VM3VB_CROAT
ID VM3VB_CROAT Reviewed; 609 AA.
AC Q90282; C9E1R6; Q7LZK3;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like VAP2B;
DE EC=3.4.24.-;
DE AltName: Full=Catrocollastatin;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE AltName: Full=Vascular apoptosis-inducing protein 2B;
DE Short=VAP2B;
DE Contains:
DE RecName: Full=Disintegrin-like catrocollastatin-C;
DE Flags: Precursor;
OS Crotalus atrox (Western diamondback rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8730;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 240-279 AND 507-537,
RP FUNCTION, AND SUBUNIT.
RC TISSUE=Venom, and Venom gland;
RX PubMed=7733877; DOI=10.1042/bj3070411;
RA Zhou Q., Smith J.B., Grossman M.H.;
RT "Molecular cloning and expression of catrocollastatin, a snake-venom
RT protein from Crotalus atrox (western diamondback rattlesnake) which
RT inhibits platelet adhesion to collagen.";
RL Biochem. J. 307:411-417(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=19799929; DOI=10.1016/j.toxicon.2009.09.016;
RA Jia Y., Perez J.C.;
RT "Molecular cloning and characterization of cDNAs encoding
RT metalloproteinases from snake venom glands.";
RL Toxicon 55:462-469(2010).
RN [3]
RP PROTEIN SEQUENCE OF 199-208; 225-237; 257-274; 284-297; 298-312; 437-451;
RP 532-539 AND 596-609, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=19371136; DOI=10.1021/pr900249q;
RA Calvete J.J., Fasoli E., Sanz L., Boschetti E., Righetti P.G.;
RT "Exploring the venom proteome of the western diamondback rattlesnake,
RT Crotalus atrox, via snake venomics and combinatorial peptide ligand library
RT approaches.";
RL J. Proteome Res. 8:3055-3067(2009).
RN [4]
RP PROTEIN SEQUENCE OF 226-236 AND 240-250, AND SUBUNIT.
RC TISSUE=Venom, and Venom gland;
RX PubMed=17497365; DOI=10.1080/10623320701346882;
RA Masuda S., Maeda H., Miao J.Y., Hayashi H., Araki S.;
RT "cDNA cloning and some additional peptide characterization of a single-
RT chain vascular apoptosis-inducing protein, VAP2.";
RL Endothelium 14:89-96(2007).
RN [5]
RP PROTEIN SEQUENCE OF 394-609, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, MASS SPECTROMETRY (CATROCOLLASTATIN-C), AND SYNTHESIS OF
RP CYCLIC PEPTIDE OF 459-472.
RC TISSUE=Venom;
RX PubMed=9210644; DOI=10.1006/abbi.1997.0133;
RA Shimokawa K., Shannon J.D., Jia L.-G., Fox J.W.;
RT "Sequence and biological activity of catrocollastatin-C: a disintegrin-
RT like/cysteine-rich two-domain protein from Crotalus atrox venom.";
RL Arch. Biochem. Biophys. 343:35-43(1997).
RN [6]
RP PROTEIN SEQUENCE OF 394-609, MASS SPECTROMETRY, AND DISULFIDE BONDS
RP (CATROCOLLASTATIN-C).
RX PubMed=10933502; DOI=10.1110/ps.9.7.1365;
RA Calvete J.J., Moreno-Murciano M.P., Sanz L., Jurgens M., Schrader M.,
RA Raida M., Benjamin D.C., Fox J.W.;
RT "The disulfide bond pattern of catrocollastatin C, a disintegrin-
RT like/cysteine-rich protein isolated from Crotalus atrox venom.";
RL Protein Sci. 9:1365-1373(2000).
RN [7]
RP FUNCTION, SUBUNIT, INTERACTION WITH COLLAGEN, AND SYNTHESIS OF CYCLIC
RP PEPTIDE OF 459-472 (CATROCOLLASTATIN).
RX PubMed=8645248; DOI=10.1006/bbrc.1996.0301;
RA Zhou Q., Dangelmaier C., Smith J.B.;
RT "The hemorrhagin catrocollastatin inhibits collagen-induced platelet
RT aggregation by binding to collagen via its disintegrin-like domain.";
RL Biochem. Biophys. Res. Commun. 219:720-726(1996).
RN [8]
RP CRYSTALLIZATION.
RC TISSUE=Venom;
RX PubMed=16820695; DOI=10.1107/s1744309106022548;
RA Igarashi T., Oishi Y., Araki S., Mori H., Takeda S.;
RT "Crystallization and preliminary X-ray crystallographic analysis of two
RT vascular apoptosis-inducing proteins (VAPs) from Crotalus atrox venom.";
RL Acta Crystallogr. F 62:688-691(2006).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 191-609, METAL-BINDING SITES,
RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-371.
RC TISSUE=Venom;
RX PubMed=17485084; DOI=10.1016/j.febslet.2007.04.057;
RA Igarashi T., Araki S., Mori H., Takeda S.;
RT "Crystal structures of catrocollastatin/VAP2B reveal a dynamic, modular
RT architecture of ADAM/adamalysin/reprolysin family proteins.";
RL FEBS Lett. 581:2416-2422(2007).
CC -!- FUNCTION: [Zinc metalloproteinase-disintegrin-like VAP2B]: Zinc
CC metalloprotease that abolishes platelet aggregation induced by
CC collagen, but has no effect on platelet aggregation induced by ADP or
CC thromboxane analog. This inhibition may be due to its ability to bind
CC collagen and block the binding site on collagen for platelets and/or to
CC its ability to bind to the platelet alpha-2/beta-1 collagen receptor
CC (ITGA2/ITGB1) to block its interaction with collagen and hence prevent
CC platelet stimulation.
CC -!- FUNCTION: Disintegrin catrocollastatin-C: abolishes platelet
CC aggregation induced by collagen (IC(50)=66 nM) but not ADP-stimulated
CC platelet aggregation. This inhibition may be due to its ability to bind
CC collagen and block the binding site on collagen for platelets and/or to
CC its ability to bind to the platelet alpha-2/beta-1 collagen receptor
CC (ITGA2/ITGB1) to block its interaction with collagen and hence prevent
CC platelet stimulation.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer (PubMed:17485084) or heterodimer; non-covalently
CC linked (PubMed:17497365). Interacts with fibrillar collagen.
CC {ECO:0000269|PubMed:17485084, ECO:0000269|PubMed:17497365,
CC ECO:0000269|PubMed:7733877, ECO:0000269|PubMed:8645248}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9210644}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:9210644}.
CC -!- PTM: The N-terminus is blocked.
CC -!- MASS SPECTROMETRY: [Disintegrin-like catrocollastatin-C]: Mass=23532;
CC Mass_error=2; Method=Electrospray; Note=Average mass.;
CC Evidence={ECO:0000269|PubMed:10933502};
CC -!- MASS SPECTROMETRY: [Disintegrin-like catrocollastatin-C]: Mass=23572;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:9210644};
CC -!- MISCELLANEOUS: Catrocollastatin-C represents at least 0.5% of the total
CC protein in the venom.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIb sub-subfamily. {ECO:0000305}.
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DR EMBL; U21003; AAC59672.1; -; mRNA.
DR EMBL; GQ451437; ACV83931.1; -; mRNA.
DR PIR; S55264; S55264.
DR PIR; S55270; S55270.
DR PDB; 2DW0; X-ray; 2.15 A; A/B=191-609.
DR PDB; 2DW1; X-ray; 2.50 A; A/B=191-609.
DR PDB; 2DW2; X-ray; 2.70 A; A/B=191-609.
DR PDBsum; 2DW0; -.
DR PDBsum; 2DW1; -.
DR PDBsum; 2DW2; -.
DR AlphaFoldDB; Q90282; -.
DR SMR; Q90282; -.
DR MEROPS; M12.332; -.
DR iPTMnet; Q90282; -.
DR EvolutionaryTrace; Q90282; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion impairing toxin;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Platelet aggregation inhibiting toxin; Protease;
KW Pyrrolidone carboxylic acid; Secreted; Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..189
FT /evidence="ECO:0000250"
FT /id="PRO_0000406909"
FT CHAIN 190..609
FT /note="Zinc metalloproteinase-disintegrin-like VAP2B"
FT /id="PRO_5000144525"
FT CHAIN 394..609
FT /note="Disintegrin-like catrocollastatin-C"
FT /id="PRO_0000406910"
FT DOMAIN 198..393
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 401..487
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT REGION 459..472
FT /note="Inhibits platelet aggregation"
FT MOTIF 465..467
FT /note="D/ECD-tripeptide"
FT ACT_SITE 334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 410
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 416
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 467
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 468
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 470
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 482
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 483
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT MOD_RES 190
FT /note="Pyrrolidone carboxylic acid (Glu)"
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17485084"
FT DISULFID 308..388
FT /note="In zinc metalloproteinase-disintegrin-like VAP2B"
FT DISULFID 348..372
FT /note="In zinc metalloproteinase-disintegrin-like VAP2B"
FT DISULFID 350..355
FT /note="In zinc metalloproteinase-disintegrin-like VAP2B"
FT DISULFID 404..433
FT /note="In zinc metalloproteinase-disintegrin-like VAP2B;
FT alternate"
FT DISULFID 404..423
FT /note="In disintegrin-like catrocollastatin-C; alternate"
FT DISULFID 415..433
FT /note="In disintegrin-like catrocollastatin-C; alternate"
FT DISULFID 415..428
FT /note="In zinc metalloproteinase-disintegrin-like VAP2B;
FT alternate"
FT DISULFID 417..423
FT /note="In zinc metalloproteinase-disintegrin-like VAP2B;
FT alternate"
FT DISULFID 427..450
FT /note="In zinc metalloproteinase-disintegrin-like VAP2B"
FT DISULFID 441..447
FT /note="In zinc metalloproteinase-disintegrin-like VAP2B"
FT DISULFID 446..472
FT /note="In zinc metalloproteinase-disintegrin-like VAP2B"
FT DISULFID 459..479
FT /note="In both disintegrin-like catrocollastatin-C and zinc
FT metalloproteinase-disintegrin-like VAP2B"
FT DISULFID 466..498
FT /note="In zinc metalloproteinase-disintegrin-like VAP2B;
FT alternate"
FT DISULFID 466..491
FT /note="In disintegrin-like catrocollastatin-C; alternate"
FT DISULFID 491..503
FT /note="In zinc metalloproteinase-disintegrin-like VAP2B;
FT alternate"
FT DISULFID 498..503
FT /note="In disintegrin-like catrocollastatin-C"
FT DISULFID 510..560
FT /note="In zinc metalloproteinase-disintegrin-like VAP2B;
FT alternate"
FT DISULFID 510..525
FT /note="In disintegrin-like catrocollastatin-C; alternate"
FT DISULFID 525..571
FT /note="In zinc metalloproteinase-disintegrin-like VAP2B;
FT alternate"
FT DISULFID 538..548
FT /note="In zinc metalloproteinase-disintegrin-like VAP2B;
FT alternate"
FT DISULFID 548..555
FT /note="In disintegrin-like catrocollastatin-C; alternate"
FT DISULFID 555..597
FT /note="In zinc metalloproteinase-disintegrin-like VAP2B;
FT alternate"
FT DISULFID 560..571
FT /note="In disintegrin-like catrocollastatin-C"
FT DISULFID 591..602
FT /note="In zinc metalloproteinase-disintegrin-like VAP2B;
FT alternate"
FT DISULFID 597..602
FT /note="In disintegrin-like catrocollastatin-C"
FT CONFLICT 33..34
FT /note="VI -> IV (in Ref. 2; ACV83931)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="G -> E (in Ref. 2; ACV83931)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="G -> Q (in Ref. 2; ACV83931)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="P -> S (in Ref. 2; ACV83931)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="F -> V (in Ref. 2; ACV83931)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="D -> N (in Ref. 2; ACV83931)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="M -> V (in Ref. 2; ACV83931)"
FT /evidence="ECO:0000305"
FT CONFLICT 507..508
FT /note="YH -> VL (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="A -> G (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="Y -> V (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="S -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="C -> G (in Ref. 2; ACV83931)"
FT /evidence="ECO:0000305"
FT STRAND 198..206
FT /evidence="ECO:0007829|PDB:2DW0"
FT HELIX 208..213
FT /evidence="ECO:0007829|PDB:2DW0"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:2DW0"
FT HELIX 218..237
FT /evidence="ECO:0007829|PDB:2DW0"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:2DW0"
FT STRAND 241..250
FT /evidence="ECO:0007829|PDB:2DW0"
FT HELIX 263..276
FT /evidence="ECO:0007829|PDB:2DW0"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:2DW0"
FT STRAND 285..293
FT /evidence="ECO:0007829|PDB:2DW0"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:2DW0"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:2DW0"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:2DW0"
FT HELIX 324..338
FT /evidence="ECO:0007829|PDB:2DW0"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:2DW0"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:2DW0"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:2DW1"
FT HELIX 371..384
FT /evidence="ECO:0007829|PDB:2DW0"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:2DW0"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:2DW0"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:2DW0"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:2DW0"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:2DW0"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:2DW0"
FT STRAND 447..452
FT /evidence="ECO:0007829|PDB:2DW1"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:2DW0"
FT TURN 492..495
FT /evidence="ECO:0007829|PDB:2DW0"
FT HELIX 506..514
FT /evidence="ECO:0007829|PDB:2DW0"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:2DW0"
FT HELIX 523..526
FT /evidence="ECO:0007829|PDB:2DW0"
FT HELIX 527..530
FT /evidence="ECO:0007829|PDB:2DW0"
FT STRAND 533..535
FT /evidence="ECO:0007829|PDB:2DW0"
FT STRAND 538..541
FT /evidence="ECO:0007829|PDB:2DW0"
FT STRAND 544..546
FT /evidence="ECO:0007829|PDB:2DW0"
FT HELIX 550..555
FT /evidence="ECO:0007829|PDB:2DW0"
FT STRAND 560..562
FT /evidence="ECO:0007829|PDB:2DW0"
FT STRAND 569..572
FT /evidence="ECO:0007829|PDB:2DW0"
FT TURN 580..583
FT /evidence="ECO:0007829|PDB:2DW0"
FT STRAND 590..592
FT /evidence="ECO:0007829|PDB:2DW0"
FT STRAND 595..598
FT /evidence="ECO:0007829|PDB:2DW0"
FT STRAND 601..604
FT /evidence="ECO:0007829|PDB:2DW0"
FT HELIX 605..607
FT /evidence="ECO:0007829|PDB:2DW0"
SQ SEQUENCE 609 AA; 68248 MW; D58876161F64FAA5 CRC64;
MIQVLLVTIC LAAFPYQGSS IILESGNVND YEVIYPRKVT ALPKGAVQPK YEDAMQYELK
VNGEPVVLHL GKNKGLFSKD YSETHYSPDG REITTYPLVE DHCYYHGRIE NDADSTASIS
ACNGLKGHFK LQGEMYLIEP LKLPDSEAHA VYKYENVEKE DEALKMCGVT QNWESYEPIK
KASQLVVTAE HQKYNPFRFV ELFLVVDKAM VTKNNGDLDK IKTRMYEIVN TVNEIYRYMY
IHVALVGLEI WSNEDKITVK PEAGYTLNAF GEWRKTDLLT RKKHDNAQLL TAIDLDRVIG
LAYVGSMCHP KRSTGIIQDY SEINLVVAVI MAHEMGHNLG INHDSGYCSC GDYACIMRPE
ISPEPSTFFS NCSYFECWDF IMNHNPECIL NEPLGTDIIS PPVCGNELLE VGEECDCGTP
ENCQNECCDA ATCKLKSGSQ CGHGDCCEQC KFSKSGTECR ASMSECDPAE HCTGQSSECP
ADVFHKNGQP CLDNYGYCYN GNCPIMYHQC YDLFGADVYE AEDSCFERNQ KGNYYGYCRK
ENGNKIPCAP EDVKCGRLYC KDNSPGQNNP CKMFYSNEDE HKGMVLPGTK CADGKVCSNG
HCVDVATAY
