WDR12_HUMAN
ID WDR12_HUMAN Reviewed; 423 AA.
AC Q9GZL7; B3KPA9; Q96HU0; Q9NV80; Q9NYI8;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Ribosome biogenesis protein WDR12 {ECO:0000255|HAMAP-Rule:MF_03029};
DE AltName: Full=WD repeat-containing protein 12 {ECO:0000255|HAMAP-Rule:MF_03029};
GN Name=WDR12 {ECO:0000255|HAMAP-Rule:MF_03029};
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].
RA Matsumoto S.;
RT "Human homolog of Saccharomyces cervisiae YTM1.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-75.
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 MRNA].
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 [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [5]
RP FUNCTION, INTERACTION WITH BOP1 AND PES1, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RX PubMed=16043514; DOI=10.1083/jcb.200501141;
RA Hoelzel M., Rohrmoser M., Schlee M., Grimm T., Harasim T., Malamoussi A.,
RA Gruber-Eber A., Kremmer E., Hiddemann W., Bornkamm G.W., Eick D.;
RT "Mammalian WDR12 is a novel member of the Pes1-Bop1 complex and is required
RT for ribosome biogenesis and cell proliferation.";
RL J. Cell Biol. 170:367-378(2005).
RN [6]
RP INTERACTION WITH PES1 AND WDR12.
RX PubMed=16738141; DOI=10.1093/nar/gkl378;
RA Grimm T., Hoelzel M., Rohrmoser M., Harasim T., Malamoussi A.,
RA Gruber-Eber A., Kremmer E., Eick D.;
RT "Dominant-negative Pes1 mutants inhibit ribosomal RNA processing and cell
RT proliferation via incorporation into the PeBoW-complex.";
RL Nucleic Acids Res. 34:3030-3043(2006).
RN [7]
RP FUNCTION, AND INTERACTION WITH BOP1 AND PES1.
RX PubMed=17353269; DOI=10.1128/mcb.00172-07;
RA Rohrmoser M., Hoelzel M., Grimm T., Malamoussi A., Harasim T., Orban M.,
RA Pfisterer I., Gruber-Eber A., Kremmer E., Eick D.;
RT "Interdependence of Pes1, Bop1, and WDR12 controls nucleolar localization
RT and assembly of the PeBoW complex required for maturation of the 60S
RT ribosomal subunit.";
RL Mol. Cell. Biol. 27:3682-3694(2007).
RN [8]
RP INTERACTION WITH BOP1 AND PES1.
RX PubMed=17189298; DOI=10.1093/nar/gkl1058;
RA Hoelzel M., Grimm T., Rohrmoser M., Malamoussi A., Harasim T.,
RA Gruber-Eber A., Kremmer E., Eick D.;
RT "The BRCT domain of mammalian Pes1 is crucial for nucleolar localization
RT and rRNA processing.";
RL Nucleic Acids Res. 35:789-800(2007).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-239, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [13]
RP INTERACTION WITH MDN1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-76 AND
RP GLU-78.
RX PubMed=26601951; DOI=10.1074/jbc.m115.693259;
RA Romes E.M., Sobhany M., Stanley R.E.;
RT "The crystal structure of the ubiquitin-like domain of ribosome assembly
RT factor Ytm1 and characterization of its interaction with the AAA-ATPase
RT Midasin.";
RL J. Biol. Chem. 291:882-893(2016).
CC -!- FUNCTION: Component of the PeBoW complex, which is required for
CC maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S
CC ribosome. {ECO:0000255|HAMAP-Rule:MF_03029,
CC ECO:0000269|PubMed:16043514, ECO:0000269|PubMed:17353269}.
CC -!- SUBUNIT: Component of the PeBoW complex, composed of BOP1, PES1 and
CC WDR12 (ECO:0000269|PubMed:16043514, ECO:0000269|PubMed:16738141,
CC PubMed:17189298, ECO:0000269|PubMed:17353269). The complex is held
CC together by BOP1, which interacts with PES1 via its N-terminal domain
CC and with WDR12 via a high-affinity interaction between the seven-bladed
CC beta-propeller domains of the 2 proteins. The PeBoW complex associates
CC with the 66S pre-ribosome (By similarity). Interacts (via UBL domain)
CC with MDN1 (via VWFA/MIDAS domain) (PubMed:26601951).
CC {ECO:0000255|HAMAP-Rule:MF_03029, ECO:0000269|PubMed:16043514,
CC ECO:0000269|PubMed:16738141, ECO:0000269|PubMed:17189298,
CC ECO:0000269|PubMed:17353269, ECO:0000269|PubMed:26601951}.
CC -!- INTERACTION:
CC Q9GZL7; Q14137: BOP1; NbExp=3; IntAct=EBI-2490660, EBI-1050828;
CC Q9GZL7; O00541: PES1; NbExp=4; IntAct=EBI-2490660, EBI-1053271;
CC Q9GZL7; Q13148: TARDBP; NbExp=3; IntAct=EBI-2490660, EBI-372899;
CC Q9GZL7; P40337-2: VHL; NbExp=3; IntAct=EBI-2490660, EBI-12157263;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC Rule:MF_03029, ECO:0000269|PubMed:12429849,
CC ECO:0000269|PubMed:16043514, ECO:0000269|PubMed:26601951}. Nucleus,
CC nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03029,
CC ECO:0000269|PubMed:16043514}.
CC -!- INDUCTION: By MYC. {ECO:0000269|PubMed:16043514}.
CC -!- SIMILARITY: Belongs to the WD repeat WDR12/YTM1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03029}.
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DR EMBL; AF242546; AAF60355.1; -; mRNA.
DR EMBL; AK001743; BAA91875.1; -; mRNA.
DR EMBL; AK022781; BAB14242.1; -; mRNA.
DR EMBL; AK022782; BAB14243.1; -; mRNA.
DR EMBL; AK056092; BAG51621.1; -; mRNA.
DR EMBL; BC008082; AAH08082.1; -; mRNA.
DR CCDS; CCDS2356.1; -.
DR RefSeq; NP_060726.3; NM_018256.3.
DR PDB; 6N31; X-ray; 2.60 A; A/B=90-422.
DR PDB; 6P0Q; X-ray; 1.72 A; A/B=1-87.
DR PDBsum; 6N31; -.
DR PDBsum; 6P0Q; -.
DR AlphaFoldDB; Q9GZL7; -.
DR SMR; Q9GZL7; -.
DR BioGRID; 120877; 118.
DR CORUM; Q9GZL7; -.
DR IntAct; Q9GZL7; 21.
DR MINT; Q9GZL7; -.
DR STRING; 9606.ENSP00000261015; -.
DR GlyGen; Q9GZL7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9GZL7; -.
DR PhosphoSitePlus; Q9GZL7; -.
DR SwissPalm; Q9GZL7; -.
DR BioMuta; WDR12; -.
DR DMDM; 20140802; -.
DR SWISS-2DPAGE; Q9GZL7; -.
DR EPD; Q9GZL7; -.
DR jPOST; Q9GZL7; -.
DR MassIVE; Q9GZL7; -.
DR MaxQB; Q9GZL7; -.
DR PaxDb; Q9GZL7; -.
DR PeptideAtlas; Q9GZL7; -.
DR PRIDE; Q9GZL7; -.
DR ProteomicsDB; 80083; -.
DR Antibodypedia; 19949; 160 antibodies from 25 providers.
DR DNASU; 55759; -.
DR Ensembl; ENST00000261015.5; ENSP00000261015.4; ENSG00000138442.11.
DR Ensembl; ENST00000688520.1; ENSP00000509107.1; ENSG00000138442.11.
DR GeneID; 55759; -.
DR KEGG; hsa:55759; -.
DR MANE-Select; ENST00000261015.5; ENSP00000261015.4; NM_018256.4; NP_060726.3.
DR UCSC; uc002uzl.4; human.
DR CTD; 55759; -.
DR DisGeNET; 55759; -.
DR GeneCards; WDR12; -.
DR HGNC; HGNC:14098; WDR12.
DR HPA; ENSG00000138442; Low tissue specificity.
DR MIM; 616620; gene.
DR neXtProt; NX_Q9GZL7; -.
DR OpenTargets; ENSG00000138442; -.
DR PharmGKB; PA37841; -.
DR VEuPathDB; HostDB:ENSG00000138442; -.
DR eggNOG; KOG0313; Eukaryota.
DR GeneTree; ENSGT00930000150950; -.
DR HOGENOM; CLU_000288_57_0_1; -.
DR InParanoid; Q9GZL7; -.
DR OMA; VDCTRTK; -.
DR OrthoDB; 1540178at2759; -.
DR PhylomeDB; Q9GZL7; -.
DR TreeFam; TF313023; -.
DR PathwayCommons; Q9GZL7; -.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q9GZL7; -.
DR BioGRID-ORCS; 55759; 743 hits in 1080 CRISPR screens.
DR ChiTaRS; WDR12; human.
DR GeneWiki; WDR12; -.
DR GenomeRNAi; 55759; -.
DR Pharos; Q9GZL7; Tbio.
DR PRO; PR:Q9GZL7; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9GZL7; protein.
DR Bgee; ENSG00000138442; Expressed in ventricular zone and 202 other tissues.
DR ExpressionAtlas; Q9GZL7; baseline and differential.
DR Genevisible; Q9GZL7; HS.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0070545; C:PeBoW complex; IDA:UniProtKB.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:UniProtKB.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:UniProtKB.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IC:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR HAMAP; MF_03029; WDR12; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR012972; NLE.
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; IPR028599; WDR12/Ytm1.
DR Pfam; PF08154; NLE; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribosome biogenesis; rRNA processing;
KW Ubl conjugation; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..423
FT /note="Ribosome biogenesis protein WDR12"
FT /id="PRO_0000051358"
FT REPEAT 99..137
FT /note="WD 1"
FT REPEAT 138..180
FT /note="WD 2"
FT REPEAT 187..226
FT /note="WD 3"
FT REPEAT 255..293
FT /note="WD 4"
FT REPEAT 295..334
FT /note="WD 5"
FT REPEAT 340..380
FT /note="WD 6"
FT REPEAT 384..422
FT /note="WD 7"
FT REGION 4..87
FT /note="Ubiquitin-like (UBL) domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03029"
FT REGION 98..423
FT /note="Sufficient for nucleolar localization"
FT REGION 220..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT VARIANT 72
FT /note="M -> V"
FT /id="VAR_012863"
FT VARIANT 75
FT /note="I -> V (in dbSNP:rs35212307)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_054888"
FT VARIANT 89
FT /note="Y -> C (in dbSNP:rs751438871)"
FT /id="VAR_012864"
FT VARIANT 286
FT /note="E -> G"
FT /id="VAR_012865"
FT MUTAGEN 76
FT /note="S->L: Reduces interaction with MDN1."
FT /evidence="ECO:0000269|PubMed:26601951"
FT MUTAGEN 78
FT /note="E->A: Abolishes interaction with MDN1."
FT /evidence="ECO:0000269|PubMed:26601951"
FT CONFLICT 333
FT /note="L -> M (in Ref. 1; AAF60355)"
FT /evidence="ECO:0000305"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:6P0Q"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:6P0Q"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:6P0Q"
FT HELIX 30..44
FT /evidence="ECO:0007829|PDB:6P0Q"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:6P0Q"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:6P0Q"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:6P0Q"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:6P0Q"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 153..162
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:6N31"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 260..275
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:6N31"
FT TURN 285..288
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:6N31"
FT TURN 307..310
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 311..324
FT /evidence="ECO:0007829|PDB:6N31"
FT TURN 329..332
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 333..339
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 389..394
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 398..404
FT /evidence="ECO:0007829|PDB:6N31"
FT STRAND 407..413
FT /evidence="ECO:0007829|PDB:6N31"
SQ SEQUENCE 423 AA; 47708 MW; 6D088C640AC981D8 CRC64;
MAQLQTRFYT DNKKYAVDDV PFSIPAASEI ADLSNIINKL LKDKNEFHKH VEFDFLIKGQ
FLRMPLDKHM EMENISSEEV VEIEYVEKYT APQPEQCMFH DDWISSIKGA EEWILTGSYD
KTSRIWSLEG KSIMTIVGHT DVVKDVAWVK KDSLSCLLLS ASMDQTILLW EWNVERNKVK
ALHCCRGHAG SVDSIAVDGS GTKFCSGSWD KMLKIWSTVP TDEEDEMEES TNRPRKKQKT
EQLGLTRTPI VTLSGHMEAV SSVLWSDAEE ICSASWDHTI RVWDVESGSL KSTLTGNKVF
NCISYSPLCK RLASGSTDRH IRLWDPRTKD GSLVSLSLTS HTGWVTSVKW SPTHEQQLIS
GSLDNIVKLW DTRSCKAPLY DLAAHEDKVL SVDWTDTGLL LSGGADNKLY SYRYSPTTSH
VGA
