ID ETS2_HUMAN Reviewed; 469 AA. AC P15036; A6NM68; D3DSH6; Q53Y89; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 04-NOV-2026, entry version 228. DE RecName: Full=Protein C-ets-2; GN Name=ETS2; 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]. RX PubMed=2847145; DOI=10.1073/pnas.85.21.7862; RA Watson D.K., McWilliams M.J., Lapis P., Lautenberger J.A., RA Schweinfest C.W., Papas T.S.; RT "Mammalian ets-1 and ets-2 genes encode highly conserved proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 85:7862-7866(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Zimmermann W.W.K., Korenberg J., Rosenthal A., Schattevoy R.; RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10830953; DOI=10.1038/35012518; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U., RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.; RT "The DNA sequence of human chromosome 21."; RL Nature 405:311-319(2000). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Colon; 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 [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 399-469. RX PubMed=2250910; RA Watson D.K., Mavrothalassitis G.J., Jorcyk C.L., Smyth F.E., Papas T.S.; RT "Molecular organization and differential polyadenylation sites of the human RT ETS2 gene."; RL Oncogene 5:1521-1527(1990). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 324-469. RX PubMed=2997781; DOI=10.1073/pnas.82.21.7294; RA Watson D.K., McWilliams-Smith M.J., Nunn M.F., Duesberg P.H., O'Brien S.J., RA Papas T.S.; RT "The ets sequence from the transforming gene of avian erythroblastosis RT virus, E26, has unique domains on human chromosomes 11 and 21: both loci RT are transcriptionally active."; RL Proc. Natl. Acad. Sci. U.S.A. 82:7294-7298(1985). RN [10] RP FUNCTION AS A TRANSCRIPTIONAL ACTIVATOR. RX PubMed=11909962; DOI=10.1128/mcb.22.8.2687-2702.2002; RA Wasylyk C., Schlumberger S.E., Criqui-Filipe P., Wasylyk B.; RT "Sp100 interacts with ETS-1 and stimulates its transcriptional activity."; RL Mol. Cell. Biol. 22:2687-2702(2002). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [12] RP PHOSPHORYLATION AT SER-220 AND SER-225. RX PubMed=24218572; DOI=10.1073/pnas.1306814110; RA Guen V.J., Gamble C., Flajolet M., Unger S., Thollet A., Ferandin Y., RA Superti-Furga A., Cohen P.A., Meijer L., Colas P.; RT "CDK10/cyclin M is a protein kinase that controls ETS2 degradation and is RT deficient in STAR syndrome."; RL Proc. Natl. Acad. Sci. U.S.A. 110:19525-19530(2013). CC -!- FUNCTION: Transcription factor activating transcription. Binds CC specifically the DNA GGAA/T core motif (Ets-binding site or EBS) in CC gene promoters and stimulates transcription. CC {ECO:0000269|PubMed:11909962}. CC -!- INTERACTION: CC P15036; Q15131: CDK10; NbExp=2; IntAct=EBI-1646991, EBI-1646959; CC P15036; Q8NHY2: COP1; NbExp=2; IntAct=EBI-1646991, EBI-1176214; CC P15036; Q16236: NFE2L2; NbExp=2; IntAct=EBI-1646991, EBI-2007911; CC P15036; P17612: PRKACA; NbExp=3; IntAct=EBI-1646991, EBI-476586; CC P15036; P50454: SERPINH1; NbExp=3; IntAct=EBI-1646991, EBI-350723; CC P15036; P37173: TGFBR2; NbExp=3; IntAct=EBI-1646991, EBI-296151; CC P15036; P04637: TP53; NbExp=4; IntAct=EBI-1646991, EBI-366083; CC P15036; Q15672: TWIST1; NbExp=2; IntAct=EBI-1646991, EBI-1797287; CC P15036; Q8WVJ9: TWIST2; NbExp=2; IntAct=EBI-1646991, EBI-1797313; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- PTM: Phosphorylation by CDK10 at Ser-220 and Ser-225 creates a CC phosphodegron that targets ETS2 for proteasomal degradation. CC {ECO:0000269|PubMed:24218572}. CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/40503/ETS2"; 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; J04102; AAA52412.1; -; mRNA. DR EMBL; AF017257; AAB94057.1; -; Genomic_DNA. DR EMBL; AK315563; BAG37939.1; -; mRNA. DR EMBL; BT006838; AAP35484.1; -; mRNA. DR EMBL; AL163278; CAB90468.1; -; Genomic_DNA. DR EMBL; AP001732; BAA95514.1; -; Genomic_DNA. DR EMBL; AP001040; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471079; EAX09673.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09674.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09676.1; -; Genomic_DNA. DR EMBL; BC017040; AAH17040.1; -; mRNA. DR EMBL; BC042954; AAH42954.1; -; mRNA. DR EMBL; X55181; CAA38966.1; -; Genomic_DNA. DR EMBL; M11922; AAA52411.1; -; mRNA. DR CCDS; CCDS13659.1; -. DR PIR; B32066; TVHUE2. DR RefSeq; NP_005230.1; NM_005239.6. DR RefSeq; XP_005260992.1; XM_005260935.2. DR RefSeq; XP_016883779.1; XM_017028290.2. DR RefSeq; XP_054180345.1; XM_054324370.1. DR PDB; 4BQA; X-ray; 2.50 A; A/D/G=325-464. DR PDB; 4MHV; X-ray; 2.45 A; A/B=76-170. DR AlphaFoldDB; P15036; -. DR SMR; P15036; -. DR BioGRID; 108415; 52. DR CORUM; P15036; -. DR DIP; DIP-40452N; -. DR FunCoup; P15036; 2195. DR IntAct; P15036; 41. DR NDEx; IQUERY-CP-ETS2; 5 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000353344; -. DR GlyGen; P15036; 1 site. DR iPTMnet; P15036; -. DR PhosphoSitePlus; P15036; -. DR BioMuta; ETS2; -. DR DMDM; 119645; -. DR jPOST; P15036; -. DR MassIVE; P15036; -. DR PaxDb; 9606-ENSP00000353344; -. DR PeptideAtlas; P15036; -. DR ProteomicsDB; 53101; -. DR Pumba; P15036; -. DR Antibodypedia; 8721; 463 antibodies from 36 providers. DR DNASU; 2114; -. DR Ensembl; ENST00000360214.8; ENSP00000353344.3; ENSG00000157557.14. DR Ensembl; ENST00000360938.8; ENSP00000354194.3; ENSG00000157557.14. DR Ensembl; ENST00000653642.1; ENSP00000499315.1; ENSG00000157557.14. DR Ensembl; ENST00000662305.1; ENSP00000499226.1; ENSG00000157557.14. DR Ensembl; ENST00000666778.1; ENSP00000499775.1; ENSG00000157557.14. DR Ensembl; ENST00000859949.1; ENSP00000530008.1; ENSG00000157557.14. DR Ensembl; ENST00000859950.1; ENSP00000530009.1; ENSG00000157557.14. DR Ensembl; ENST00000859953.1; ENSP00000530012.1; ENSG00000157557.14. DR Ensembl; ENST00000859954.1; ENSP00000530013.1; ENSG00000157557.14. DR Ensembl; ENST00000938968.1; ENSP00000609027.1; ENSG00000157557.14. DR Ensembl; ENST00000938970.1; ENSP00000609029.1; ENSG00000157557.14. DR Ensembl; ENST00000968689.1; ENSP00000638748.1; ENSG00000157557.14. DR Ensembl; ENST00000968690.1; ENSP00000638749.1; ENSG00000157557.14. DR GeneID; 2114; -. DR KEGG; hsa:2114; -. DR MANE-Select; ENST00000360938.8; ENSP00000354194.3; NM_005239.6; NP_005230.1. DR UCSC; uc002yxf.4; human. DR AGR; HGNC:3489; -. DR CIViC; 2114; 1 evidence item across 1 molecular profile. DR ClinPGx; PA27903; -. DR CTD; 2114; -. DR DisGeNET; 2114; -. DR GeneCards; ETS2; -. DR HGNC; HGNC:3489; ETS2. DR HPA; ENSG00000157557; Low tissue specificity. DR MIM; 164740; gene. DR OpenTargets; ENSG00000157557; -. DR VEuPathDB; HostDB:ENSG00000157557; -. DR eggNOG; KOG3806; Eukaryota. DR GeneTree; ENSGT00940000160202; -. DR HOGENOM; CLU_031197_1_1_1; -. DR InParanoid; P15036; -. DR OMA; AANCELP; -. DR OrthoDB; 10067219at2759; -. DR PAN-GO; P15036; 4 GO annotations based on evolutionary models. DR PhylomeDB; P15036; -. DR PathwayCommons; P15036; -. DR Reactome; R-HSA-2559585; Oncogene Induced Senescence. DR SignaLink; P15036; -. DR SIGNOR; P15036; -. DR Agora; ENSG00000157557; -. DR BioGRID-ORCS; 2114; 25 hits in 1181 CRISPR screens. DR ChiTaRS; ETS2; human. DR EvolutionaryTrace; P15036; -. DR GeneWiki; ETS2; -. DR GenomeRNAi; 2114; -. DR Pharos; P15036; Tbio. DR PRO; PR:P15036; -. DR Proteomes; UP000005640; Chromosome 21. DR RNAct; P15036; protein. DR Bgee; ENSG00000157557; Expressed in skin of abdomen and 203 other cell types or tissues. DR ExpressionAtlas; P15036; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; TAS:ProtInc. DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:ProtInc. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; IEA:Ensembl. DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:BHF-UCL. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc. DR CDD; cd08543; SAM_PNT-ETS-2; 1. DR FunFam; 1.10.10.10:FF:000097; Protein c-ets-1 isoform 1; 1. DR FunFam; 1.10.150.50:FF:000014; Protein c-ets-1 isoform 1; 1. DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR045688; Ets1_N_flank. DR InterPro; IPR000418; Ets_dom. DR InterPro; IPR046328; ETS_fam. DR InterPro; IPR003118; Pointed_dom. DR InterPro; IPR013761; SAM/pointed_sf. DR InterPro; IPR016311; Transform_prot_C-ets. DR InterPro; IPR027276; Transform_prot_C-ets-2. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR11849; ETS; 1. DR PANTHER; PTHR11849:SF188; PROTEIN C-ETS-2; 1. DR Pfam; PF00178; Ets; 1. DR Pfam; PF19525; Ets1_N_flank; 1. DR Pfam; PF02198; SAM_PNT; 1. DR PIRSF; PIRSF501032; C-ets-2; 1. DR PIRSF; PIRSF001698; Transforming_factor_C-ets; 1. DR PRINTS; PR00454; ETSDOMAIN. DR SMART; SM00413; ETS; 1. DR SMART; SM00251; SAM_PNT; 1. DR SUPFAM; SSF47769; SAM/Pointed domain; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS00345; ETS_DOMAIN_1; 1. DR PROSITE; PS00346; ETS_DOMAIN_2; 1. DR PROSITE; PS50061; ETS_DOMAIN_3; 1. DR PROSITE; PS51433; PNT; 1. PE 1: Evidence at protein level; KW 3D-structure; DNA-binding; Nucleus; Phosphoprotein; KW Proteomics identification; Proto-oncogene; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1..469 FT /note="Protein C-ets-2" FT /id="PRO_0000204077" FT DOMAIN 85..170 FT /note="PNT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00762" FT DNA_BIND 363..443 FT /note="ETS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237" FT REGION 264..289 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 220 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:24218572" FT MOD_RES 225 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:24218572" FT MOD_RES 295 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 298 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P15037" FT MOD_RES 301 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P15037" FT HELIX 78..84 FT /evidence="ECO:0007829|PDB:4MHV" FT HELIX 85..89 FT /evidence="ECO:0007829|PDB:4MHV" FT HELIX 90..96 FT /evidence="ECO:0007829|PDB:4MHV" FT HELIX 103..105 FT /evidence="ECO:0007829|PDB:4MHV" FT HELIX 108..121 FT /evidence="ECO:0007829|PDB:4MHV" FT HELIX 129..132 FT /evidence="ECO:0007829|PDB:4MHV" FT HELIX 136..141 FT /evidence="ECO:0007829|PDB:4MHV" FT HELIX 144..150 FT /evidence="ECO:0007829|PDB:4MHV" FT HELIX 155..169 FT /evidence="ECO:0007829|PDB:4MHV" FT HELIX 331..334 FT /evidence="ECO:0007829|PDB:4BQA" FT HELIX 335..337 FT /evidence="ECO:0007829|PDB:4BQA" FT STRAND 338..342 FT /evidence="ECO:0007829|PDB:4BQA" FT STRAND 344..346 FT /evidence="ECO:0007829|PDB:4BQA" FT HELIX 351..358 FT /evidence="ECO:0007829|PDB:4BQA" FT HELIX 365..373 FT /evidence="ECO:0007829|PDB:4BQA" FT HELIX 376..378 FT /evidence="ECO:0007829|PDB:4BQA" FT TURN 379..381 FT /evidence="ECO:0007829|PDB:4BQA" FT STRAND 382..384 FT /evidence="ECO:0007829|PDB:4BQA" FT STRAND 390..392 FT /evidence="ECO:0007829|PDB:4BQA" FT HELIX 396..407 FT /evidence="ECO:0007829|PDB:4BQA" FT HELIX 414..422 FT /evidence="ECO:0007829|PDB:4BQA" FT TURN 423..428 FT /evidence="ECO:0007829|PDB:4BQA" FT STRAND 429..432 FT /evidence="ECO:0007829|PDB:4BQA" FT STRAND 439..442 FT /evidence="ECO:0007829|PDB:4BQA" FT HELIX 446..450 FT /evidence="ECO:0007829|PDB:4BQA" FT HELIX 454..457 FT /evidence="ECO:0007829|PDB:4BQA" SQ SEQUENCE 469 AA; 53001 MW; 5944EC4B5AAB553E CRC64; MNDFGIKNMD QVAPVANSYR GTLKRQPAFD TFDGSLFAVF PSLNEEQTLQ EVPTGLDSIS HDSANCELPL LTPCSKAVMS QALKATFSGF KKEQRRLGIP KNPWLWSEQQ VCQWLLWATN EFSLVNVNLQ RFGMNGQMLC NLGKERFLEL APDFVGDILW EHLEQMIKEN QEKTEDQYEE NSHLTSVPHW INSNTLGFGT EQAPYGMQTQ NYPKGGLLDS MCPASTPSVL SSEQEFQMFP KSRLSSVSVT YCSVSQDFPG SNLNLLTNNS GTPKDHDSPE NGADSFESSD SLLQSWNSQS SLLDVQRVPS FESFEDDCSQ SLCLNKPTMS FKDYIQERSD PVEQGKPVIP AAVLAGFTGS GPIQLWQFLL ELLSDKSCQS FISWTGDGWE FKLADPDEVA RRWGKRKNKP KMNYEKLSRG LRYYYDKNII HKTSGKRYVY RFVCDLQNLL GFTPEELHAI LGVQPDTED //