IRF4_HUMAN
ID IRF4_HUMAN Reviewed; 451 AA.
AC Q15306; Q5VUI7; Q99660;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Interferon regulatory factor 4;
DE Short=IRF-4;
DE AltName: Full=Lymphocyte-specific interferon regulatory factor;
DE Short=LSIRF;
DE AltName: Full=Multiple myeloma oncogene 1;
DE AltName: Full=NF-EM5;
GN Name=IRF4; Synonyms=MUM1;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Spleen;
RX PubMed=8921401; DOI=10.1006/geno.1996.0547;
RA Grossman A., Mittrucker H.W., Nicholl J., Suzuki A., Chung S., Antonio L.,
RA Sugga S., Sutherland G.R., Siderovski D.P., Mak T.W.;
RT "Cloning of human lymphocyte-specific interferon regulatory factor
RT (hLSIRF/hIRF4) and mapping of the gene to 6p23-p25.";
RL Genomics 37:229-233(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INVOLVEMENT IN MULTIPLE
RP MYELOMA.
RC TISSUE=Spleen;
RX PubMed=9326949; DOI=10.1038/ng1097-226;
RA Iida S., Rao P.H., Butler M., Corradini P., Boccadoro M., Klein B.,
RA Chaganti R.S.K., Dalla-Favera R.;
RT "Deregulation of MUM1/IRF4 by chromosomal translocation in multiple
RT myeloma.";
RL Nat. Genet. 17:226-230(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [5]
RP INTERACTION WITH SPIB.
RX PubMed=10196196; DOI=10.1074/jbc.274.16.11115;
RA Rao S., Matsumura A., Yoon J., Simon M.C.;
RT "SPI-B activates transcription via a unique proline, serine, and threonine
RT domain and exhibits DNA binding affinity differences from PU.1.";
RL J. Biol. Chem. 274:11115-11124(1999).
RN [6]
RP INTERACTION WITH DEF6.
RC TISSUE=Lymph node;
RX PubMed=12651066; DOI=10.1016/s0198-8859(03)00024-7;
RA Gupta S., Lee A.E., Hu C., Fanzo J.C., Goldberg I., Cattoretti G.,
RA Pernis A.B.;
RT "Molecular cloning of IBP, a SWAP-70 homologous GEF, which is highly
RT expressed in the immune system.";
RL Hum. Immunol. 64:389-401(2003).
RN [7]
RP POLYMORPHISM.
RX PubMed=18483556; DOI=10.1371/journal.pgen.1000074;
RA Han J., Kraft P., Nan H., Guo Q., Chen C., Qureshi A., Hankinson S.E.,
RA Hu F.B., Duffy D.L., Zhao Z.Z., Martin N.G., Montgomery G.W., Hayward N.K.,
RA Thomas G., Hoover R.N., Chanock S., Hunter D.J.;
RT "A genome-wide association study identifies novel alleles associated with
RT hair color and skin pigmentation.";
RL PLoS Genet. 4:E1000074-E1000074(2008).
RN [8]
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 [9]
RP POLYMORPHISM.
RX PubMed=24267888; DOI=10.1016/j.cell.2013.10.022;
RA Praetorius C., Grill C., Stacey S.N., Metcalf A.M., Gorkin D.U.,
RA Robinson K.C., Van Otterloo E., Kim R.S., Bergsteinsdottir K.,
RA Ogmundsdottir M.H., Magnusdottir E., Mishra P.J., Davis S.R., Guo T.,
RA Zaidi M.R., Helgason A.S., Sigurdsson M.I., Meltzer P.S., Merlino G.,
RA Petit V., Larue L., Loftus S.K., Adams D.R., Sobhiafshar U., Emre N.C.,
RA Pavan W.J., Cornell R., Smith A.G., McCallion A.S., Fisher D.E.,
RA Stefansson K., Sturm R.A., Steingrimsson E.;
RT "A polymorphism in IRF4 affects human pigmentation through a tyrosinase-
RT dependent MITF/TFAP2A pathway.";
RL Cell 155:1022-1033(2013).
RN [10]
RP STRUCTURE BY NMR OF 22-130.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the IRF domain of human interferon regulator factor
RT 4.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: Transcriptional activator. Binds to the interferon-stimulated
CC response element (ISRE) of the MHC class I promoter. Binds the
CC immunoglobulin lambda light chain enhancer, together with PU.1.
CC Probably plays a role in ISRE-targeted signal transduction mechanisms
CC specific to lymphoid cells. Involved in CD8(+) dendritic cell
CC differentiation by forming a complex with the BATF-JUNB heterodimer in
CC immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-
CC 3'), an immune-specific regulatory element, followed by cooperative
CC binding of BATF and IRF4 and activation of genes (By similarity).
CC {ECO:0000250|UniProtKB:Q64287}.
CC -!- SUBUNIT: Interacts with the BATF-JUNB heterodimer. Interacts with BATF
CC (via bZIP domain); the interaction is direct (By similarity). Interacts
CC with SPIB and DEF6. Directly interacts with NLRP3 in the nucleus of Th2
CC cells; this interaction enhances IRF4 ability to bind to the IL4
CC promoter and is required for optimal IRF4-dependent IL4 transcription
CC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q64287,
CC ECO:0000269|PubMed:10196196, ECO:0000269|PubMed:12651066}.
CC -!- INTERACTION:
CC Q15306; O95163: ELP1; NbExp=2; IntAct=EBI-751345, EBI-347559;
CC Q15306; Q8TF65: GIPC2; NbExp=5; IntAct=EBI-751345, EBI-712067;
CC Q15306; P51617: IRAK1; NbExp=2; IntAct=EBI-751345, EBI-358664;
CC Q15306; Q86UE8: TLK2; NbExp=2; IntAct=EBI-751345, EBI-1047967;
CC Q15306; Q7Z6J9: TSEN54; NbExp=3; IntAct=EBI-751345, EBI-2559824;
CC Q15306; Q9H6S0: YTHDC2; NbExp=2; IntAct=EBI-751345, EBI-1057466;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15306-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15306-2; Sequence=VSP_002755;
CC -!- TISSUE SPECIFICITY: Lymphoid cells.
CC -!- INDUCTION: Not induced by interferons.
CC -!- PTM: Phosphorylation by ROCK2 regulates IL-17 and IL-21 production.
CC {ECO:0000250}.
CC -!- POLYMORPHISM: Genetic variants in IRF4 define the skin/hair/eye
CC pigmentation variation locus 8 (SHEP8) [MIM:611724]. Hair, eye and skin
CC pigmentation are among the most visible examples of human phenotypic
CC variation, with a broad normal range that is subject to substantial
CC geographic stratification. In the case of skin, individuals tend to
CC have lighter pigmentation with increasing distance from the equator. By
CC contrast, the majority of variation in human eye and hair color is
CC found among individuals of European ancestry, with most other human
CC populations fixed for brown eyes and black hair.
CC {ECO:0000269|PubMed:18483556, ECO:0000269|PubMed:24267888}.
CC -!- DISEASE: Multiple myeloma (MM) [MIM:254500]: A malignant tumor of
CC plasma cells usually arising in the bone marrow and characterized by
CC diffuse involvement of the skeletal system, hyperglobulinemia, Bence-
CC Jones proteinuria and anemia. Complications of multiple myeloma are
CC bone pain, hypercalcemia, renal failure and spinal cord compression.
CC The aberrant antibodies that are produced lead to impaired humoral
CC immunity and patients have a high prevalence of infection. Amyloidosis
CC may develop in some patients. Multiple myeloma is part of a spectrum of
CC diseases ranging from monoclonal gammopathy of unknown significance
CC (MGUS) to plasma cell leukemia. {ECO:0000269|PubMed:9326949}. Note=The
CC gene represented in this entry may be involved in disease pathogenesis.
CC A chromosomal aberration involving IRF4 has been found in multiple
CC myeloma. Translocation t(6;14)(p25;q32) with the IgH locus.
CC -!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
CC ProRule:PRU00840}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/IRF4ID231ch6p25.html";
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DR EMBL; U52682; AAC50779.1; -; mRNA.
DR EMBL; U63738; AAB37258.1; -; mRNA.
DR EMBL; AL365272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL589962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015752; AAH15752.1; -; mRNA.
DR CCDS; CCDS4469.1; -. [Q15306-1]
DR RefSeq; NP_001182215.1; NM_001195286.1. [Q15306-2]
DR RefSeq; NP_002451.2; NM_002460.3. [Q15306-1]
DR PDB; 2DLL; NMR; -; A=23-130.
DR PDB; 6TD4; X-ray; 1.71 A; A=20-132.
DR PDB; 7JM4; X-ray; 2.95 A; A/B/G/H=21-129.
DR PDB; 7O56; X-ray; 2.60 A; A/B/C=20-139.
DR PDBsum; 2DLL; -.
DR PDBsum; 6TD4; -.
DR PDBsum; 7JM4; -.
DR PDBsum; 7O56; -.
DR AlphaFoldDB; Q15306; -.
DR SMR; Q15306; -.
DR BioGRID; 109870; 77.
DR IntAct; Q15306; 68.
DR STRING; 9606.ENSP00000370343; -.
DR iPTMnet; Q15306; -.
DR PhosphoSitePlus; Q15306; -.
DR BioMuta; IRF4; -.
DR DMDM; 2497445; -.
DR jPOST; Q15306; -.
DR MassIVE; Q15306; -.
DR MaxQB; Q15306; -.
DR PaxDb; Q15306; -.
DR PeptideAtlas; Q15306; -.
DR PRIDE; Q15306; -.
DR ProteomicsDB; 60524; -. [Q15306-1]
DR ProteomicsDB; 60525; -. [Q15306-2]
DR Antibodypedia; 1057; 697 antibodies from 47 providers.
DR DNASU; 3662; -.
DR Ensembl; ENST00000380956.9; ENSP00000370343.4; ENSG00000137265.15. [Q15306-1]
DR GeneID; 3662; -.
DR KEGG; hsa:3662; -.
DR MANE-Select; ENST00000380956.9; ENSP00000370343.4; NM_002460.4; NP_002451.2.
DR UCSC; uc003msz.5; human. [Q15306-1]
DR CTD; 3662; -.
DR DisGeNET; 3662; -.
DR GeneCards; IRF4; -.
DR HGNC; HGNC:6119; IRF4.
DR HPA; ENSG00000137265; Tissue enhanced (bone marrow, cervix, lymphoid tissue).
DR MalaCards; IRF4; -.
DR MIM; 254500; phenotype.
DR MIM; 601900; gene.
DR MIM; 611724; phenotype.
DR neXtProt; NX_Q15306; -.
DR OpenTargets; ENSG00000137265; -.
DR Orphanet; 3452; Whipple disease.
DR PharmGKB; PA29918; -.
DR VEuPathDB; HostDB:ENSG00000137265; -.
DR eggNOG; ENOG502QUE4; Eukaryota.
DR GeneTree; ENSGT00940000159059; -.
DR InParanoid; Q15306; -.
DR OMA; CPVTFGH; -.
DR OrthoDB; 648909at2759; -.
DR PhylomeDB; Q15306; -.
DR TreeFam; TF328512; -.
DR PathwayCommons; Q15306; -.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR SignaLink; Q15306; -.
DR SIGNOR; Q15306; -.
DR BioGRID-ORCS; 3662; 35 hits in 1098 CRISPR screens.
DR ChiTaRS; IRF4; human.
DR EvolutionaryTrace; Q15306; -.
DR GeneWiki; IRF4; -.
DR GenomeRNAi; 3662; -.
DR Pharos; Q15306; Tbio.
DR PRO; PR:Q15306; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q15306; protein.
DR Bgee; ENSG00000137265; Expressed in lymph node and 130 other tissues.
DR ExpressionAtlas; Q15306; baseline and differential.
DR Genevisible; Q15306; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000786; C:nucleosome; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0042832; P:defense response to protozoan; ISS:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; IEA:Ensembl.
DR GO; GO:0043967; P:histone H4 acetylation; IEA:Ensembl.
DR GO; GO:0002376; P:immune system process; IBA:GO_Central.
DR GO; GO:0043011; P:myeloid dendritic cell differentiation; IEA:Ensembl.
DR GO; GO:0034122; P:negative regulation of toll-like receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:UniProtKB.
DR GO; GO:0032736; P:positive regulation of interleukin-13 production; IDA:UniProtKB.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IDA:UniProtKB.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045622; P:regulation of T-helper cell differentiation; NAS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0042110; P:T cell activation; NAS:UniProtKB.
DR GO; GO:0072540; P:T-helper 17 cell lineage commitment; ISS:UniProtKB.
DR CDD; cd00103; IRF; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.60.200.10; -; 1.
DR InterPro; IPR019817; Interferon_reg_fac_CS.
DR InterPro; IPR001346; Interferon_reg_fact_DNA-bd_dom.
DR InterPro; IPR019471; Interferon_reg_factor-3.
DR InterPro; IPR017855; SMAD-like_dom_sf.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00605; IRF; 1.
DR Pfam; PF10401; IRF-3; 1.
DR PRINTS; PR00267; INTFRNREGFCT.
DR SMART; SM00348; IRF; 1.
DR SMART; SM01243; IRF-3; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS00601; IRF_1; 1.
DR PROSITE; PS51507; IRF_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Chromosomal rearrangement;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..451
FT /note="Interferon regulatory factor 4"
FT /id="PRO_0000154556"
FT DNA_BIND 21..129
FT /note="IRF tryptophan pentad repeat"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00840"
FT MOD_RES 447
FT /note="Phosphoserine; by ROCK2"
FT /evidence="ECO:0000250|UniProtKB:Q64287"
FT MOD_RES 448
FT /note="Phosphoserine; by ROCK2"
FT /evidence="ECO:0000250|UniProtKB:Q64287"
FT VAR_SEQ 165
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8921401"
FT /id="VSP_002755"
FT CONFLICT 300
FT /note="Q -> H (in Ref. 2; AAB37258)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="K -> N (in Ref. 2; AAB37258)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="R -> T (in Ref. 2; AAB37258)"
FT /evidence="ECO:0000305"
FT HELIX 24..34
FT /evidence="ECO:0007829|PDB:6TD4"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2DLL"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:6TD4"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:6TD4"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:6TD4"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:7O56"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:2DLL"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:6TD4"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:6TD4"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:6TD4"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:6TD4"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:6TD4"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:6TD4"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:6TD4"
SQ SEQUENCE 451 AA; 51772 MW; 17CD1327C6F5BFFA CRC64;
MNLEGGGRGG EFGMSAVSCG NGKLRQWLID QIDSGKYPGL VWENEEKSIF RIPWKHAGKQ
DYNREEDAAL FKAWALFKGK FREGIDKPDP PTWKTRLRCA LNKSNDFEEL VERSQLDISD
PYKVYRIVPE GAKKGAKQLT LEDPQMSMSH PYTMTTPYPS LPAQQVHNYM MPPLDRSWRD
YVPDQPHPEI PYQCPMTFGP RGHHWQGPAC ENGCQVTGTF YACAPPESQA PGVPTEPSIR
SAEALAFSDC RLHICLYYRE ILVKELTTSS PEGCRISHGH TYDASNLDQV LFPYPEDNGQ
RKNIEKLLSH LERGVVLWMA PDGLYAKRLC QSRIYWDGPL ALCNDRPNKL ERDQTCKLFD
TQQFLSELQA FAHHGRSLPR FQVTLCFGEE FPDPQRQRKL ITAHVEPLLA RQLYYFAQQN
SGHFLRGYDL PEHISNPEDY HRSIRHSSIQ E
