UTP21_YEAST
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 03-AUG-2022, entry version 195.
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}.
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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 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 AlphaFoldDB; Q06078; -.
DR SMR; Q06078; -.
DR BioGRID; 31666; 253.
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; Q06078; -.
DR PRIDE; Q06078; -.
DR EnsemblFungi; YLR409C_mRNA; YLR409C; YLR409C.
DR GeneID; 851125; -.
DR KEGG; sce:YLR409C; -.
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; KFVGHTA; -.
DR BioCyc; YEAST:G3O-32471-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
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; IC:ComplexPortal.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IC:SGD.
DR GO; GO:0006364; P:rRNA processing; IGI:SGD.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR024977; Apc4_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; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF04192; Utp21; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 9.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF50998; SSF50998; 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
