note="S -> P (in dbSNP:rs10080628)" FT /id="VAR_032325" FT VARIANT 316 FT /note="P -> S (in dbSNP:rs10080628)" FT /evidence="ECO:0000269|Ref.1" FT /id="VAR_047969" FT VARIANT 371 FT /note="D -> Y (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036240" FT VARIANT 390 FT /note="L -> M (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036241" FT STRAND 53..57 FT /evidence="ECO:0007829|PDB:3LF5" FT HELIX 59..64 FT /evidence="ECO:0007829|PDB:3LF5" FT STRAND 70..75 FT /evidence="ECO:0007829|PDB:3LF5" FT STRAND 78..81 FT /evidence="ECO:0007829|PDB:3LF5" FT HELIX 83..85 FT /evidence="ECO:0007829|PDB:3LF5" FT TURN 86..88 FT /evidence="ECO:0007829|PDB:3LF5" FT HELIX 93..97 FT /evidence="ECO:0007829|PDB:3LF5" FT TURN 98..101 FT /evidence="ECO:0007829|PDB:3LF5" FT HELIX 105..112 FT /evidence="ECO:0007829|PDB:3LF5" FT HELIX 117..120 FT /evidence="ECO:0007829|PDB:3LF5" FT HELIX 122..124 FT /evidence="ECO:0007829|PDB:3LF5" FT STRAND 125..129 FT /evidence="ECO:0007829|PDB:3LF5" FT HELIX 133..136 FT /evidence="ECO:0007829|PDB:3LF5" FT STRAND 169..174 FT /evidence="ECO:0007829|PDB:6MV2" FT STRAND 176..184 FT /evidence="ECO:0007829|PDB:6MV2" FT STRAND 194..199 FT /evidence="ECO:0007829|PDB:6MV2" FT STRAND 201..210 FT /evidence="ECO:0007829|PDB:6MV2" FT STRAND 213..223 FT /evidence="ECO:0007829|PDB:6MV2" FT STRAND 230..234 FT /evidence="ECO:0007829|PDB:6MV2" FT TURN 235..238 FT /evidence="ECO:0007829|PDB:6MV2" FT STRAND 239..248 FT /evidence="ECO:0007829|PDB:6MV2" FT STRAND 253..258 FT /evidence="ECO:0007829|PDB:6MV2" FT TURN 260..263 FT /evidence="ECO:0007829|PDB:6MV2" FT STRAND 264..267 FT /evidence="ECO:0007829|PDB:6MV2" FT HELIX 268..270 FT /evidence="ECO:0007829|PDB:6MV2" FT STRAND 275..296 FT /evidence="ECO:0007829|PDB:6MV2" FT STRAND 310..317 FT /evidence="ECO:0007829|PDB:6MV2" FT STRAND 320..326 FT /evidence="ECO:0007829|PDB:6MV2" FT TURN 335..337 FT /evidence="ECO:0007829|PDB:6MV2" FT STRAND 347..353 FT /evidence="ECO:0007829|PDB:6MV2" FT HELIX 360..366 FT /evidence="ECO:0007829|PDB:6MV2" FT STRAND 372..376 FT /evidence="ECO:0007829|PDB:6MV2" FT HELIX 384..387 FT /evidence="ECO:0007829|PDB:6MV2" FT STRAND 392..398 FT /evidence="ECO:0007829|PDB:6MV2" FT HELIX 399..402 FT /evidence="ECO:0007829|PDB:6MV2" FT HELIX 403..414 FT /evidence="ECO:0007829|PDB:6MV2" FT STRAND 421..430 FT /evidence="ECO:0007829|PDB:6MV2" FT HELIX 431..433 FT /evidence="ECO:0007829|PDB:6MV2" FT HELIX 437..445 FT /evidence="ECO:0007829|PDB:6MV2" FT STRAND 450..458 FT /evidence="ECO:0007829|PDB:6MV2" FT STRAND 465..468 FT /evidence="ECO:0007829|PDB:6MV2" FT HELIX 472..478 FT /evidence="ECO:0007829|PDB:6MV2" FT STRAND 488..495 FT /evidence="ECO:0007829|PDB:6MV2" FT HELIX 496..508 FT /evidence="ECO:0007829|PDB:6MV2" FT HELIX 513..515 FT /evidence="ECO:0007829|PDB:6MV2" FT STRAND 516..519 FT /evidence="ECO:0007829|PDB:6MV2" SQ SEQUENCE 521 AA; 59474 MW; 9D83BAB387E3B0F4 CRC64; MLNVPSQSFP APRSQQRVAS GGRSKVPLKQ GRSLMDWIRL TKSGKDLTGL KGRLIEVTEE ELKKHNKKDD CWICIRGFVY NVSPYMEYHP GGEDELMRAA GSDGTELFDQ VHRWVNYESM LKECLVGRMA IKPAVLKDYR EEEKKVLNGM LPKSQVTDTL AKEGPSYPSY DWFQTDSLVT IAIYTKQKDI NLDSIIVDHQ NDSFRAETII KDCLYLIHIG LSHEVQEDFS VRVVESVGKI EIVLQKKENT SWDFLGHPLK NHNSLIPRKD TGLYYRKCQL ISKEDVTHDT RLFCLMLPPS THLQVPIGQH VYLKLPITGT EIVKPYTPVS GSLLSEFKEP VLPNNKYIYF LIKIYPTGLF TPELDRLQIG DFVSVSSPEG NFKISKFQEL EDLFLLAAGT GFTPMVKILN YALTDIPSLR KVKLMFFNKT EDDIIWRSQL EKLAFKDKRL DVEFVLSAPI SEWNGKQGHI SPALLSEFLK RNLDKSKVLV CICGPVPFTE QGVRLLHDLN FSKNEIHSFT A //