WDR41_HUMAN
ID WDR41_HUMAN Reviewed; 459 AA.
AC Q9HAD4; B4DT55; Q7Z792; Q8IWG3; Q8IXA9; Q8NDA7; Q9NV62;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=WD repeat-containing protein 41 {ECO:0000305};
GN Name=WDR41 {ECO:0000312|HGNC:HGNC:25601}; ORFNames=MSTP048;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Aorta;
RA Zhao B., Xu Y.Y., Liu Y.Q., Wang X.Y., Liu B., Ye J., Song L., Zhao Y.,
RA Cao H.Q., Zhao X.W., Gao Y., Liu L.S., Ding J.F., Gao R.L., Wu Q.Y.,
RA Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ILE-329.
RC TISSUE=Embryo, Ovarian carcinoma, and Pericardium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 175-459 (ISOFORM 1/2), AND
RP VARIANT ILE-329.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION, IDENTIFICATION IN THE C9ORF72-SMCR8 COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=27193190; DOI=10.1186/s40478-016-0324-5;
RA Sullivan P.M., Zhou X., Robins A.M., Paushter D.H., Kim D., Smolka M.B.,
RA Hu F.;
RT "The ALS/FTLD associated protein C9orf72 associates with SMCR8 and WDR41 to
RT regulate the autophagy-lysosome pathway.";
RL Acta Neuropathol. Commun. 4:51-51(2016).
RN [7]
RP FUNCTION, AND IDENTIFICATION IN THE C9ORF72-SMCR8 COMPLEX.
RX PubMed=27103069; DOI=10.15252/embj.201593350;
RA Sellier C., Campanari M.L., Julie Corbier C., Gaucherot A.,
RA Kolb-Cheynel I., Oulad-Abdelghani M., Ruffenach F., Page A., Ciura S.,
RA Kabashi E., Charlet-Berguerand N.;
RT "Loss of C9ORF72 impairs autophagy and synergizes with polyQ Ataxin-2 to
RT induce motor neuron dysfunction and cell death.";
RL EMBO J. 35:1276-1297(2016).
RN [8]
RP FUNCTION, AND IDENTIFICATION IN THE C9ORF72-SMCR8 COMPLEX.
RX PubMed=27617292; DOI=10.1126/sciadv.1601167;
RA Yang M., Liang C., Swaminathan K., Herrlinger S., Lai F., Shiekhattar R.,
RA Chen J.F.;
RT "A C9ORF72/SMCR8-containing complex regulates ULK1 and plays a dual role in
RT autophagy.";
RL Sci. Adv. 2:E1601167-E1601167(2016).
RN [9]
RP FUNCTION, AND IDENTIFICATION IN THE C9ORF72-SMCR8 COMPLEX.
RX PubMed=28195531; DOI=10.7554/elife.23063;
RA Jung J., Nayak A., Schaeffer V., Starzetz T., Kirsch A.K., Mueller S.,
RA Dikic I., Mittelbronn M., Behrends C.;
RT "Multiplex image-based autophagy RNAi screening identifies SMCR8 as ULK1
RT kinase activity and gene expression regulator.";
RL Elife 6:0-0(2017).
RN [10] {ECO:0007744|PDB:6LT0}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) IN THE C9ORF72-SMCR8
RP COMPLEX, FUNCTION, AND MUTAGENESIS OF SER-438; ARG-441; SER-442; LEU-445;
RP PHE-446 AND LEU-449.
RX PubMed=32303654; DOI=10.1073/pnas.2002110117;
RA Tang D., Sheng J., Xu L., Zhan X., Liu J., Jiang H., Shu X., Liu X.,
RA Zhang T., Jiang L., Zhou C., Li W., Cheng W., Li Z., Wang K., Lu K.,
RA Yan C., Qi S.;
RT "Cryo-EM structure of C9ORF72-SMCR8-WDR41 reveals the role as a GAP for
RT Rab8a and Rab11a.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:9876-9883(2020).
CC -!- FUNCTION: Non-catalytic component of the C9orf72-SMCR8 complex, a
CC complex that has guanine nucleotide exchange factor (GEF) activity and
CC regulates autophagy (PubMed:27193190, PubMed:27103069, PubMed:27617292,
CC PubMed:28195531). The C9orf72-SMCR8 complex promotes the exchange of
CC GDP to GTP, converting inactive GDP-bound RAB8A and RAB39B into their
CC active GTP-bound form, thereby promoting autophagosome maturation
CC (PubMed:27103069). As part of the C9orf72-SMCR8 complex, stimulates
CC RAB8A and RAB11A GTPase activity in vitro, however WDR42 is shown not
CC be an essential complex component for this function (PubMed:32303654).
CC The C9orf72-SMCR8 complex also acts as a negative regulator of
CC autophagy initiation by interacting with the ULK1/ATG1 kinase complex
CC and inhibiting its protein kinase activity (PubMed:27103069,
CC PubMed:27617292). {ECO:0000269|PubMed:27103069,
CC ECO:0000269|PubMed:27193190, ECO:0000269|PubMed:27617292,
CC ECO:0000269|PubMed:28195531, ECO:0000269|PubMed:32303654}.
CC -!- SUBUNIT: Component of the C9orf72-SMCR8 complex, at least composed of
CC C9orf72, SMCR8 and WDR41 (PubMed:27193190, PubMed:27103069,
CC PubMed:27617292, PubMed:28195531, PubMed:32303654). The complex is
CC formed of two protomers, each individually consisting of one molecule
CC each of C9orf72, SMCR8 and WDR41 (PubMed:32303654). The protomers
CC homodimerize via an interaction between C9orf72 (via C-terminus) and
CC SMCR8 (via N-terminus) (PubMed:32303654). Within each protomer SMCR8
CC (via DENN domain) acts as a bridging protein between WDR41 (via C-
CC terminus and N-terminus) and C9orf72 (via C-terminus)
CC (PubMed:32303654). The C9orf72-SMCR8 complex associates with the
CC ULK1/ATG1 kinase complex (PubMed:27617292, PubMed:28195531).
CC {ECO:0000269|PubMed:27103069, ECO:0000269|PubMed:27193190,
CC ECO:0000269|PubMed:27617292, ECO:0000269|PubMed:28195531,
CC ECO:0000269|PubMed:32303654}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27193190}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HAD4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HAD4-2; Sequence=VSP_054014;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO06948.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF115511; AAO06948.1; ALT_FRAME; mRNA.
DR EMBL; AK001766; BAA91895.1; -; mRNA.
DR EMBL; AK021855; BAB13915.1; -; mRNA.
DR EMBL; AK023977; BAB14749.1; -; mRNA.
DR EMBL; AK300058; BAG61867.1; -; mRNA.
DR EMBL; AC010234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040241; AAH40241.1; -; mRNA.
DR EMBL; AL834138; CAD38853.2; -; mRNA.
DR CCDS; CCDS4038.1; -. [Q9HAD4-1]
DR RefSeq; NP_060738.2; NM_018268.3. [Q9HAD4-1]
DR PDB; 6LT0; EM; 3.20 A; A/D=1-459.
DR PDB; 6V4U; EM; 3.80 A; C=1-459.
DR PDB; 6WHH; X-ray; 2.71 A; A=30-440.
DR PDB; 7MGE; EM; 3.94 A; A=1-459.
DR PDBsum; 6LT0; -.
DR PDBsum; 6V4U; -.
DR PDBsum; 6WHH; -.
DR PDBsum; 7MGE; -.
DR AlphaFoldDB; Q9HAD4; -.
DR SMR; Q9HAD4; -.
DR BioGRID; 120546; 118.
DR ComplexPortal; CPX-3961; C9orf72-SMCR8 complex.
DR CORUM; Q9HAD4; -.
DR IntAct; Q9HAD4; 27.
DR MINT; Q9HAD4; -.
DR STRING; 9606.ENSP00000296679; -.
DR iPTMnet; Q9HAD4; -.
DR PhosphoSitePlus; Q9HAD4; -.
DR BioMuta; WDR41; -.
DR DMDM; 134047969; -.
DR EPD; Q9HAD4; -.
DR jPOST; Q9HAD4; -.
DR MassIVE; Q9HAD4; -.
DR MaxQB; Q9HAD4; -.
DR PaxDb; Q9HAD4; -.
DR PeptideAtlas; Q9HAD4; -.
DR PRIDE; Q9HAD4; -.
DR ProteomicsDB; 5074; -.
DR ProteomicsDB; 81396; -. [Q9HAD4-1]
DR Antibodypedia; 24490; 94 antibodies from 18 providers.
DR DNASU; 55255; -.
DR Ensembl; ENST00000296679.9; ENSP00000296679.4; ENSG00000164253.14. [Q9HAD4-1]
DR Ensembl; ENST00000507029.5; ENSP00000424287.1; ENSG00000164253.14. [Q9HAD4-2]
DR GeneID; 55255; -.
DR KEGG; hsa:55255; -.
DR MANE-Select; ENST00000296679.9; ENSP00000296679.4; NM_018268.4; NP_060738.2.
DR UCSC; uc003kff.2; human. [Q9HAD4-1]
DR CTD; 55255; -.
DR DisGeNET; 55255; -.
DR GeneCards; WDR41; -.
DR HGNC; HGNC:25601; WDR41.
DR HPA; ENSG00000164253; Low tissue specificity.
DR MIM; 617502; gene.
DR neXtProt; NX_Q9HAD4; -.
DR OpenTargets; ENSG00000164253; -.
DR PharmGKB; PA134906058; -.
DR VEuPathDB; HostDB:ENSG00000164253; -.
DR eggNOG; ENOG502QURA; Eukaryota.
DR GeneTree; ENSGT00390000017026; -.
DR InParanoid; Q9HAD4; -.
DR OMA; QLQCHRQ; -.
DR PhylomeDB; Q9HAD4; -.
DR TreeFam; TF332914; -.
DR PathwayCommons; Q9HAD4; -.
DR SignaLink; Q9HAD4; -.
DR BioGRID-ORCS; 55255; 8 hits in 1079 CRISPR screens.
DR ChiTaRS; WDR41; human.
DR GenomeRNAi; 55255; -.
DR Pharos; Q9HAD4; Tbio.
DR PRO; PR:Q9HAD4; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9HAD4; protein.
DR Bgee; ENSG00000164253; Expressed in secondary oocyte and 201 other tissues.
DR ExpressionAtlas; Q9HAD4; baseline and differential.
DR Genevisible; Q9HAD4; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; IDA:HGNC.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0045920; P:negative regulation of exocytosis; IC:ComplexPortal.
DR GO; GO:0050777; P:negative regulation of immune response; IC:ComplexPortal.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
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 InterPro; IPR040102; WDR41.
DR PANTHER; PTHR22805; PTHR22805; 1.
DR Pfam; PF00400; WD40; 3.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Autophagy; Cytoplasm;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..459
FT /note="WD repeat-containing protein 41"
FT /id="PRO_0000051390"
FT REPEAT 40..79
FT /note="WD 1"
FT REPEAT 82..128
FT /note="WD 2"
FT REPEAT 131..168
FT /note="WD 3"
FT REPEAT 220..258
FT /note="WD 4"
FT REPEAT 321..359
FT /note="WD 5"
FT REPEAT 403..441
FT /note="WD 6"
FT VAR_SEQ 18..72
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054014"
FT VARIANT 61
FT /note="G -> D (in dbSNP:rs389319)"
FT /id="VAR_031215"
FT VARIANT 260
FT /note="R -> C (in dbSNP:rs17751013)"
FT /id="VAR_031216"
FT VARIANT 329
FT /note="V -> I (in dbSNP:rs33204)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_023777"
FT MUTAGEN 438
FT /note="S->A: No effect on interaction with SMCR8."
FT /evidence="ECO:0000269|PubMed:32303654"
FT MUTAGEN 441
FT /note="R->A: No effect on interaction with SMCR8."
FT /evidence="ECO:0000269|PubMed:32303654"
FT MUTAGEN 442
FT /note="S->A: No effect on interaction with SMCR8."
FT /evidence="ECO:0000269|PubMed:32303654"
FT MUTAGEN 445
FT /note="L->R: Reduces interaction with the C9ORF72-SMCR8
FT complex; when associated with R-449. No effect on
FT interaction with SMCR8."
FT /evidence="ECO:0000269|PubMed:32303654"
FT MUTAGEN 446
FT /note="F->R: No effect on interaction with SMCR8."
FT /evidence="ECO:0000269|PubMed:32303654"
FT MUTAGEN 449
FT /note="L->R: Reduces interaction with the C9ORF72-SMCR8
FT complex; when associated with R-445. No effect on
FT interaction with SMCR8."
FT /evidence="ECO:0000269|PubMed:32303654"
FT CONFLICT 365
FT /note="G -> D (in Ref. 1; BAB13915)"
FT /evidence="ECO:0000305"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:6WHH"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:6WHH"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:6LT0"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:6WHH"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 147..158
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:6LT0"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:6WHH"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:6WHH"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:6WHH"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:6LT0"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 293..300
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:6WHH"
FT TURN 309..312
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 333..341
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:6LT0"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 396..400
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 408..414
FT /evidence="ECO:0007829|PDB:6WHH"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 418..423
FT /evidence="ECO:0007829|PDB:6WHH"
FT STRAND 426..432
FT /evidence="ECO:0007829|PDB:6WHH"
FT TURN 434..436
FT /evidence="ECO:0007829|PDB:6LT0"
FT HELIX 441..452
FT /evidence="ECO:0007829|PDB:6LT0"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:6LT0"
SQ SEQUENCE 459 AA; 51728 MW; AADC0725E29B5B84 CRC64;
MLRWLIGGGR EPQGLAEKSP LQTIGEEQTQ NPYTELLVLK AHHDIVRFLV QLDDYRFASA
GDDGIVVVWN AQTGEKLLEL NGHTQKITAI ITFPSLESCE EKNQLILTAS ADRTVIVWDG
DTTRQVQRIS CFQSTVKCLT VLQRLDVWLS GGNDLCVWNR KLDLLCKTSH LSDTGISALV
EIPKNCVVAA VGKELIIFRL VAPTEGSLEW DILEVKRLLD HQDNILSLIN VNDLSFVTGS
HVGELIIWDA LDWTMQAYER NFWDPSPQLD TQQEIKLCQK SNDISIHHFT CDEENVFAAV
GRGLYVYSLQ MKRVIACQKT AHDSNVLHVA RLPNRQLISC SEDGSVRIWE LREKQQLAAE
PVPTGFFNMW GFGRVSKQAS QPVKKQQENA TSCSLELIGD LIGHSSSVEM FLYFEDHGLV
TCSADHLIIL WKNGERESGL RSLRLFQKLE ENGDLYLAV
