ID   VWF_CANLF               Reviewed;        2813 AA.
AC   Q28295; Q28311; Q9TSI4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=von Willebrand factor;
DE            Short=vWF;
DE   Flags: Precursor;
GN   Name=VWF; Synonyms=F8VWF;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Stoy S.J., Shibuya H., Nonneman D.J., Holzhauer J., Mohammed I.H.,
RA   Johnson G.S.;
RT   "Canine vWF cDNA sequence.";
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND SUBCELLULAR LOCATION.
RC   TISSUE=Heart;
RX   PubMed=10961880;
RA   Haberichter S.L., Fahs S.A., Montgomery R.R.;
RT   "von Willebrand factor storage and multimerization: 2 independent
RT   intracellular processes.";
RL   Blood 96:1808-1815(2000).
RN   [3]
RP   SEQUENCE REVISION TO 55.
RA   Montgomery R.R., Fahs S., Montgomery M.W.;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DISEASE.
RC   STRAIN=Scottish terrier; TISSUE=Uterus;
RX   PubMed=10668811; DOI=10.1892/0891-6640(2000)014<0010:mcvwdi>2.3.co;2;
RA   Venta P.J., Li J., Yuzbasiyan-Gurkan V., Brewer G.J., Schall W.D.;
RT   "Mutation causing von Willebrand's disease in Scottish Terriers.";
RL   J. Vet. Intern. Med. 14:10-19(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1234-1669.
RC   TISSUE=Blood;
RA   Mancuso D.J., Christopherson P.A., Kroner P.A., Montgomery R.R.;
RT   "The canine von Willebrand factor gene: sequence and expression of a region
RT   encoding the glycoprotein Ib/IX binding domain.";
RL   Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   REVIEW.
RX   PubMed=12871266; DOI=10.1046/j.1538-7836.2003.00260.x;
RA   Ruggeri Z.M.;
RT   "von Willebrand factor, platelets and endothelial cell interactions.";
RL   J. Thromb. Haemost. 1:1335-1342(2003).
CC   -!- FUNCTION: Important in the maintenance of hemostasis, it promotes
CC       adhesion of platelets to the sites of vascular injury by forming a
CC       molecular bridge between sub-endothelial collagen matrix and platelet-
CC       surface receptor complex, glycoprotein Ibalpha/IX/V. Also acts as a
CC       chaperone for coagulation factor VIII, delivering it to the site of
CC       injury, stabilizing its heterodimeric structure and protecting it from
CC       premature clearance from plasma (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Multimeric. Interacts with F8. {ECO:0000269|PubMed:10961880}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10961880}. Secreted,
CC       extracellular space, extracellular matrix
CC       {ECO:0000269|PubMed:10961880}. Note=Localized to storage granules.
CC   -!- TISSUE SPECIFICITY: Plasma.
CC   -!- DOMAIN: The propeptide is required for multimerization of vWF and for
CC       its targeting to storage granules.
CC   -!- PTM: All cysteine residues are involved in intrachain or interchain
CC       disulfide bonds. {ECO:0000250}.
CC   -!- PTM: N- and O-glycosylated. {ECO:0000250}.
CC   -!- DISEASE: Note=Defects in VWF are the cause of von Willebrand disease
CC       (VWD) in the Scottish Terrier. VWD is characterized by frequent
CC       bleeding. Type I VWD is associated with a deficiency of VWF; type II by
CC       normal to decreased plasma level of VWF; type III by a virtual absence
CC       of VWF. {ECO:0000269|PubMed:10668811}.
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; L76227; AAB05549.1; -; mRNA.
DR   EMBL; U66246; AAB93766.2; -; mRNA.
DR   EMBL; AF099154; AAD04919.1; -; mRNA.
DR   EMBL; L16903; AAA30903.1; -; Genomic_DNA.
DR   RefSeq; NP_001002932.1; NM_001002932.1.
DR   SMR; Q28295; -.
DR   STRING; 9615.ENSCAFP00000053390; -.
DR   MEROPS; I08.950; -.
DR   MEROPS; I08.954; -.
DR   GlyCosmos; Q28295; 15 sites, No reported glycans.
DR   PaxDb; 9612-ENSCAFP00000022453; -.
DR   Ensembl; ENSCAFT00000083915.2; ENSCAFP00000065165.2; ENSCAFG00000015228.5.
DR   GeneID; 399544; -.
DR   KEGG; cfa:399544; -.
DR   CTD; 7450; -.
DR   VGNC; VGNC:48329; VWF.
DR   eggNOG; KOG1216; Eukaryota.
DR   InParanoid; Q28295; -.
DR   OrthoDB; 2872912at2759; -.
DR   Proteomes; UP000002254; Chromosome 27.
DR   Proteomes; UP000694429; Unplaced.
DR   Proteomes; UP000694542; Unplaced.
DR   Proteomes; UP000805418; Unplaced.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0033093; C:Weibel-Palade body; ISS:UniProtKB.
DR   GO; GO:0005518; F:collagen binding; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0019865; F:immunoglobulin binding; ISS:UniProtKB.
DR   GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR   GO; GO:0002020; F:protease binding; ISS:UniProtKB.
DR   GO; GO:0051087; F:protein-folding chaperone binding; ISS:UniProtKB.
DR   GO; GO:0007596; P:blood coagulation; ISS:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR   GO; GO:0031589; P:cell-substrate adhesion; ISS:UniProtKB.
DR   GO; GO:0007599; P:hemostasis; ISS:UniProtKB.
DR   GO; GO:0030168; P:platelet activation; ISS:UniProtKB.
DR   CDD; cd19941; TIL; 5.
DR   CDD; cd01450; vWFA_subfamily_ECM; 3.
DR   Gene3D; 2.10.25.10; Laminin; 5.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 3.
DR   InterPro; IPR006207; Cys_knot_C.
DR   InterPro; IPR036084; Ser_inhib-like_sf.
DR   InterPro; IPR002919; TIL_dom.
DR   InterPro; IPR037578; Von_Willebrand_factor.
DR   InterPro; IPR032361; VWA_N2.
DR   InterPro; IPR014853; VWF/SSPO/ZAN-like_Cys-rich_dom.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR001007; VWF_dom.
DR   InterPro; IPR001846; VWF_type-D.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR11339; EXTRACELLULAR MATRIX GLYCOPROTEIN RELATED; 1.
DR   PANTHER; PTHR11339:SF361; VON WILLEBRAND FACTOR; 1.
DR   Pfam; PF08742; C8; 4.
DR   Pfam; PF01826; TIL; 4.
DR   Pfam; PF00092; VWA; 3.
DR   Pfam; PF16164; VWA_N2; 1.
DR   Pfam; PF00093; VWC; 2.
DR   Pfam; PF00094; VWD; 4.
DR   PIRSF; PIRSF002495; VWF; 1.
DR   PRINTS; PR00453; VWFADOMAIN.
DR   SMART; SM00832; C8; 4.
DR   SMART; SM00041; CT; 1.
DR   SMART; SM00327; VWA; 3.
DR   SMART; SM00214; VWC; 5.
DR   SMART; SM00215; VWC_out; 2.
DR   SMART; SM00216; VWD; 4.
DR   SUPFAM; SSF57603; FnI-like domain; 1.
DR   SUPFAM; SSF57567; Serine protease inhibitors; 5.
DR   SUPFAM; SSF53300; vWA-like; 3.
DR   PROSITE; PS01185; CTCK_1; 1.
DR   PROSITE; PS01225; CTCK_2; 1.
DR   PROSITE; PS50234; VWFA; 3.
DR   PROSITE; PS01208; VWFC_1; 3.
DR   PROSITE; PS50184; VWFC_2; 3.
DR   PROSITE; PS51233; VWFD; 4.
PE   1: Evidence at protein level;
KW   Blood coagulation; Cell adhesion; Cleavage on pair of basic residues;
KW   Disulfide bond; Extracellular matrix; Glycoprotein; Hemostasis;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   PROPEP          23..763
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000022680"
FT   CHAIN           764..2813
FT                   /note="von Willebrand factor"
FT                   /id="PRO_0000022681"
FT   DOMAIN          33..201
FT                   /note="VWFD 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DOMAIN          295..348
FT                   /note="TIL 1"
FT   DOMAIN          386..560
FT                   /note="VWFD 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DOMAIN          652..707
FT                   /note="TIL 2"
FT   DOMAIN          776..827
FT                   /note="TIL 3"
FT   DOMAIN          865..1032
FT                   /note="VWFD 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DOMAIN          1146..1196
FT                   /note="TIL 4"
FT   DOMAIN          1277..1453
FT                   /note="VWFA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   DOMAIN          1498..1665
FT                   /note="VWFA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   DOMAIN          1691..1871
FT                   /note="VWFA 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   DOMAIN          1948..2124
FT                   /note="VWFD 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DOMAIN          2255..2328
FT                   /note="VWFC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          2429..2495
FT                   /note="VWFC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          2580..2645
FT                   /note="VWFC 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          2724..2812
FT                   /note="CTCK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   REGION          764..787
FT                   /note="Amino-terminal"
FT   REGION          788..833
FT                   /note="E1"
FT   REGION          826..853
FT                   /note="CX"
FT   REGION          2216..2261
FT                   /note="E2"
FT   MOTIF           531..533
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOTIF           698..700
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOTIF           2507..2509
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        211
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        666
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        857
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1515
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1574
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2223
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2290
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2357
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2400
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2546
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2585
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2790
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        35..162
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        57..200
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        388..524
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        410..559
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        432..440
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        767..808
FT                   /evidence="ECO:0000250"
FT   DISULFID        776..804
FT                   /evidence="ECO:0000250"
FT   DISULFID        810..821
FT                   /evidence="ECO:0000250"
FT   DISULFID        867..996
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        889..1031
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        898..993
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        914..921
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        1060..1084
FT                   /evidence="ECO:0000250"
FT   DISULFID        1071..1111
FT                   /evidence="ECO:0000250"
FT   DISULFID        1089..1091
FT                   /evidence="ECO:0000250"
FT   DISULFID        1126..1130
FT                   /evidence="ECO:0000250"
FT   DISULFID        1149..1169
FT                   /evidence="ECO:0000250"
FT   DISULFID        1153..1165
FT                   /evidence="ECO:0000250"
FT   DISULFID        1196..1199
FT                   /evidence="ECO:0000250"
FT   DISULFID        1234..1237
FT                   /evidence="ECO:0000250"
FT   DISULFID        1272..1458
FT                   /evidence="ECO:0000250"
FT   DISULFID        1669..1670
FT                   /evidence="ECO:0000250"
FT   DISULFID        1686..1872
FT                   /evidence="ECO:0000250"
FT   DISULFID        1879..1904
FT                   /evidence="ECO:0000250"
FT   DISULFID        1899..1940
FT                   /note="Or C-1899 with C-1942"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039,
FT                   ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        1927..2088
FT                   /evidence="ECO:0000250"
FT   DISULFID        1950..2085
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        1972..2123
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        1993..2001
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        2724..2774
FT                   /evidence="ECO:0000250"
FT   DISULFID        2739..2788
FT                   /evidence="ECO:0000250"
FT   DISULFID        2750..2804
FT                   /evidence="ECO:0000250"
FT   DISULFID        2754..2806
FT                   /evidence="ECO:0000250"
FT   DISULFID        ?..2811
FT                   /evidence="ECO:0000250"
FT   CONFLICT        70
FT                   /note="V -> I (in Ref. 4; AAD04919)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        266
FT                   /note="A -> G (in Ref. 2; AAB93766)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        280
FT                   /note="I -> V (in Ref. 2; AAB93766)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        409..411
FT                   /note="VCH -> ICQ (in Ref. 2; AAB93766)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        994
FT                   /note="G -> A (in Ref. 1; AAB05549)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1021
FT                   /note="F -> L (in Ref. 2; AAB93766)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2381
FT                   /note="L -> P (in Ref. 2; AAB93766)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2406
FT                   /note="P -> L (in Ref. 2; AAB93766)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2813 AA;  309719 MW;  5DF93E1E5E72F80C CRC64;
     MSPTRLVRVL LALALILPGK LCTKGTVGRS SMARCSLFGG DFINTFDESM YSFAGDCSYL
     LAGDCQEHSV SLIGGFQNGK RVSLSVYLGE FFDIHLFVNG TMLQGTQSIS MPYASNGLYL
     EAEAGYYKLS SEAYGFVARI DGNGNFQVLL SDRYFNKTCG LCGNFNIFAE DDFRTQEGTL
     TSDPYDFANS WALSSGEQRC KRVSPPSSPC NVSSDEVQQV LWEQCQLLKS ASVFARCHPL
     VDPEPFVALC ERTLCTCVQG MECPCAVLLE YARACAQQGI VLYGWTDHSV CRPACPAGME
     YKECVSPCTR TCQSLHVKEV CQEQCVDGCS CPEGQLLDEG HCVGSAECSC VHAGQRYPPG
     ASLLQDCHTC ICRNSLWICS NEECPGECLV TGQSHFKSFD NRYFTFSGVC HYLLAQDCQD
     HTFSVVIETV QCADDLDAVC TRSVTVRLPG HHNSLVKLKH GGGVSMDGQD IQIPLLQGDL
     RIQHTVMASV RLSYGEDLQM DWDGRGRLLV TLSPAYAGKT CGLCGNYNGN RGDDFVTPAG
     LAEPLVEDFG NAWKLLGACE NLQKQHRDPC SLNPRQARFA EEACALLTSS KFEPCHRAVG
     PQPYVQNCRY DVCSCSDGRD CLCSAVANYA AACARRGVHI AWREPGFCAL SCPQGQVYLQ
     CGTPCNMTCR SLSYPEEDCN EVCLEGCFCP PGLYLDERGD CVPKAQCPCY YDGEIFQPED
     IFSDHHTMCY CEDGFMHCTT SGGLGSLLPN PVLSSPRSHR SKRSLSCRPP MVKLVCPADN
     PRAEGLECAK TCQNYDLQCM STGCVSGCLC PQGMVRHENR CVALERCPCF HQGQEYAPGE
     TVKIDCNTCV CRDRKWNCTD HVCDATCSAI GMAHYLTFDG LKYLFPGECQ YVLVQDYCGS
     NPGTFRILVG NEGCSYPSVK CKKRVTILVE GGEIELFDGE VNVKKPMKDE THFEVVESGQ
     YVILLLGKAL SVVWDHRLSI SVTLKRTYQE QVCGLCGNFD GIQNNDFTSS SLQIEEDPVD
     FGNSWKVNPQ CADTKKVPLD SSPAVCHNNI MKQTMVDSSC RILTSDIFQD CNRLVDPEPF
     LDICIYDTCS CESIGDCTCF CDTIAAYAHV CAQHGKVVAW RTATFCPQNC EERNLHENGY
     ECEWRYNSCA PACPITCQHP EPLACPVQCV EGCHAHCPPG KILDELLQTC IDPEDCPVCE
     VAGRRLAPGK KIILNPSDPE HCQICHCDGV NFTCQACREP GSLVVPPTEG PIGSTTSYVE
     DTPEPPLHDF HCSRLLDLVF LLDGSSKLSE DEFEVLKVFV VGMMEHLHIS QKRIRVAVVE
     YHDGSHAYIE LKDRKRPSEL RRITSQVKYA GSEVASTSEV LKYTLFQIFG KIDRPEASRI
     ALLLMASQEP SRLARNLVRY VQGLKKKKVI VIPVGIGPHA SLKQIHLIEK QAPENKAFVF
     SGVDELEQRR DEIINYLCDL APEAPAPTQH PPMAQVTVGS ELLGVSSPGP KRNSMVLDVV
     FVLEGSDKIG EANFNKSREF MEEVIQRMDV GQDRIHVTVL QYSYMVTVEY TFSEAQSKGE
     VLQQVRDIRY RGGNRTNTGL ALQYLSEHSF SVSQGDREQV PNLVYMVTGN PASDEIKRMP
     GDIQVVPIGV GPHANVQELE KIGWPNAPIL IHDFEMLPRE APDLVLQRCC SGEGLQIPTL
     SPTPDCSQPL DVVLLLDGSS SIPASYFDEM KSFTKAFISR ANIGPRLTQV SVLQYGSITT
     IDVPWNVAYE KVHLLSLVDL MQQEGGPSQI GDALSFAVRY VTSEVHGARP GASKAVVILV
     TDVSVDSVDA AAEAARSNRV TVFPIGIGDR YSEAQLSSLA GPKAGSNMVR LQRIEDLPTV
     ATLGNSFFHK LCSGFDRVCV DEDGNEKRPG DVWTLPDQCH TVTCLPDGQT LLKSHRVNCD
     RGPRPSCPNG QPPLRVEETC GCRWTCPCVC MGSSTRHIVT FDGQNFKLTG SCSYVLFQNK
     EQDLEVILHN GACSPGAKET CMKSIEVKHD GLSVELHSDM QMTVNGRLVS IPYVGGDMEV
     NVYGTIMYEV RFNHLGHIFT FTPQNNEFQL QLSPRTFASK TYGLCGICDE NGANDFILRD
     GTVTTDWKAL IQEWTVQQLG KTCQPVPEEQ CPVSSSSHCQ VLLSELFAEC HKVLAPATFY
     AMCQPDSCHP KKVCEAIALY AHLCRTKGVC VDWRRANFCA MSCPPSLVYN HCEHGCPRLC
     EGNTSSCGDQ PSEGCFCPPN QVMLEGSCVP EEACTQCISE DGVRHQFLET WVPAHQPCQI
     CTCLSGRKVN CTLQPCPTAR APTCGPCEVA RLRQNAEQCC PEYECVCDLV SCDLPPVPPC
     EDGLQMTLTN PGECRPNFTC ACRKDECRRE SPPSCPPHRT LALRKTQCCD EYECACNCVN
     STVSCPLGYL ASAVTNDCGC TTTTCFPDKV CVHRGTIYPV GQFWEEACDV CTCTDLEDSV
     MGLRVAQCSQ KPCEDNCLSG FTYVLHEGEC CGRCLPSACE VVIGSPRGDA QSHWKNVGSH
     WASPDNPCLI NECVRVKEEV FVQQRNVSCP QLNVPTCPTG FQLSCKTSEC CPTCHCEPLE
     ACLLNGTIIG PGKSLMIDVC TTCRCTVQVG VISGFKLECR KTTCEACPLG YKEEKNQGEC
     CGRCLPIACT IQLRGGQIMT LKRDETIQDG CDSHFCKVNE RGEYIWEKRV TGCPPFDEHK
     CLAEGGKIMK IPGTCCDTCE EPECKDIIAK LQRVKVGDCK SEEEVDIHYC EGKCASKAVY
     SIHMEDVQDQ CSCCSPTQTE PMQVPLRCTN GSLIYHEILN AMQCRCSPRK CSK
//