ID UTP21_YEAST Reviewed; 939 AA. AC Q06078; D6VZ43; DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 203. DE RecName: Full=U3 small nucleolar RNA-associated protein 21; DE Short=U3 snoRNA-associated protein 21; DE AltName: Full=U three protein 21; GN Name=UTP21; OrderedLocusNames=YLR409C; ORFNames=L8084.22; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169871; RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J., RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., RA Zollner A., Hani J., Hoheisel J.D.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."; RL Nature 387:87-90(1997). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [3] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [4] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [5] RP FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU RP PROCESSOME, AND SUBCELLULAR LOCATION. RX PubMed=15590835; DOI=10.1128/ec.3.6.1619-1626.2004; RA Bernstein K.A., Gallagher J.E.G., Mitchell B.M., Granneman S., RA Baserga S.J.; RT "The small-subunit processome is a ribosome assembly intermediate."; RL Eukaryot. Cell 3:1619-1626(2004). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-772, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [8] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-684, SUBUNIT, AND WD REPEATS. RX PubMed=24466140; DOI=10.1371/journal.pone.0086540; RA Zhang C., Lin J., Liu W., Chen X., Chen R., Ye K.; RT "Structure of Utp21 tandem WD domain provides insight into the organization RT of the UTPB complex involved in ribosome synthesis."; RL PLoS ONE 9:E86540-E86540(2014). CC -!- FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA and CC ribosome assembly. {ECO:0000269|PubMed:15590835}. CC -!- SUBUNIT: Interacts with snoRNA U3. Interacts with MPP10. Interacts (via CC WD repeats) with UTP18. Component of the ribosomal small subunit (SSU) CC processome composed of at least 40 protein subunits and snoRNA U3. CC {ECO:0000269|PubMed:15590835, ECO:0000269|PubMed:24466140}. CC -!- INTERACTION: CC Q06078; P38333: ENP1; NbExp=3; IntAct=EBI-359, EBI-6482; CC Q06078; P25635: PWP2; NbExp=15; IntAct=EBI-359, EBI-14332; CC Q06078; Q05022: RRP5; NbExp=2; IntAct=EBI-359, EBI-16011; CC Q06078; P40362: UTP18; NbExp=11; IntAct=EBI-359, EBI-4534; CC Q06078; Q02354: UTP6; NbExp=15; IntAct=EBI-359, EBI-22119; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095, CC ECO:0000269|PubMed:15590835}. CC -!- DOMAIN: The WD repeats are grouped into two tandem seven-bladed beta- CC propeller regions. CC -!- MISCELLANEOUS: Present with 2020 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U19729; AAB82361.1; -; Genomic_DNA. DR EMBL; BK006945; DAA09709.1; -; Genomic_DNA. DR PIR; S55965; S55965. DR RefSeq; NP_013513.3; NM_001182297.3. DR PDB; 4HNX; X-ray; 2.10 A; A=1-684. DR PDB; 4NSX; X-ray; 2.10 A; A=1-684. DR PDB; 5JPQ; EM; 7.30 A; I=1-939. DR PDB; 5TZS; EM; 5.10 A; T=21-673. DR PDB; 5WLC; EM; 3.80 A; LT=1-939. DR PDB; 5WYJ; EM; 8.70 A; BE=1-939. DR PDB; 5WYK; EM; 4.50 A; BE=1-939. DR PDB; 6KE6; EM; 3.40 A; BE=1-939. DR PDB; 6LQP; EM; 3.20 A; BE=1-939. DR PDB; 6LQQ; EM; 4.10 A; BE=1-939. DR PDB; 6LQR; EM; 8.60 A; BE=1-939. DR PDB; 6LQS; EM; 3.80 A; BE=1-939. DR PDB; 6LQT; EM; 4.90 A; BE=1-939. DR PDB; 6LQU; EM; 3.70 A; BE=1-939. DR PDB; 6LQV; EM; 4.80 A; BE=1-939. DR PDB; 6ND4; EM; 4.30 A; T=1-939. DR PDB; 6ZQA; EM; 4.40 A; UU=1-939. DR PDB; 6ZQB; EM; 3.90 A; UU=1-939. DR PDB; 6ZQC; EM; 3.80 A; UU=1-939. DR PDB; 6ZQD; EM; 3.80 A; UU=1-939. DR PDB; 6ZQE; EM; 7.10 A; UU=1-939. DR PDB; 6ZQF; EM; 4.90 A; UU=1-939. DR PDB; 7AJT; EM; 4.60 A; UU=1-939. DR PDB; 7AJU; EM; 3.80 A; UU=1-939. DR PDB; 7D4I; EM; 4.00 A; BE=1-939. DR PDB; 7D5S; EM; 4.60 A; BE=1-939. DR PDB; 7D5T; EM; 6.00 A; BE=1-939. DR PDB; 7D63; EM; 12.30 A; BE=1-939. DR PDB; 7SUK; EM; 3.99 A; LT=19-939. DR PDBsum; 4HNX; -. DR PDBsum; 4NSX; -. DR PDBsum; 5JPQ; -. DR PDBsum; 5TZS; -. DR PDBsum; 5WLC; -. DR PDBsum; 5WYJ; -. DR PDBsum; 5WYK; -. DR PDBsum; 6KE6; -. DR PDBsum; 6LQP; -. DR PDBsum; 6LQQ; -. DR PDBsum; 6LQR; -. DR PDBsum; 6LQS; -. DR PDBsum; 6LQT; -. DR PDBsum; 6LQU; -. DR PDBsum; 6LQV; -. DR PDBsum; 6ND4; -. DR PDBsum; 6ZQA; -. DR PDBsum; 6ZQB; -. DR PDBsum; 6ZQC; -. DR PDBsum; 6ZQD; -. DR PDBsum; 6ZQE; -. DR PDBsum; 6ZQF; -. DR PDBsum; 7AJT; -. DR PDBsum; 7AJU; -. DR PDBsum; 7D4I; -. DR PDBsum; 7D5S; -. DR PDBsum; 7D5T; -. DR PDBsum; 7D63; -. DR PDBsum; 7SUK; -. DR AlphaFoldDB; Q06078; -. DR EMDB; EMD-0949; -. DR EMDB; EMD-0950; -. DR EMDB; EMD-0951; -. DR EMDB; EMD-0952; -. DR EMDB; EMD-0953; -. DR EMDB; EMD-0954; -. DR EMDB; EMD-0955; -. DR EMDB; EMD-11357; -. DR EMDB; EMD-11358; -. DR EMDB; EMD-11359; -. DR EMDB; EMD-11360; -. DR EMDB; EMD-11361; -. DR EMDB; EMD-11362; -. DR EMDB; EMD-11807; -. DR EMDB; EMD-11808; -. DR EMDB; EMD-25441; -. DR EMDB; EMD-30574; -. DR EMDB; EMD-30584; -. DR EMDB; EMD-30585; -. DR EMDB; EMD-30588; -. DR EMDB; EMD-6695; -. DR EMDB; EMD-6696; -. DR EMDB; EMD-8473; -. DR EMDB; EMD-9964; -. DR SMR; Q06078; -. DR BioGRID; 31666; 275. DR ComplexPortal; CPX-1410; UTP-B complex. DR DIP; DIP-6416N; -. DR IntAct; Q06078; 32. DR MINT; Q06078; -. DR STRING; 4932.YLR409C; -. DR iPTMnet; Q06078; -. DR MaxQB; Q06078; -. DR PaxDb; 4932-YLR409C; -. DR PeptideAtlas; Q06078; -. DR EnsemblFungi; YLR409C_mRNA; YLR409C; YLR409C. DR GeneID; 851125; -. DR KEGG; sce:YLR409C; -. DR AGR; SGD:S000004401; -. DR SGD; S000004401; UTP21. DR VEuPathDB; FungiDB:YLR409C; -. DR eggNOG; KOG1539; Eukaryota. DR GeneTree; ENSGT00940000153662; -. DR HOGENOM; CLU_002774_2_0_1; -. DR InParanoid; Q06078; -. DR OMA; WESVVTG; -. DR OrthoDB; 5477616at2759; -. DR BioCyc; YEAST:G3O-32471-MONOMER; -. DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR BioGRID-ORCS; 851125; 2 hits in 10 CRISPR screens. DR PRO; PR:Q06078; -. DR Proteomes; UP000002311; Chromosome XII. DR RNAct; Q06078; Protein. DR GO; GO:0030686; C:90S preribosome; HDA:SGD. DR GO; GO:0005730; C:nucleolus; IDA:SGD. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; HDA:SGD. DR GO; GO:0034388; C:Pwp2p-containing subcomplex of 90S preribosome; IDA:SGD. DR GO; GO:0032040; C:small-subunit processome; IDA:SGD. DR GO; GO:0030490; P:maturation of SSU-rRNA; NAS:ComplexPortal. DR GO; GO:0006364; P:rRNA processing; IGI:SGD. DR CDD; cd00200; WD40; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2. DR InterPro; IPR024977; Apc4-like_WD40_dom. DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam. DR InterPro; IPR007319; SSU_processome_Utp21. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR22840; WD REPEAT-CONTAINING PROTEIN 36; 1. DR PANTHER; PTHR22840:SF12; WD REPEAT-CONTAINING PROTEIN 36; 1. DR Pfam; PF12894; ANAPC4_WD40; 1. DR Pfam; PF04192; Utp21; 1. DR Pfam; PF00400; WD40; 1. DR SMART; SM00320; WD40; 9. DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; 1. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Nucleus; Phosphoprotein; Reference proteome; KW Repeat; Ribonucleoprotein; Ribosome biogenesis; rRNA processing; WD repeat. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..939 FT /note="U3 small nucleolar RNA-associated protein 21" FT /id="PRO_0000051480" FT REPEAT 40..71 FT /note="WD 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:24466140" FT REPEAT 81..111 FT /note="WD 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:24466140" FT REPEAT 119..158 FT /note="WD 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:24466140" FT REPEAT 168..201 FT /note="WD 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:24466140" FT REPEAT 208..245 FT /note="WD 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:24466140" FT REPEAT 252..287 FT /note="WD 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:24466140" FT REPEAT 295..347 FT /note="WD 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:24466140" FT REPEAT 354..388 FT /note="WD 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:24466140" FT REPEAT 415..454 FT /note="WD 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:24466140" FT REPEAT 463..497 FT /note="WD 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:24466140" FT REPEAT 505..541 FT /note="WD 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:24466140" FT REPEAT 546..581 FT /note="WD 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:24466140" FT REPEAT 583..624 FT /note="WD 13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:24466140" FT REPEAT 626..664 FT /note="WD 14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:24466140" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 772 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT STRAND 22..31 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 40..44 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 47..53 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 58..62 FT /evidence="ECO:0007829|PDB:4NSX" FT TURN 63..65 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 68..71 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 82..86 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 89..94 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 97..102 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 105..111 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 113..116 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 118..124 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 127..132 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 135..141 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 147..149 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 152..158 FT /evidence="ECO:0007829|PDB:4NSX" FT TURN 161..163 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 165..171 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 179..186 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 188..192 FT /evidence="ECO:0007829|PDB:4NSX" FT TURN 193..195 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 198..201 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 209..214 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 220..234 FT /evidence="ECO:0007829|PDB:4NSX" FT TURN 235..238 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 239..245 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 251..256 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 259..261 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 263..268 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 273..277 FT /evidence="ECO:0007829|PDB:4NSX" FT TURN 278..281 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 282..287 FT /evidence="ECO:0007829|PDB:4NSX" FT HELIX 293..295 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 299..303 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 307..313 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 315..323 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 341..347 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 353..358 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 365..370 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 375..379 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 386..388 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 414..419 FT /evidence="ECO:0007829|PDB:4NSX" FT TURN 422..426 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 430..434 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 438..444 FT /evidence="ECO:0007829|PDB:4NSX" FT TURN 445..448 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 449..456 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 458..460 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 463..468 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 474..479 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 482..488 FT /evidence="ECO:0007829|PDB:4NSX" FT TURN 489..491 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 494..499 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 505..510 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 516..521 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 524..533 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 536..541 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 546..551 FT /evidence="ECO:0007829|PDB:4NSX" FT TURN 553..555 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 557..562 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 567..571 FT /evidence="ECO:0007829|PDB:4NSX" FT TURN 572..575 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 576..581 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 588..593 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 597..604 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 607..613 FT /evidence="ECO:0007829|PDB:4NSX" FT TURN 614..616 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 619..624 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 629..634 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 640..647 FT /evidence="ECO:0007829|PDB:4NSX" FT STRAND 649..656 FT /evidence="ECO:0007829|PDB:4NSX" SQ SEQUENCE 939 AA; 104791 MW; F1F856EF28369351 CRC64; MSIDLKKRKV EEDVRSRGKN SKIFSPFRII GNVSNGVPFA TGTLGSTFYI VTCVGKTFQI YDANTLHLLF VSEKETPSSI VALSAHFHYV YAAYENKVGI YKRGIEEHLL ELETDANVEH LCIFGDYLCA STDDNSIFIY KKSDPQDKYP SEFYTKLTVT EIQGGEIVSL QHLATYLNKL TVVTKSNVLL FNVRTGKLVF TSNEFPDQIT TAEPAPVLDI IALGTVTGEV IMFNMRKGKR IRTIKIPQSR ISSLSFRTDG SSHLSVGTSS GDLIFYDLDR RSRIHVLKNI HRESYGGVTQ ATFLNGQPII VTSGGDNSLK EYVFDPSLSQ GSGDVVVQPP RYLRSRGGHS QPPSYIAFAD SQSHFMLSAS KDRSLWSFSL RKDAQSQEMS QRLHKKQDGG RVGGSTIKSK FPEIVALAIE NARIGEWENI ITAHKDEKFA RTWDMRNKRV GRWTFDTTDD GFVKSVAMSQ CGNFGFIGSS NGSITIYNMQ SGILRKKYKL HKRAVTGISL DGMNRKMVSC GLDGIVGFYD FNKSTLLGKL KLDAPITAMV YHRSSDLFAL ALDDLSIVVI DAVTQRVVRQ LWGHSNRITA FDFSPEGRWI VSASLDSTIR TWDLPTGGCI DGIIVDNVAT NVKFSPNGDL LATTHVTGNG ICIWTNRAQF KTVSTRTIDE SEFARMALPS TSVRGNDSML SGALESNGGE DLNDIDFNTY TSLEQIDKEL LTLSIGPRSK MNTLLHLDVI RKRSKPKEAP KKSEKLPFFL QLSGEKVGDE ASVREGIAHE TPEEIHRRDQ EAQKKLDAEE QMNKFKVTGR LGFESHFTKQ LREGSQSKDY SSLLATLINF SPAAVDLEIR SLNSFEPFDE IVWFIDALTQ GLKSNKNFEL YETFMSLLFK AHGDVIHANN KNQDIASALQ NWEDVHKKED RLDDLVKFCM GVAAFVTTA //