DNS2A_HUMAN
ID DNS2A_HUMAN Reviewed; 360 AA.
AC O00115; B2RD06; B7Z4K6; O43910;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Deoxyribonuclease-2-alpha;
DE EC=3.1.22.1;
DE AltName: Full=Acid DNase;
DE AltName: Full=Deoxyribonuclease II alpha;
DE Short=DNase II alpha;
DE AltName: Full=Lysosomal DNase II;
DE AltName: Full=R31240_2;
DE Flags: Precursor;
GN Name=DNASE2; Synonyms=DNASE2A, DNL2;
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 [GENOMIC DNA].
RX PubMed=9924608; DOI=10.1046/j.1469-1809.1998.6240299.x;
RA Yasuda T., Takeshita H., Iida R., Tsutsumi S., Nakajima T., Hosomi O.,
RA Nakashima Y., Mori S., Kishi K.;
RT "Structure and organization of the human deoxyribonuclease II (DNase II)
RT gene.";
RL Ann. Hum. Genet. 62:299-305(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9647784; DOI=10.1006/bbrc.1998.8839;
RA Shiokawa D., Tanuma S.;
RT "Cloning of cDNAs encoding porcine and human DNase II.";
RL Biochem. Biophys. Res. Commun. 247:864-869(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9714827; DOI=10.1016/s0378-1119(98)00280-7;
RA Baker K.P., Baron W.F., Henzel W.J., Spencer S.A.;
RT "Molecular cloning and characterization of human and murine DNase II.";
RL Gene 215:281-289(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9812984; DOI=10.1074/jbc.273.47.30909;
RA Krieser R.J., Eastman A.;
RT "The cloning and expression of human deoxyribonuclease II. A possible role
RT in apoptosis.";
RL J. Biol. Chem. 273:30909-30914(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9446563; DOI=10.1074/jbc.273.5.2610;
RA Yasuda T., Takeshita H., Iida R., Nakajima T., Hosomi O., Nakashima Y.,
RA Kishi K.;
RT "Molecular cloning of the cDNA encoding human deoxyribonuclease II.";
RL J. Biol. Chem. 273:2610-2616(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [9]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
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 [11]
RP LACK OF PROTEOLYTIC PROCESSING, AND GLYCOSYLATION.
RX PubMed=11906178; DOI=10.1006/bbrc.2002.6687;
RA MacLea K.S., Krieser R.J., Eastman A.;
RT "Revised structure of the active form of human deoxyribonuclease IIalpha.";
RL Biochem. Biophys. Res. Commun. 292:415-421(2002).
RN [12]
RP MUTAGENESIS OF CYS-19; ASN-86; CYS-151; CYS-159; ASN-212; ASN-266; CYS-267;
RP ASN-290; CYS-299; CYS-308; CYS-327 AND CYS-347, GLYCOSYLATION, AND
RP DISULFIDE BONDS.
RX PubMed=12558498; DOI=10.1042/bj20021875;
RA MacLea K.S., Krieser R.J., Eastman A.;
RT "Structural requirements of human DNase II alpha for formation of the
RT active enzyme: the role of the signal peptide, N-glycosylation, and
RT disulphide bridging.";
RL Biochem. J. 371:867-876(2003).
RN [13]
RP MUTAGENESIS OF HIS-295.
RX PubMed=12594037; DOI=10.1016/s0378-1119(02)01233-7;
RA MacLea K.S., Krieser R.J., Eastman A.;
RT "A family history of deoxyribonuclease II: surprises from Trichinella
RT spiralis and Burkholderia pseudomallei.";
RL Gene 305:1-12(2003).
RN [14]
RP GLYCOSYLATION AT ASN-212.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Hydrolyzes DNA under acidic conditions with a preference for
CC double-stranded DNA. Plays a major role in the degradation of nuclear
CC DNA in cellular apoptosis during development. Necessary for proper
CC fetal development and for definitive erythropoiesis in fetal liver,
CC where it degrades nuclear DNA expelled from erythroid precursor cells.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-
CC phosphooligonucleotide end-products.; EC=3.1.22.1;
CC -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00115-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00115-2; Sequence=VSP_056921;
CC -!- PTM: Glycosylated. Mutations that eliminate N-glycosylation sites
CC reduce activity, but enzymatic deglycosylation has no effect.
CC {ECO:0000269|PubMed:11906178, ECO:0000269|PubMed:12558498,
CC ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:19159218}.
CC -!- MISCELLANEOUS: Not required for the generation of the characteristic
CC DNA fragmentation observed in apoptotic cells, but for the degradation
CC of DNA from dying cells. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNase II family. {ECO:0000305}.
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DR EMBL; AB008564; BAB55598.1; -; Genomic_DNA.
DR EMBL; AF060222; AAC39852.1; -; mRNA.
DR EMBL; AF045937; AAC35751.1; -; mRNA.
DR EMBL; AF047016; AAC77366.1; -; mRNA.
DR EMBL; AB004574; BAA28623.1; -; mRNA.
DR EMBL; BT007047; AAP35696.1; -; mRNA.
DR EMBL; AK297493; BAH12592.1; -; mRNA.
DR EMBL; AK315358; BAG37753.1; -; mRNA.
DR EMBL; AC020934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AD000092; AAB51172.1; -; Genomic_DNA.
DR EMBL; CH471106; EAW84320.1; -; Genomic_DNA.
DR EMBL; BC010419; AAH10419.3; -; mRNA.
DR EMBL; BC065209; AAH65209.1; -; mRNA.
DR CCDS; CCDS12284.1; -. [O00115-1]
DR PIR; JE0206; JE0206.
DR PIR; T45071; T45071.
DR RefSeq; NP_001366.1; NM_001375.2. [O00115-1]
DR AlphaFoldDB; O00115; -.
DR SMR; O00115; -.
DR BioGRID; 108116; 23.
DR IntAct; O00115; 3.
DR STRING; 9606.ENSP00000222219; -.
DR BindingDB; O00115; -.
DR ChEMBL; CHEMBL1250342; -.
DR GlyConnect; 1170; 2 N-Linked glycans (2 sites).
DR GlyGen; O00115; 4 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; O00115; -.
DR PhosphoSitePlus; O00115; -.
DR BioMuta; DNASE2; -.
DR EPD; O00115; -.
DR jPOST; O00115; -.
DR MassIVE; O00115; -.
DR MaxQB; O00115; -.
DR PaxDb; O00115; -.
DR PeptideAtlas; O00115; -.
DR PRIDE; O00115; -.
DR ProteomicsDB; 47717; -. [O00115-1]
DR ProteomicsDB; 6606; -.
DR Antibodypedia; 13408; 230 antibodies from 32 providers.
DR DNASU; 1777; -.
DR Ensembl; ENST00000222219.8; ENSP00000222219.2; ENSG00000105612.9. [O00115-1]
DR GeneID; 1777; -.
DR KEGG; hsa:1777; -.
DR MANE-Select; ENST00000222219.8; ENSP00000222219.2; NM_001375.3; NP_001366.1.
DR UCSC; uc002mvn.2; human. [O00115-1]
DR CTD; 1777; -.
DR DisGeNET; 1777; -.
DR GeneCards; DNASE2; -.
DR HGNC; HGNC:2960; DNASE2.
DR HPA; ENSG00000105612; Low tissue specificity.
DR MIM; 126350; gene.
DR neXtProt; NX_O00115; -.
DR OpenTargets; ENSG00000105612; -.
DR PharmGKB; PA27431; -.
DR VEuPathDB; HostDB:ENSG00000105612; -.
DR eggNOG; KOG3825; Eukaryota.
DR GeneTree; ENSGT00390000002634; -.
DR HOGENOM; CLU_053867_0_1_1; -.
DR InParanoid; O00115; -.
DR OMA; ILYNDQK; -.
DR PhylomeDB; O00115; -.
DR TreeFam; TF314536; -.
DR BRENDA; 3.1.22.1; 2681.
DR PathwayCommons; O00115; -.
DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
DR SignaLink; O00115; -.
DR BioGRID-ORCS; 1777; 36 hits in 1076 CRISPR screens.
DR ChiTaRS; DNASE2; human.
DR GenomeRNAi; 1777; -.
DR Pharos; O00115; Tbio.
DR PRO; PR:O00115; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O00115; protein.
DR Bgee; ENSG00000105612; Expressed in pancreatic ductal cell and 181 other tissues.
DR ExpressionAtlas; O00115; baseline and differential.
DR Genevisible; O00115; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; TAS:ProtInc.
DR GO; GO:0004531; F:deoxyribonuclease II activity; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0006309; P:apoptotic DNA fragmentation; IBA:GO_Central.
DR GO; GO:0006259; P:DNA metabolic process; TAS:ProtInc.
DR GO; GO:0043353; P:enucleate erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0050776; P:regulation of immune response; IEA:Ensembl.
DR InterPro; IPR004947; DNase_II.
DR PANTHER; PTHR10858; PTHR10858; 1.
DR Pfam; PF03265; DNase_II; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Developmental protein; Disulfide bond;
KW Endonuclease; Glycoprotein; Hydrolase; Lysosome; Nuclease;
KW Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..360
FT /note="Deoxyribonuclease-2-alpha"
FT /id="PRO_0000007291"
FT ACT_SITE 295
FT /evidence="ECO:0000305"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 19..159
FT /evidence="ECO:0000255"
FT DISULFID 267..347
FT /evidence="ECO:0000255"
FT DISULFID 308..327
FT /evidence="ECO:0000255"
FT VAR_SEQ 116..170
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056921"
FT VARIANT 39
FT /note="R -> I (in dbSNP:rs36075196)"
FT /id="VAR_048870"
FT VARIANT 204
FT /note="H -> R (in dbSNP:rs16978744)"
FT /id="VAR_048871"
FT VARIANT 314
FT /note="R -> L (in dbSNP:rs1061192)"
FT /id="VAR_012044"
FT MUTAGEN 19
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12558498"
FT MUTAGEN 86
FT /note="N->Q: Reduced N-glycosylation, complete loss of N-
FT glycosylation; when associated with Q-212; Q-266 and Q-
FT 290."
FT /evidence="ECO:0000269|PubMed:12558498"
FT MUTAGEN 151
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12558498"
FT MUTAGEN 159
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12558498"
FT MUTAGEN 212
FT /note="N->Q: Reduced N-glycosylation, complete loss of N-
FT glycosylation; when associated with Q-86; Q-266 and Q-290."
FT /evidence="ECO:0000269|PubMed:12558498"
FT MUTAGEN 266
FT /note="N->Q: Reduced N-glycosylation, complete loss of N-
FT glycosylation; when associated with Q-86; Q-212 and Q-290."
FT /evidence="ECO:0000269|PubMed:12558498"
FT MUTAGEN 267
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12558498"
FT MUTAGEN 290
FT /note="N->Q: Reduced N-glycosylation, complete loss of N-
FT glycosylation; when associated with Q-86; Q-212 and Q-266."
FT /evidence="ECO:0000269|PubMed:12558498"
FT MUTAGEN 295
FT /note="H->A,K,N,R,S: Loss of activity, but not of DNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:12594037"
FT MUTAGEN 299
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:12558498"
FT MUTAGEN 308
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12558498"
FT MUTAGEN 327
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12558498"
FT MUTAGEN 347
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12558498"
FT CONFLICT 160..171
FT /note="Missing (in Ref. 8; AAB51172)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 39581 MW; DF1BBFBA8A9676EA CRC64;
MIPLLLAALL CVPAGALTCY GDSGQPVDWF VVYKLPALRG SGEAAQRGLQ YKYLDESSGG
WRDGRALINS PEGAVGRSLQ PLYRSNTSQL AFLLYNDQPP QPSKAQDSSM RGHTKGVLLL
DHDGGFWLVH SVPNFPPPAS SAAYSWPHSA CTYGQTLLCV SFPFAQFSKM GKQLTYTYPW
VYNYQLEGIF AQEFPDLENV VKGHHVSQEP WNSSITLTSQ AGAVFQSFAK FSKFGDDLYS
GWLAAALGTN LQVQFWHKTV GILPSNCSDI WQVLNVNQIA FPGPAGPSFN STEDHSKWCV
SPKGPWTCVG DMNRNQGEEQ RGGGTLCAQL PALWKAFQPL VKNYQPCNGM ARKPSRAYKI
