NB5R4_HUMAN
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 03-AUG-2022, entry version 144.
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/";
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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; 18.
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; Q7L1T6; -.
DR PeptideAtlas; Q7L1T6; -.
DR PRIDE; Q7L1T6; -.
DR ProteomicsDB; 68750; -.
DR TopDownProteomics; Q7L1T6; -.
DR Antibodypedia; 18533; 157 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 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; DFNHDSF; -.
DR OrthoDB; 1311668at2759; -.
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; 210 hits in 1085 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 179 other tissues.
DR ExpressionAtlas; Q7L1T6; baseline and differential.
DR Genevisible; Q7L1T6; HS.
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; cd06490; p23_NCB5OR; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR Gene3D; 3.10.120.10; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR001834; CBR-like.
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; PTHR19370; PTHR19370; 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; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR SUPFAM; SSF63380; SSF63380; 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.
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
