UTP15_HUMAN
ID UTP15_HUMAN Reviewed; 518 AA.
AC Q8TED0; B4DU75; B4DXK8; Q6IA60; Q96E08; Q9H9F8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=U3 small nucleolar RNA-associated protein 15 homolog;
GN Name=UTP15;
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] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Prostate, and Testis;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 191-518 (ISOFORM 1/2/3).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 234-518 (ISOFORM 1/2/3).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=17699751; DOI=10.1101/gad.436707;
RA Prieto J.L., McStay B.;
RT "Recruitment of factors linking transcription and processing of pre-rRNA to
RT NOR chromatin is UBF-dependent and occurs independent of transcription in
RT human cells.";
RL Genes Dev. 21:2041-2054(2007).
RN [7]
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 [8]
RP POSSIBLE ASSOCIATION IN THE SSU PROCESSOME T-UTP SUBCOMPLEX.
RX PubMed=22916032; DOI=10.1371/journal.pgen.1002892;
RA Freed E.F., Prieto J.L., McCann K.L., McStay B., Baserga S.J.;
RT "NOL11, implicated in the pathogenesis of North American Indian childhood
RT cirrhosis, is required for pre-rRNA transcription and processing.";
RL PLoS Genet. 8:E1002892-E1002892(2012).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH UTP4 AND WDR43.
RX PubMed=24219289; DOI=10.1139/bcb-2013-0062;
RA Sato M., Araki N., Kumeta M., Takeyasu K., Taguchi Y., Asai T.,
RA Furukawa K., Horigome T.;
RT "Interaction, mobility, and phosphorylation of human orthologues of WD
RT repeat-containing components of the yeast SSU processome t-UTP sub-
RT complex.";
RL Biochem. Cell Biol. 91:466-475(2013).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-249, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Ribosome biogenesis factor. Involved in nucleolar processing
CC of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA
CC transcription by RNA polymerase I. {ECO:0000269|PubMed:17699751}.
CC -!- SUBUNIT: Interacts directly with UTP4 and WDR43 (PubMed:24219289). May
CC be a component of the proposed t-UTP subcomplex of the ribosomal small
CC subunit (SSU) processome containing at least UTP4, WDR43, HEATR1,
CC UTP15, WDR75 (PubMed:17699751, PubMed:22916032).
CC {ECO:0000269|PubMed:24219289, ECO:0000305|PubMed:17699751,
CC ECO:0000305|PubMed:22916032}.
CC -!- INTERACTION:
CC Q8TED0; Q969X6: UTP4; NbExp=3; IntAct=EBI-1048301, EBI-2602591;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
CC ECO:0000269|PubMed:24219289}. Note=Found predominantly at the fibrillar
CC center. {ECO:0000269|PubMed:24219289}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8TED0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TED0-2; Sequence=VSP_055255;
CC Name=3;
CC IsoId=Q8TED0-3; Sequence=VSP_055256;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14271.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB85020.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK022849; BAB14271.1; ALT_INIT; mRNA.
DR EMBL; AK074217; BAB85020.1; ALT_FRAME; mRNA.
DR EMBL; AK300525; BAG62237.1; -; mRNA.
DR EMBL; AK302021; BAG63420.1; -; mRNA.
DR EMBL; AC010279; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013064; AAH13064.1; -; mRNA.
DR EMBL; CR457295; CAG33576.1; -; mRNA.
DR CCDS; CCDS34186.1; -. [Q8TED0-1]
DR CCDS; CCDS68893.1; -. [Q8TED0-3]
DR CCDS; CCDS68894.1; -. [Q8TED0-2]
DR RefSeq; NP_001271359.1; NM_001284430.1. [Q8TED0-3]
DR RefSeq; NP_001271360.1; NM_001284431.1. [Q8TED0-2]
DR RefSeq; NP_115551.2; NM_032175.3. [Q8TED0-1]
DR RefSeq; XP_011541982.1; XM_011543680.2. [Q8TED0-1]
DR PDB; 7MQ8; EM; 3.60 A; LJ=1-518.
DR PDB; 7MQ9; EM; 3.87 A; LJ=1-518.
DR PDB; 7MQA; EM; 2.70 A; LJ=1-518.
DR PDB; 7RUO; X-ray; 1.80 A; A/B=1-370.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR PDBsum; 7RUO; -.
DR AlphaFoldDB; Q8TED0; -.
DR SMR; Q8TED0; -.
DR BioGRID; 123907; 104.
DR IntAct; Q8TED0; 29.
DR MINT; Q8TED0; -.
DR STRING; 9606.ENSP00000296792; -.
DR iPTMnet; Q8TED0; -.
DR PhosphoSitePlus; Q8TED0; -.
DR BioMuta; UTP15; -.
DR DMDM; 296452998; -.
DR SWISS-2DPAGE; Q8TED0; -.
DR EPD; Q8TED0; -.
DR jPOST; Q8TED0; -.
DR MassIVE; Q8TED0; -.
DR MaxQB; Q8TED0; -.
DR PaxDb; Q8TED0; -.
DR PeptideAtlas; Q8TED0; -.
DR PRIDE; Q8TED0; -.
DR ProteomicsDB; 5157; -.
DR ProteomicsDB; 5447; -.
DR ProteomicsDB; 74446; -. [Q8TED0-1]
DR Antibodypedia; 44207; 63 antibodies from 17 providers.
DR DNASU; 84135; -.
DR Ensembl; ENST00000296792.9; ENSP00000296792.4; ENSG00000164338.10. [Q8TED0-1]
DR Ensembl; ENST00000508491.1; ENSP00000424609.1; ENSG00000164338.10. [Q8TED0-3]
DR Ensembl; ENST00000543251.5; ENSP00000440796.1; ENSG00000164338.10. [Q8TED0-2]
DR GeneID; 84135; -.
DR KEGG; hsa:84135; -.
DR MANE-Select; ENST00000296792.9; ENSP00000296792.4; NM_032175.4; NP_115551.2.
DR UCSC; uc003kcw.3; human. [Q8TED0-1]
DR CTD; 84135; -.
DR DisGeNET; 84135; -.
DR GeneCards; UTP15; -.
DR HGNC; HGNC:25758; UTP15.
DR HPA; ENSG00000164338; Tissue enhanced (bone).
DR MIM; 616194; gene.
DR neXtProt; NX_Q8TED0; -.
DR OpenTargets; ENSG00000164338; -.
DR PharmGKB; PA142670631; -.
DR VEuPathDB; HostDB:ENSG00000164338; -.
DR eggNOG; KOG0267; Eukaryota.
DR eggNOG; KOG0310; Eukaryota.
DR GeneTree; ENSGT00390000004228; -.
DR HOGENOM; CLU_021102_4_1_1; -.
DR InParanoid; Q8TED0; -.
DR OMA; WKEHKQP; -.
DR OrthoDB; 621827at2759; -.
DR PhylomeDB; Q8TED0; -.
DR TreeFam; TF319494; -.
DR PathwayCommons; Q8TED0; -.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q8TED0; -.
DR BioGRID-ORCS; 84135; 764 hits in 1084 CRISPR screens.
DR ChiTaRS; UTP15; human.
DR GeneWiki; UTP15; -.
DR GenomeRNAi; 84135; -.
DR Pharos; Q8TED0; Tbio.
DR PRO; PR:Q8TED0; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8TED0; protein.
DR Bgee; ENSG00000164338; Expressed in calcaneal tendon and 135 other tissues.
DR ExpressionAtlas; Q8TED0; baseline and differential.
DR Genevisible; Q8TED0; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0001650; C:fibrillar center; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:2000234; P:positive regulation of rRNA processing; IMP:UniProtKB.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR018983; U3_snoRNA-assocProt_15_C.
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; PF09384; UTP15_C; 1.
DR Pfam; PF00400; WD40; 4.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Isopeptide bond; Nucleus;
KW Reference proteome; Repeat; Ribosome biogenesis; rRNA processing;
KW Transcription; Transcription regulation; Ubl conjugation; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..518
FT /note="U3 small nucleolar RNA-associated protein 15
FT homolog"
FT /id="PRO_0000051321"
FT REPEAT 36..75
FT /note="WD 1"
FT REPEAT 78..117
FT /note="WD 2"
FT REPEAT 120..159
FT /note="WD 3"
FT REPEAT 162..202
FT /note="WD 4"
FT REPEAT 204..242
FT /note="WD 5"
FT REPEAT 246..285
FT /note="WD 6"
FT REPEAT 287..326
FT /note="WD 7"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..190
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055255"
FT VAR_SEQ 31..49
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055256"
FT VARIANT 228
FT /note="Y -> H (in dbSNP:rs16870608)"
FT /id="VAR_057621"
FT VARIANT 332
FT /note="R -> S (in dbSNP:rs35313343)"
FT /id="VAR_057622"
FT VARIANT 483
FT /note="T -> P (in dbSNP:rs35898225)"
FT /id="VAR_057623"
FT CONFLICT 130
FT /note="F -> S (in Ref. 1; BAB85020)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="L -> P (in Ref. 4; CAG33576)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="D -> G (in Ref. 1; BAB14271)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="E -> G (in Ref. 1; BAB85020)"
FT /evidence="ECO:0000305"
FT HELIX 21..27
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:7RUO"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:7RUO"
FT TURN 234..237
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 238..244
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 270..276
FT /evidence="ECO:0007829|PDB:7RUO"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:7RUO"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:7RUO"
FT STRAND 311..318
FT /evidence="ECO:0007829|PDB:7RUO"
SQ SEQUENCE 518 AA; 58415 MW; CB1994E968981BD0 CRC64;
MAGYKPVAIQ TYPILGEKIT QDTLYWNNYK TPVQIKEFGA VSKVDFSPQP PYNYAVTASS
RIHIYGRYSQ EPIKTFSRFK DTAYCATFRQ DGRLLVAGSE DGGVQLFDIS GRAPLRQFEG
HTKAVHTVDF TADKYHVVSG ADDYTVKLWD IPNSKEILTF KEHSDYVRCG CASKLNPDLF
ITGSYDHTVK MFDARTSESV LSVEHGQPVE SVLLFPSGGL LVSAGGRYVK VWDMLKGGQL
LVSLKNHHKT VTCLCLSSSG QRLLSGSLDR KVKVYSTTSY KVVHSFDYAA SILSLALAHE
DETIVVGMTN GILSVKHRKS EAKKESLPRR RRPAYRTFIK GKNYMKQRDD ILINRPAKKH
LELYDRDLKH FRISKALDRV LDPTCTIKTP EITVSIIKEL NRRGVLANAL AGRDEKEISH
VLNFLIRNLS QPRFAPVLIN AAEIIIDIYL PVIGQSPVVD KKFLLLQGLV EKEIDYQREL
LETLGMMDML FATMRRKEGT SVLEHTSDGF PENKKIES
