YETS2_MOUSE
ID YETS2_MOUSE Reviewed; 1407 AA.
AC Q3TUF7; Q6PGF8; Q80TI2; Q8CG86;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=YEATS domain-containing protein 2 {ECO:0000305};
GN Name=Yeats2 {ECO:0000312|MGI:MGI:2447762};
GN Synonyms=Kiaa1197 {ECO:0000303|PubMed:12693553};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-497.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-1407 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 991-1407 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary gland;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-472, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Chromatin reader component of the ATAC complex, a complex
CC with histone acetyltransferase activity on histones H3 and H4. YEATS2
CC specifically recognizes and binds histone H3 crotonylated at 'Lys-27'
CC (H3K27cr). Crotonylation marks active promoters and enhancers and
CC confers resistance to transcriptional repressors.
CC {ECO:0000250|UniProtKB:Q9ULM3}.
CC -!- SUBUNIT: Component of the ADA2A-containing complex (ATAC), composed of
CC KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, SGF29 and DR1.
CC {ECO:0000250|UniProtKB:Q9ULM3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ULM3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3TUF7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TUF7-2; Sequence=VSP_017007, VSP_017008;
CC Name=3;
CC IsoId=Q3TUF7-3; Sequence=VSP_017006;
CC -!- DOMAIN: The YEATS domain specifically recognizes and binds crotonylated
CC histones. {ECO:0000250|UniProtKB:Q9ULM3}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH57045.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC65745.3; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it is derived from pre-RNA.; Evidence={ECO:0000305};
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DR EMBL; AK160791; BAE36014.1; -; mRNA.
DR EMBL; AK122463; BAC65745.3; ALT_SEQ; Transcribed_RNA.
DR EMBL; BC042768; AAH42768.1; -; mRNA.
DR EMBL; BC057045; AAH57045.1; ALT_INIT; mRNA.
DR CCDS; CCDS28043.1; -. [Q3TUF7-3]
DR CCDS; CCDS49790.1; -. [Q3TUF7-1]
DR RefSeq; NP_001028409.2; NM_001033237.2. [Q3TUF7-3]
DR RefSeq; NP_001139402.1; NM_001145930.1. [Q3TUF7-1]
DR RefSeq; XP_006521965.1; XM_006521902.3. [Q3TUF7-1]
DR AlphaFoldDB; Q3TUF7; -.
DR SMR; Q3TUF7; -.
DR BioGRID; 228952; 6.
DR ComplexPortal; CPX-1025; GCN5-containing ATAC complex.
DR ComplexPortal; CPX-1029; PCAF-containing ATAC complex.
DR IntAct; Q3TUF7; 3.
DR MINT; Q3TUF7; -.
DR STRING; 10090.ENSMUSP00000111222; -.
DR iPTMnet; Q3TUF7; -.
DR PhosphoSitePlus; Q3TUF7; -.
DR EPD; Q3TUF7; -.
DR jPOST; Q3TUF7; -.
DR MaxQB; Q3TUF7; -.
DR PaxDb; Q3TUF7; -.
DR PeptideAtlas; Q3TUF7; -.
DR PRIDE; Q3TUF7; -.
DR ProteomicsDB; 299624; -. [Q3TUF7-1]
DR ProteomicsDB; 299625; -. [Q3TUF7-2]
DR ProteomicsDB; 299626; -. [Q3TUF7-3]
DR Antibodypedia; 50874; 90 antibodies from 26 providers.
DR Ensembl; ENSMUST00000090052; ENSMUSP00000087506; ENSMUSG00000041215. [Q3TUF7-3]
DR Ensembl; ENSMUST00000115560; ENSMUSP00000111222; ENSMUSG00000041215. [Q3TUF7-1]
DR GeneID; 208146; -.
DR KEGG; mmu:208146; -.
DR UCSC; uc007ypj.2; mouse. [Q3TUF7-1]
DR CTD; 55689; -.
DR MGI; MGI:2447762; Yeats2.
DR VEuPathDB; HostDB:ENSMUSG00000041215; -.
DR eggNOG; KOG3149; Eukaryota.
DR GeneTree; ENSGT00940000156789; -.
DR HOGENOM; CLU_258270_0_0_1; -.
DR InParanoid; Q3TUF7; -.
DR PhylomeDB; Q3TUF7; -.
DR TreeFam; TF314586; -.
DR BioGRID-ORCS; 208146; 19 hits in 77 CRISPR screens.
DR ChiTaRS; Yeats2; mouse.
DR PRO; PR:Q3TUF7; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q3TUF7; protein.
DR Bgee; ENSMUSG00000041215; Expressed in dorsal pancreas and 228 other tissues.
DR ExpressionAtlas; Q3TUF7; baseline and differential.
DR Genevisible; Q3TUF7; MM.
DR GO; GO:0140672; C:ATAC complex; IDA:ComplexPortal.
DR GO; GO:0072686; C:mitotic spindle; IDA:MGI.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0140030; F:modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0017025; F:TBP-class protein binding; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
DR GO; GO:0044154; P:histone H3-K14 acetylation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0051302; P:regulation of cell division; IDA:ComplexPortal.
DR GO; GO:0045995; P:regulation of embryonic development; IDA:ComplexPortal.
DR GO; GO:0031063; P:regulation of histone deacetylation; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; ISO:MGI.
DR Gene3D; 2.60.40.1970; -; 1.
DR InterPro; IPR038704; YEAST_sf.
DR InterPro; IPR005033; YEATS.
DR PANTHER; PTHR23195; PTHR23195; 1.
DR Pfam; PF03366; YEATS; 1.
DR PROSITE; PS51037; YEATS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..1407
FT /note="YEATS domain-containing protein 2"
FT /id="PRO_0000076367"
FT DOMAIN 201..346
FT /note="YEATS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00376"
FT REGION 116..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..262
FT /note="Histone H3K27cr binding"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT REGION 283..285
FT /note="Histone H3K27cr binding"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT REGION 462..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 54..80
FT /evidence="ECO:0000255"
FT COMPBIAS 117..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT MOD_RES 406
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 477
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT MOD_RES 1204
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT CROSSLNK 9
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT CROSSLNK 113
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT CROSSLNK 189
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT CROSSLNK 486
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT CROSSLNK 550
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT CROSSLNK 590
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT CROSSLNK 647
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT CROSSLNK 771
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT CROSSLNK 908
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT CROSSLNK 1095
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT CROSSLNK 1095
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT CROSSLNK 1115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT CROSSLNK 1207
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT CROSSLNK 1270
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULM3"
FT VAR_SEQ 1..53
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017006"
FT VAR_SEQ 1291..1305
FT /note="NIKKEQEEKQEEMRF -> SASVVNLLFVCSKET (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017007"
FT VAR_SEQ 1306..1407
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017008"
FT CONFLICT 310
FT /note="L -> V (in Ref. 2; BAC65745)"
FT /evidence="ECO:0000305"
FT CONFLICT 1162
FT /note="K -> E (in Ref. 1; BAE36014)"
FT /evidence="ECO:0000305"
FT CONFLICT 1294
FT /note="K -> R (in Ref. 1; BAE36014)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1407 AA; 148950 MW; E5530016D1846E2E CRC64;
MSGIKRTIKE TDPDYEDVSV ALPNKRHKAI ESSARDAAVQ KIETIIKEQF ALEMKNKEHE
IDVIDQRLIE ARRMMDKLRA CIVANYYASA GLLKVSEGLK TFDPMAFNHP AIKKFLESPS
RSSSPTNQRS ETPSANHSES DSLSQHNDFL SDKDNNSNVD VEERPPSTGE QRPSRKAGRD
TSSISGSHKR ELRNADLTGD ETSRLFVKKT IVVGNVSKYI PPDKREENDQ STHKWMVYVR
GSRREPSINH FVKKVWFFLH PSYKPNDLVE VREPPFHLTR RGWGEFPVRV QVHFKDSQNK
RIDIIHNLKL DRTYTGLQTL GAETVVDVEL HRHSLGEDSV YPQSSESDVC DAPPPTLTLP
AAVKASAVAQ SPEPAAAAPV GEGFPETTEA ERHSTFYSLP SSLERTPTKV TTAQKVTFSS
HGNSAFQPIA SSCKIVPQSQ VPNPESPGKS FQPITMSCKI VSGSPISTPS PSPLPRTPTS
TPVHLKQGTA SSGVSNPHVI VDKPGQVIGA STPSTGSPTS KLPVASQASQ GTGSPIPKIH
GSSFLTSTVK QEESLFASMP PLCPIGSHPK VQSPKAVTGG LGAFTKVIIK QEPGEAPHVS
TTGAASQSAF PQYVTVKGGH MIAVSPQKQV ISAGEGTTQS PKIAPSKVVG VPVGSALPST
VKQAVAISSG QILVAKASSS VTKAVGPKQV VTQGVAKAIV SGGGGTIVAQ PVQTLTKTQV
TAAGPQKSGS QGSVMATLQL PATNLANLAN LPPGTKLYLT TNSKNPSGKG KLLLIPQGAI
LRATNNANLQ SGSAAAGGSG SSGAGGGSGG GGGSGAGGTP STSGPGGGPQ HLTYTSYILK
QTPQGTFLVG QPSPQTPGKQ LTTASVVQGT LGVSSSSAQG QQTLKVISGQ KTTLFTQAAT
AGQASLLKLP DNTLKSVPAA PQLAKPGTTM LRVAGGVITA APSPAVAFSA NGAVHQSEGS
TPVSSSVGSI IKTPGQPQVC VSQATMATCK GPAAVAGTAA SLVSAPSSIS GKATVSGLLK
VHSAQSSPQQ AVLTIPSQLK PLSINTSGGV QTVLMPVNKV VQSFSTSKLP TTVLPISVPN
QAAPSSAPVA IAKVKTEPET PGPNCISQEN QVAVKTEESS ELSNYVIKVD HLETIQQLLT
AVVKKIPLIT AKGDDASCFS AKSLEQYYGW NIGKRRAAEW QRAMTVRKVL QEILEKNPRF
HHLTPLKTKH IAHWCRCHGY TPPDPESLRH DGDSIEDVLT QIDSEPECLS SFSTADDLCR
KLEDLQQFQK REPENEEEVD ILSLSEPLKT NIKKEQEEKQ EEMRFYLPPT PGSGFVGDIT
QKIGITLQPV ALHRNMYASV VEDMILKATE QLVSDILRQA LAVGYQTASP NRIPKEITVS
NIHQAICNIP FLDFLTNKHM GRLNEDQ
