WDR5_MOUSE
ID WDR5_MOUSE Reviewed; 334 AA.
AC P61965; Q91VA5; Q922C9; Q9NWX7; Q9UGP9;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=WD repeat-containing protein 5;
DE AltName: Full=BMP2-induced 3-kb gene protein;
DE AltName: Full=WD repeat-containing protein BIG-3;
GN Name=Wdr5; Synonyms=Big, Big3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=C57BL/6J;
RX PubMed=11551928; DOI=10.1074/jbc.m105757200;
RA Gori F., Divieti P., Demay M.B.;
RT "Cloning and characterization of a novel WD-40 repeat protein that
RT dramatically accelerates osteoblastic differentiation.";
RL J. Biol. Chem. 276:46515-46522(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N;
RC TISSUE=Liver, Mammary tumor, and Salivary gland;
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 TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15860628; DOI=10.1126/science.1107373;
RA Brown S.A., Ripperger J., Kadener S., Fleury-Olela F., Vilbois F.,
RA Rosbash M., Schibler U.;
RT "PERIOD1-associated proteins modulate the negative limb of the mammalian
RT circadian oscillator.";
RL Science 308:693-696(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP IDENTIFICATION IN THE MLL COMPLEX, AND INTERACTION WITH ASH2L; DPY30;
RP KMT2A; KMT2D AND RBBP5.
RX PubMed=21335234; DOI=10.1016/j.cell.2011.01.020;
RA Jiang H., Shukla A., Wang X., Chen W.Y., Bernstein B.E., Roeder R.G.;
RT "Role for Dpy-30 in ES cell-fate specification by regulation of H3K4
RT methylation within bivalent domains.";
RL Cell 144:513-525(2011).
RN [7]
RP INTERACTION WITH ZNF335.
RX PubMed=23178126; DOI=10.1016/j.cell.2012.10.043;
RA Yang Y.J., Baltus A.E., Mathew R.S., Murphy E.A., Evrony G.D.,
RA Gonzalez D.M., Wang E.P., Marshall-Walker C.A., Barry B.J., Murn J.,
RA Tatarakis A., Mahajan M.A., Samuels H.H., Shi Y., Golden J.A., Mahajnah M.,
RA Shenhav R., Walsh C.A.;
RT "Microcephaly gene links trithorax and REST/NRSF to control neural stem
RT cell proliferation and differentiation.";
RL Cell 151:1097-1112(2012).
RN [8]
RP INTERACTION WITH PAXBP1.
RX PubMed=22862948; DOI=10.1016/j.stem.2012.05.022;
RA Diao Y., Guo X., Li Y., Sun K., Lu L., Jiang L., Fu X., Zhu H., Sun H.,
RA Wang H., Wu Z.;
RT "Pax3/7BP is a Pax7- and Pax3-binding protein that regulates the
RT proliferation of muscle precursor cells by an epigenetic mechanism.";
RL Cell Stem Cell 11:231-241(2012).
CC -!- FUNCTION: Contributes to histone modification (By similarity). May
CC position the N-terminus of histone H3 for efficient trimethylation at
CC 'Lys-4' (By similarity). As part of the MLL1/MLL complex it is involved
CC in methylation and dimethylation at 'Lys-4' of histone H3 (By
CC similarity). H3 'Lys-4' methylation represents a specific tag for
CC epigenetic transcriptional activation (By similarity). As part of the
CC NSL complex it may be involved in acetylation of nucleosomal histone H4
CC on several lysine residues (By similarity). May regulate osteoblasts
CC differentiation (PubMed:11551928). In association with RBBP5 and ASH2L,
CC stimulates the histone methyltransferase activities of KMT2A, KMT2B,
CC KMT2C, KMT2D, SETD1A and SETD1B (By similarity).
CC {ECO:0000250|UniProtKB:P61964, ECO:0000269|PubMed:11551928}.
CC -!- SUBUNIT: Interacts with PAXBP1; the interaction is direct and links a
CC WDR5-containing histone methyltransferase complex to PAX7 and PAX3
CC (PubMed:22862948). Interacts with HCFC1 (By similarity). Component of
CC the ATAC complex, a complex with histone acetyltransferase activity on
CC histones H3 and H4 (By similarity). Component of the SET1 complex, at
CC least composed of the catalytic subunit (SETD1A or SETD1B), WDR5,
CC WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30 (By similarity).
CC Core component of several methyltransferase-containing complexes
CC including MLL1/MLL, MLL2/3 (also named ASCOM complex) and MLL4/WBP7
CC (PubMed:21335234). Each complex is at least composed of ASH2L, RBBP5,
CC WDR5, DPY30, one or more specific histone methyltransferases
CC (KMT2A/MLL1, KMT2D/MLL2, KMT2C/MLL3 and KMT2B/MLL4), and the
CC facultative components PAGR1, BAP18, CHD8, E2F6, HCFC1, HCFC2, HSP70,
CC INO80C, KDM6A, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, MYST1/MOF, NCOA6,
CC PAXIP1/PTIP, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B,
CC SENP3, TAF1, TAF4, TAF6, TAF7, TAF9, TEX10 and alpha- and beta-tubulin
CC (PubMed:21335234). Component of the NSL complex at least composed of
CC MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and
CC HCFC1 (By similarity). Interacts with KMT2A/MLL1 (via WIN motif) and
CC RBBP5; the interaction is direct (By similarity). Component ofthe
CC ADA2A-containing complex (ATAC), composed of KAT14, KAT2A, TADA2L,
CC TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1 (By similarity). In
CC the complex, it probably interacts directly with KAT2A, MBIP and KAT14
CC (By similarity). Interacts with histone H3 (By similarity). Interacts
CC with SETD1A (via WIN motif) (By similarity). Component of a histone
CC methylation complex composed of at least ZNF335, RBBP5, ASH2L and WDR5;
CC the complex may have histone H3-specific methyltransferase activity,
CC however does not have specificity for 'Lys-4' of histone H3 (By
CC similarity). Interacts with ZNF335 (PubMed:23178126). Components of
CC this complex may associate with components of the ZNF335-CCAR2-EMSY
CC nuclear receptor-mediated transcription complex to form a complex at
CC least composed of ZNF335, HCFC1, CCAR2, EMSY, MKI67, RBBP5, ASH2L and
CC WDR5 (By similarity). Interacts with PER1 (By similarity). Interacts
CC with KMT2D (via WIN motif) (PubMed:21335234). Interacts with KMT2B (via
CC WIN motif), KMT2C (via WIN motif) and SETD1B (via WIN motif) (By
CC similarity). {ECO:0000250|UniProtKB:P61964,
CC ECO:0000250|UniProtKB:Q498M4, ECO:0000269|PubMed:21335234,
CC ECO:0000269|PubMed:22862948, ECO:0000269|PubMed:23178126}.
CC -!- INTERACTION:
CC P61965; P20263: Pou5f1; NbExp=7; IntAct=EBI-1247084, EBI-1606219;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15860628}.
CC -!- TISSUE SPECIFICITY: Expressed in liver (at protein level). Detected in
CC brain, testis and kidney. {ECO:0000269|PubMed:15860628}.
CC -!- SIMILARITY: Belongs to the WD repeat WDR5/wds family. {ECO:0000305}.
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DR EMBL; AF416510; AAL27006.1; -; mRNA.
DR EMBL; AK075937; BAC36067.1; -; mRNA.
DR EMBL; BC008547; AAH08547.1; -; mRNA.
DR EMBL; BC016103; AAH16103.1; -; mRNA.
DR EMBL; BC025801; AAH25801.1; -; mRNA.
DR CCDS; CCDS15829.1; -.
DR RefSeq; NP_543124.1; NM_080848.2.
DR RefSeq; XP_006497735.1; XM_006497672.3.
DR PDB; 2XL2; X-ray; 2.40 A; A/B=1-334.
DR PDB; 2XL3; X-ray; 2.70 A; A/B=1-334.
DR PDBsum; 2XL2; -.
DR PDBsum; 2XL3; -.
DR AlphaFoldDB; P61965; -.
DR SMR; P61965; -.
DR BioGRID; 228326; 62.
DR ComplexPortal; CPX-1025; GCN5-containing ATAC complex.
DR ComplexPortal; CPX-1029; PCAF-containing ATAC complex.
DR ComplexPortal; CPX-875; NSL histone acetyltransferase complex.
DR CORUM; P61965; -.
DR DIP; DIP-38618N; -.
DR ELM; P61965; -.
DR IntAct; P61965; 46.
DR MINT; P61965; -.
DR STRING; 10090.ENSMUSP00000109585; -.
DR iPTMnet; P61965; -.
DR PhosphoSitePlus; P61965; -.
DR EPD; P61965; -.
DR MaxQB; P61965; -.
DR PaxDb; P61965; -.
DR PeptideAtlas; P61965; -.
DR PRIDE; P61965; -.
DR ProteomicsDB; 299669; -.
DR Antibodypedia; 31978; 441 antibodies from 42 providers.
DR DNASU; 140858; -.
DR Ensembl; ENSMUST00000113952; ENSMUSP00000109585; ENSMUSG00000026917.
DR GeneID; 140858; -.
DR KEGG; mmu:140858; -.
DR UCSC; uc012bsw.2; mouse.
DR CTD; 11091; -.
DR MGI; MGI:2155884; Wdr5.
DR VEuPathDB; HostDB:ENSMUSG00000026917; -.
DR eggNOG; KOG0266; Eukaryota.
DR GeneTree; ENSGT00940000154143; -.
DR InParanoid; P61965; -.
DR OMA; RLWNYHT; -.
DR OrthoDB; 957291at2759; -.
DR PhylomeDB; P61965; -.
DR TreeFam; TF314125; -.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR Reactome; R-MMU-3214858; RMTs methylate histone arginines.
DR Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-MMU-8951664; Neddylation.
DR BioGRID-ORCS; 140858; 28 hits in 71 CRISPR screens.
DR ChiTaRS; Wdr5; mouse.
DR EvolutionaryTrace; P61965; -.
DR PRO; PR:P61965; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P61965; protein.
DR Bgee; ENSMUSG00000026917; Expressed in secondary oocyte and 250 other tissues.
DR ExpressionAtlas; P61965; baseline and differential.
DR Genevisible; P61965; MM.
DR GO; GO:0140672; C:ATAC complex; IDA:ComplexPortal.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0035097; C:histone methyltransferase complex; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IC:ComplexPortal.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0044665; C:MLL1/2 complex; ISO:MGI.
DR GO; GO:0044666; C:MLL3/4 complex; ISO:MGI.
DR GO; GO:0044545; C:NSL complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048188; C:Set1C/COMPASS complex; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); ISO:MGI.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006094; P:gluconeogenesis; IGI:MGI.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
DR GO; GO:0044154; P:histone H3-K14 acetylation; ISO:MGI.
DR GO; GO:0051568; P:histone H3-K4 methylation; IMP:MGI.
DR GO; GO:0043984; P:histone H4-K16 acetylation; ISS:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
DR GO; GO:0051572; P:negative regulation of histone H3-K4 methylation; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IGI:MGI.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0051302; P:regulation of cell division; IDA:ComplexPortal.
DR GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; IDA:ComplexPortal.
DR GO; GO:0045995; P:regulation of embryonic development; IDA:ComplexPortal.
DR GO; GO:0031063; P:regulation of histone deacetylation; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; ISO:MGI.
DR GO; GO:0001501; P:skeletal system development; IDA:MGI.
DR Gene3D; 2.130.10.10; -; 1.
DR IDEAL; IID50144; -.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromatin regulator; Isopeptide bond; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P61964"
FT CHAIN 2..334
FT /note="WD repeat-containing protein 5"
FT /id="PRO_0000051351"
FT REPEAT 43..82
FT /note="WD 1"
FT REPEAT 85..126
FT /note="WD 2"
FT REPEAT 128..168
FT /note="WD 3"
FT REPEAT 169..208
FT /note="WD 4"
FT REPEAT 212..253
FT /note="WD 5"
FT REPEAT 256..296
FT /note="WD 6"
FT REPEAT 299..333
FT /note="WD 7"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 107
FT /note="Important for interaction with histone H3"
FT /evidence="ECO:0000250"
FT SITE 133
FT /note="Important for interaction with histone H3"
FT /evidence="ECO:0000250"
FT SITE 263
FT /note="Important for interaction with histone H3"
FT /evidence="ECO:0000250"
FT SITE 322
FT /note="Important for interaction with histone H3"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P61964"
FT MOD_RES 112
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61964"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P61964"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P61964"
FT CROSSLNK 46
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P61964"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:2XL2"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:2XL2"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:2XL2"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:2XL2"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 226..233
FT /evidence="ECO:0007829|PDB:2XL2"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:2XL2"
FT TURN 243..246
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:2XL2"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 311..320
FT /evidence="ECO:0007829|PDB:2XL2"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:2XL2"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:2XL2"
SQ SEQUENCE 334 AA; 36588 MW; 4BF30914A2250286 CRC64;
MATEEKKPET EAARAQPTPS SSATQSKPTP VKPNYALKFT LAGHTKAVSS VKFSPNGEWL
ASSSADKLIK IWGAYDGKFE KTISGHKLGI SDVAWSSDSN LLVSASDDKT LKIWDVSSGK
CLKTLKGHSN YVFCCNFNPQ SNLIVSGSFD ESVRIWDVKT GKCLKTLPAH SDPVSAVHFN
RDGSLIVSSS YDGLCRIWDT ASGQCLKTLI DDDNPPVSFV KFSPNGKYIL AATLDNTLKL
WDYSKGKCLK TYTGHKNEKY CIFANFSVTG GKWIVSGSED NLVYIWNLQT KEIVQKLQGH
TDVVISTACH PTENIIASAA LENDKTIKLW KSDC
