SUBT_BACAM
ID SUBT_BACAM Reviewed; 382 AA.
AC P00782; P83945; Q44684;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Subtilisin BPN';
DE EC=3.4.21.62;
DE AltName: Full=Alkaline protease;
DE AltName: Full=Subtilisin DFE;
DE AltName: Full=Subtilisin Novo;
DE Flags: Precursor;
GN Name=apr;
OS Bacillus amyloliquefaciens (Bacillus velezensis).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus amyloliquefaciens group.
OX NCBI_TaxID=1390;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 23844 / P;
RX PubMed=6090391; DOI=10.1128/jb.159.3.811-819.1984;
RA Vasantha N., Thompson L.D., Rhodes C., Banner C., Nagle J., Filpula D.;
RT "Genes for alkaline protease and neutral protease from Bacillus
RT amyloliquefaciens contain a large open reading frame between the regions
RT coding for signal sequence and mature protein.";
RL J. Bacteriol. 159:811-819(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-382.
RX PubMed=6316278; DOI=10.1093/nar/11.22.7911;
RA Wells J.A., Ferrari E., Henner D.J., Estell D.A., Chen E.Y.;
RT "Cloning, sequencing, and secretion of Bacillus amyloliquefaciens
RT subtilisin in Bacillus subtilis.";
RL Nucleic Acids Res. 11:7911-7925(1983).
RN [3]
RP PROTEIN SEQUENCE OF 108-382.
RX PubMed=6065094; DOI=10.1016/s0021-9258(18)99412-3;
RA Markland F.S., Smith E.L.;
RT "Subtilisin BPN. VII. Isolation of cyanogen bromide peptides and the
RT complete amino acid sequence.";
RL J. Biol. Chem. 242:5198-5211(1967).
RN [4]
RP PROTEIN SEQUENCE OF 108-131, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, AND VARIANT PHE-128.
RC STRAIN=DC-4;
RX PubMed=12524032; DOI=10.1016/s1096-4959(02)00183-5;
RA Peng Y., Huang Q., Zhang R.-H., Zhang Y.-Z.;
RT "Purification and characterization of a fibrinolytic enzyme produced by
RT Bacillus amyloliquefaciens DC-4 screened from douchi, a traditional Chinese
RT soybean food.";
RL Comp. Biochem. Physiol. 134B:45-52(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=4399039; DOI=10.1098/rstb.1970.0014;
RA Alden R.A., Wright C.S., Kraut J.;
RT "A hydrogen-bond network at the active site of subtilisin BPN'.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 257:119-124(1970).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
RX PubMed=6387152; DOI=10.1016/0022-2836(84)90150-5;
RA Hirono S., Akagawa H., Mitsui Y., Iitaka Y.;
RT "Crystal structure at 2.6-A resolution of the complex of subtilisin BPN'
RT with streptomyces subtilisin inhibitor.";
RL J. Mol. Biol. 178:389-413(1984).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT.
RX PubMed=2684274; DOI=10.1021/bi00444a012;
RA Pantoliano M.W., Whitlow M., Wood J.F., Dodd S.W., Hardman K.D.,
RA Rollence M.L., Bryan P.N.;
RT "Large increases in general stability for subtilisin BPN' through
RT incremental changes in the free energy of unfolding.";
RL Biochemistry 28:7205-7213(1989).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=15299573; DOI=10.1107/s0907444996007500;
RA Gallagher T., Oliver J., Bott R., Betzel C., Gilliland G.L.;
RT "Subtilisin BPN' at 1.6-A resolution: analysis for discrete disorder and
RT comparison of crystal forms.";
RL Acta Crystallogr. D 52:1125-1135(1996).
RN [9]
RP ACTIVE SITE.
RX PubMed=5249818; DOI=10.1073/pnas.61.4.1440;
RA Markland F.S., Shaw E., Smith E.L.;
RT "Identification of histidine 64 in the active site of subtilisin.";
RL Proc. Natl. Acad. Sci. U.S.A. 61:1440-1447(1968).
CC -!- FUNCTION: Subtilisin is an extracellular alkaline serine protease, it
CC catalyzes the hydrolysis of proteins and peptide amides. Has a high
CC substrate specificity to fibrin. {ECO:0000269|PubMed:12524032}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity for peptide
CC bonds, and a preference for a large uncharged residue in P1.
CC Hydrolyzes peptide amides.; EC=3.4.21.62;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 2 calcium ions per subunit.;
CC -!- ACTIVITY REGULATION: Completely inhibited by phenylmethylsulfony
CC fluoride (PMSF) and partially inhibited by benzamidine hydrochloride,
CC leupeptin, and pepstatin A. {ECO:0000269|PubMed:12524032}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:12524032};
CC Temperature dependence:
CC Optimum temperature is 48 degrees Celsius.
CC {ECO:0000269|PubMed:12524032};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12524032}.
CC -!- INTERACTION:
CC P00782; Q40059: Ica-2; Xeno; NbExp=8; IntAct=EBI-1033955, EBI-1040468;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- BIOTECHNOLOGY: Used as a detergent protease. Sold under the name
CC Alcalase by Novozymes.
CC -!- MISCELLANEOUS: Secretion of subtilisin is associated with onset of
CC sporulation, and many mutations which block sporulation at early stages
CC affect expression levels of subtilisin. However, subtilisin is not
CC necessary for normal sporulation.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA24990.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; K02496; AAB05345.1; -; Genomic_DNA.
DR EMBL; X00165; CAA24990.1; ALT_INIT; Genomic_DNA.
DR PIR; B25415; SUBSN.
DR RefSeq; WP_013351733.1; NZ_VRTX01000004.1.
DR PDB; 1A2Q; X-ray; 1.80 A; A=108-382.
DR PDB; 1AK9; X-ray; 1.80 A; A=108-382.
DR PDB; 1AQN; X-ray; 1.80 A; A=108-382.
DR PDB; 1AU9; X-ray; 1.80 A; A=108-382.
DR PDB; 1DUI; X-ray; 2.00 A; A=108-382.
DR PDB; 1GNS; X-ray; 1.80 A; A=112-382.
DR PDB; 1GNV; X-ray; 1.90 A; A=108-382.
DR PDB; 1LW6; X-ray; 1.50 A; E=108-382.
DR PDB; 1S01; X-ray; 1.70 A; A=108-382.
DR PDB; 1S02; X-ray; 1.90 A; A=108-382.
DR PDB; 1SBH; X-ray; 1.80 A; A=108-382.
DR PDB; 1SBI; X-ray; 2.20 A; A=108-382.
DR PDB; 1SBN; X-ray; 2.10 A; E=108-382.
DR PDB; 1SBT; X-ray; 2.50 A; A=108-382.
DR PDB; 1SIB; X-ray; 2.40 A; E=108-382.
DR PDB; 1SPB; X-ray; 2.00 A; P=37-107, S=108-382.
DR PDB; 1ST2; X-ray; 2.00 A; A=108-382.
DR PDB; 1SUA; X-ray; 2.10 A; A=108-382.
DR PDB; 1SUB; X-ray; 1.75 A; A=108-382.
DR PDB; 1SUC; X-ray; 1.80 A; A=108-382.
DR PDB; 1SUD; X-ray; 1.90 A; A=108-382.
DR PDB; 1SUE; X-ray; 1.80 A; A=108-382.
DR PDB; 1SUP; X-ray; 1.60 A; A=108-382.
DR PDB; 1TM1; X-ray; 1.70 A; E=108-382.
DR PDB; 1TM3; X-ray; 1.57 A; E=108-382.
DR PDB; 1TM4; X-ray; 1.70 A; E=108-382.
DR PDB; 1TM5; X-ray; 1.45 A; E=108-382.
DR PDB; 1TM7; X-ray; 1.59 A; E=108-382.
DR PDB; 1TMG; X-ray; 1.67 A; E=108-382.
DR PDB; 1TO1; X-ray; 1.68 A; E=108-382.
DR PDB; 1TO2; X-ray; 1.30 A; E=108-382.
DR PDB; 1UBN; X-ray; 2.40 A; A=108-382.
DR PDB; 1V5I; X-ray; 1.50 A; A=108-382.
DR PDB; 1Y1K; X-ray; 1.56 A; E=108-382.
DR PDB; 1Y33; X-ray; 1.80 A; E=108-382.
DR PDB; 1Y34; X-ray; 1.55 A; E=108-382.
DR PDB; 1Y3B; X-ray; 1.80 A; E=108-382.
DR PDB; 1Y3C; X-ray; 1.69 A; E=108-382.
DR PDB; 1Y3D; X-ray; 1.80 A; E=108-382.
DR PDB; 1Y3F; X-ray; 1.72 A; E=108-382.
DR PDB; 1Y48; X-ray; 1.84 A; E=108-382.
DR PDB; 1Y4A; X-ray; 1.60 A; E=108-382.
DR PDB; 1Y4D; X-ray; 2.00 A; E=108-382.
DR PDB; 1YJA; X-ray; 1.80 A; A=108-382.
DR PDB; 1YJB; X-ray; 1.80 A; A=108-382.
DR PDB; 1YJC; X-ray; 1.80 A; A=108-382.
DR PDB; 2SBT; X-ray; 2.80 A; A=108-382.
DR PDB; 2SIC; X-ray; 1.80 A; E=108-382.
DR PDB; 2SNI; X-ray; 2.10 A; E=108-382.
DR PDB; 2ST1; X-ray; 1.80 A; A=108-382.
DR PDB; 3BGO; X-ray; 1.80 A; P=32-111, S=108-382.
DR PDB; 3CNQ; X-ray; 1.71 A; P=32-111, S=108-382.
DR PDB; 3CO0; X-ray; 1.93 A; P=32-111, S=108-382.
DR PDB; 3F49; X-ray; 1.70 A; S=108-382.
DR PDB; 3SIC; X-ray; 1.80 A; E=108-382.
DR PDB; 5OX2; X-ray; 2.24 A; A=108-382.
DR PDB; 5SIC; X-ray; 2.20 A; E=108-382.
DR PDB; 7AM3; X-ray; 1.61 A; A=108-382.
DR PDB; 7AM4; X-ray; 1.81 A; A=108-382.
DR PDB; 7AM5; X-ray; 2.30 A; A=108-382.
DR PDB; 7AM6; X-ray; 2.70 A; A/B/C=108-382.
DR PDB; 7AM7; X-ray; 2.61 A; A/B/C=108-382.
DR PDB; 7AM8; X-ray; 2.04 A; A=108-382.
DR PDBsum; 1A2Q; -.
DR PDBsum; 1AK9; -.
DR PDBsum; 1AQN; -.
DR PDBsum; 1AU9; -.
DR PDBsum; 1DUI; -.
DR PDBsum; 1GNS; -.
DR PDBsum; 1GNV; -.
DR PDBsum; 1LW6; -.
DR PDBsum; 1S01; -.
DR PDBsum; 1S02; -.
DR PDBsum; 1SBH; -.
DR PDBsum; 1SBI; -.
DR PDBsum; 1SBN; -.
DR PDBsum; 1SBT; -.
DR PDBsum; 1SIB; -.
DR PDBsum; 1SPB; -.
DR PDBsum; 1ST2; -.
DR PDBsum; 1SUA; -.
DR PDBsum; 1SUB; -.
DR PDBsum; 1SUC; -.
DR PDBsum; 1SUD; -.
DR PDBsum; 1SUE; -.
DR PDBsum; 1SUP; -.
DR PDBsum; 1TM1; -.
DR PDBsum; 1TM3; -.
DR PDBsum; 1TM4; -.
DR PDBsum; 1TM5; -.
DR PDBsum; 1TM7; -.
DR PDBsum; 1TMG; -.
DR PDBsum; 1TO1; -.
DR PDBsum; 1TO2; -.
DR PDBsum; 1UBN; -.
DR PDBsum; 1V5I; -.
DR PDBsum; 1Y1K; -.
DR PDBsum; 1Y33; -.
DR PDBsum; 1Y34; -.
DR PDBsum; 1Y3B; -.
DR PDBsum; 1Y3C; -.
DR PDBsum; 1Y3D; -.
DR PDBsum; 1Y3F; -.
DR PDBsum; 1Y48; -.
DR PDBsum; 1Y4A; -.
DR PDBsum; 1Y4D; -.
DR PDBsum; 1YJA; -.
DR PDBsum; 1YJB; -.
DR PDBsum; 1YJC; -.
DR PDBsum; 2SBT; -.
DR PDBsum; 2SIC; -.
DR PDBsum; 2SNI; -.
DR PDBsum; 2ST1; -.
DR PDBsum; 3BGO; -.
DR PDBsum; 3CNQ; -.
DR PDBsum; 3CO0; -.
DR PDBsum; 3F49; -.
DR PDBsum; 3SIC; -.
DR PDBsum; 5OX2; -.
DR PDBsum; 5SIC; -.
DR PDBsum; 7AM3; -.
DR PDBsum; 7AM4; -.
DR PDBsum; 7AM5; -.
DR PDBsum; 7AM6; -.
DR PDBsum; 7AM7; -.
DR PDBsum; 7AM8; -.
DR AlphaFoldDB; P00782; -.
DR SMR; P00782; -.
DR IntAct; P00782; 2.
DR MINT; P00782; -.
DR STRING; 692420.BAMF_1119; -.
DR DrugBank; DB03297; Benzylsulfonic acid.
DR DrugBank; DB04491; Diisopropylphosphono Group.
DR DrugBank; DB02442; Dioxyselenocysteine.
DR DrugBank; DB01805; Monoisopropylphosphorylserine.
DR DrugBank; DB01915; S-Hydroxycysteine.
DR MEROPS; I09.001; -.
DR MEROPS; S08.034; -.
DR PRIDE; P00782; -.
DR eggNOG; COG1404; Bacteria.
DR OMA; SGQYSWI; -.
DR BRENDA; 3.4.21.62; 630.
DR SABIO-RK; P00782; -.
DR EvolutionaryTrace; P00782; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0042730; P:fibrinolysis; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR CDD; cd07477; Peptidases_S8_Subtilisin_subset; 1.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR034202; Subtilisin_Carlsberg-like.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Hydrolase; Metal-binding;
KW Protease; Secreted; Serine protease; Signal; Sporulation; Zymogen.
FT SIGNAL 1..30
FT /evidence="ECO:0000250"
FT PROPEP 31..107
FT /evidence="ECO:0000269|PubMed:12524032,
FT ECO:0000269|PubMed:6065094"
FT /id="PRO_0000027177"
FT CHAIN 108..382
FT /note="Subtilisin BPN'"
FT /id="PRO_0000027178"
FT DOMAIN 39..105
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 112..381
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 139
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240,
FT ECO:0000269|PubMed:5249818"
FT ACT_SITE 171
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240,
FT ECO:0000269|PubMed:5249818"
FT ACT_SITE 328
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240,
FT ECO:0000269|PubMed:5249818"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT VARIANT 128
FT /note="Y -> F (in strain: DC-4)"
FT /evidence="ECO:0000269|PubMed:12524032"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:3CNQ"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:1SPB"
FT HELIX 53..61
FT /evidence="ECO:0007829|PDB:3CNQ"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:3CNQ"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:3CNQ"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:3CNQ"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:3CNQ"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:3CNQ"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:3CNQ"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:1TO2"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:1TO2"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:1TO2"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1SUA"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:1TO2"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:2SBT"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:1TO2"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:1TO2"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:1TO2"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:7AM3"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:1TO2"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:1TO2"
FT HELIX 211..223
FT /evidence="ECO:0007829|PDB:1TO2"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:1TO2"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:1TO2"
FT HELIX 240..251
FT /evidence="ECO:0007829|PDB:1TO2"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:1TO2"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:1TO2"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:1TO2"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:2SBT"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:1TO2"
FT STRAND 310..316
FT /evidence="ECO:0007829|PDB:1TO2"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:1TO2"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:1TO2"
FT HELIX 327..344
FT /evidence="ECO:0007829|PDB:1TO2"
FT HELIX 350..358
FT /evidence="ECO:0007829|PDB:1TO2"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:1SPB"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:1TO2"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:1TO2"
SQ SEQUENCE 382 AA; 39181 MW; ED987DAFA37B8335 CRC64;
MRGKKVWISL LFALALIFTM AFGSTSSAQA AGKSNGEKKY IVGFKQTMST MSAAKKKDVI
SEKGGKVQKQ FKYVDAASAT LNEKAVKELK KDPSVAYVEE DHVAHAYAQS VPYGVSQIKA
PALHSQGYTG SNVKVAVIDS GIDSSHPDLK VAGGASMVPS ETNPFQDNNS HGTHVAGTVA
ALNNSIGVLG VAPSASLYAV KVLGADGSGQ YSWIINGIEW AIANNMDVIN MSLGGPSGSA
ALKAAVDKAV ASGVVVVAAA GNEGTSGSSS TVGYPGKYPS VIAVGAVDSS NQRASFSSVG
PELDVMAPGV SIQSTLPGNK YGAYNGTSMA SPHVAGAAAL ILSKHPNWTN TQVRSSLENT
TTKLGDSFYY GKGLINVQAA AQ
