ID   ATS13_MOUSE             Reviewed;        1426 AA.
AC   Q769J6; A2ALB4; Q76LW1;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 144.
DE   RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 13;
DE            Short=ADAM-TS 13;
DE            Short=ADAM-TS13;
DE            Short=ADAMTS-13;
DE            EC=3.4.24.87 {ECO:0000269|PubMed:15869605};
DE   AltName: Full=von Willebrand factor-cleaving protease;
DE            Short=vWF-CP;
DE            Short=vWF-cleaving protease;
DE   Flags: Precursor;
GN   Name=Adamts13; Synonyms=Gm710;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP   POLYMORPHISM.
RC   STRAIN=129, and 129/Sv; TISSUE=Liver;
RX   PubMed=15136581; DOI=10.1074/jbc.m314184200;
RA   Banno F., Kaminaka K., Soejima K., Kokame K., Miyata T.;
RT   "Identification of strain-specific variants of mouse Adamts13 gene encoding
RT   von Willebrand factor-cleaving protease.";
RL   J. Biol. Chem. 279:30896-30903(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15869605; DOI=10.1111/j.1538-7836.2005.01246.x;
RA   Bruno K., Voelkel D., Plaimauer B., Antoine G., Pable S., Motto D.G.,
RA   Lemmerhirt H.L., Dorner F., Zimmermann K., Scheiflinger F.;
RT   "Cloning, expression and functional characterization of the full-length
RT   murine ADAMTS13.";
RL   J. Thromb. Haemost. 3:1064-1073(2005).
CC   -!- FUNCTION: Cleaves the vWF multimers in plasma into smaller forms
CC       thereby controlling vWF-mediated platelet thrombus formation.
CC       {ECO:0000269|PubMed:15869605}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=The enzyme cleaves the von Willebrand factor at bond 842-
CC         Tyr-|-Met-843 within the A2 domain.; EC=3.4.24.87;
CC         Evidence={ECO:0000269|PubMed:15869605};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNA0};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9UNA0};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:Q76LX8};
CC       Note=Binds 4 Ca(2+) ions. {ECO:0000250|UniProtKB:Q76LX8};
CC   -!- ACTIVITY REGULATION: Zinc and calcium ions cooperatively modulate
CC       enzyme activity. The cleavage of the pro-domain is not required for
CC       protease activity. Dependence on calcium for proteolytic activity is
CC       mediated by the high affinity site (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15136581}.
CC       Note=Secretion enhanced by O-fucosylation of TSP type-1 repeats.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Plasma. Expression is consistently high in liver,
CC       medium in lung and spleen, low in skeletal muscle and undetectable in
CC       heart, brain, kidney and testis. {ECO:0000269|PubMed:15136581,
CC       ECO:0000269|PubMed:15869605}.
CC   -!- DEVELOPMENTAL STAGE: Increases steadly with the age of embryo, reaching
CC       highest levels in embryonic tissues of 19 days of gestation.
CC       {ECO:0000269|PubMed:15869605}.
CC   -!- DOMAIN: The pro-domain is not required for folding or secretion and
CC       does not perform the common function of maintening enzyme latency.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The globular cysteineless spacer domain adopts a jelly-roll
CC       topology, and is necessary to recognize and cleave vWF. The C-terminal
CC       TSP type-1 and CUB domains may modulate this interaction (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: The precursor is processed by a furin endopeptidase which cleaves
CC       off the pro-domain. {ECO:0000250}.
CC   -!- PTM: O-glycosylated (By similarity). O-fucosylated by POFUT2 on a
CC       serine or a threonine residue found within the consensus sequence C1-
CC       X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are
CC       the first and second cysteine residue of the repeat, respectively.
CC       Fucosylated repeats can then be further glycosylated by the addition of
CC       a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL.
CC       Fucosylation mediates the efficient secretion of ADAMTS13. May also be
CC       C-glycosylated on tryptophan residues within the consensus sequence W-
CC       X-X-W of the TPRs, and also N-glycosylated. These other glycosylations
CC       can also facilitate secretion (By similarity). {ECO:0000250}.
CC   -!- POLYMORPHISM: Two variants (Adamts13L and Adamts13S) were isolated that
CC       differed in the insertion of an intracisternal A particle (IAP)
CC       retrotransposon including a premature stop at the position 1036. In
CC       Adamts13S the C-terminal two TSP type-1 and two CUB domains are
CC       replaced with a 16-amino acid sequence derived from the IAP, this
CC       variant exhibited vWF cleaving activities in vitro. The IAP insertion
CC       is strain-specific and is found in BALB/c, C3H/He, C57BL/6 and DBA/2
CC       strains, but not in the 129/Sv strain.
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DR   EMBL; AB071302; BAC55159.2; -; mRNA.
DR   EMBL; AB095445; BAD04062.1; -; Genomic_DNA.
DR   EMBL; AB112362; BAD18090.1; -; mRNA.
DR   EMBL; AL773563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL845266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS15820.1; -.
DR   RefSeq; NP_001001322.1; NM_001001322.2.
DR   RefSeq; NP_001277392.1; NM_001290463.1.
DR   AlphaFoldDB; Q769J6; -.
DR   SMR; Q769J6; -.
DR   STRING; 10090.ENSMUSP00000099955; -.
DR   MEROPS; M12.241; -.
DR   GlyCosmos; Q769J6; 14 sites, No reported glycans.
DR   GlyGen; Q769J6; 14 sites.
DR   iPTMnet; Q769J6; -.
DR   PhosphoSitePlus; Q769J6; -.
DR   MaxQB; Q769J6; -.
DR   PaxDb; 10090-ENSMUSP00000099955; -.
DR   Antibodypedia; 31871; 606 antibodies from 36 providers.
DR   DNASU; 279028; -.
DR   Ensembl; ENSMUST00000102891.4; ENSMUSP00000099955.4; ENSMUSG00000014852.17.
DR   GeneID; 279028; -.
DR   KEGG; mmu:279028; -.
DR   UCSC; uc008iwp.1; mouse.
DR   AGR; MGI:2685556; -.
DR   CTD; 11093; -.
DR   MGI; MGI:2685556; Adamts13.
DR   VEuPathDB; HostDB:ENSMUSG00000014852; -.
DR   eggNOG; KOG3538; Eukaryota.
DR   GeneTree; ENSGT00940000158379; -.
DR   InParanoid; Q769J6; -.
DR   OMA; ILPDTQC; -.
DR   OrthoDB; 2910701at2759; -.
DR   PhylomeDB; Q769J6; -.
DR   TreeFam; TF313537; -.
DR   BRENDA; 3.4.24.87; 3474.
DR   Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR   BioGRID-ORCS; 279028; 1 hit in 78 CRISPR screens.
DR   ChiTaRS; Adamts13; mouse.
DR   PRO; PR:Q769J6; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q769J6; Protein.
DR   Bgee; ENSMUSG00000014852; Expressed in liver and 20 other cell types or tissues.
DR   ExpressionAtlas; Q769J6; baseline and differential.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0004175; F:endopeptidase activity; IMP:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR   GO; GO:0071346; P:cellular response to type II interferon; IEA:Ensembl.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0043171; P:peptide catabolic process; ISO:MGI.
DR   GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR   GO; GO:0006508; P:proteolysis; ISO:MGI.
DR   GO; GO:0014075; P:response to amine; IEA:Ensembl.
DR   GO; GO:0035864; P:response to potassium ion; IEA:Ensembl.
DR   GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR   CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR   Gene3D; 2.60.120.830; -; 1.
DR   Gene3D; 3.40.1620.60; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 3.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR   InterPro; IPR041645; ADAMTS_CR_2.
DR   InterPro; IPR045371; ADAMTS_CR_3.
DR   InterPro; IPR010294; ADAMTS_spacer1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   PANTHER; PTHR13723:SF20; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 13; 1.
DR   PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR   Pfam; PF17771; ADAMTS_CR_2; 1.
DR   Pfam; PF19236; ADAMTS_CR_3; 1.
DR   Pfam; PF05986; ADAMTS_spacer1; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   Pfam; PF19030; TSP1_ADAMTS; 4.
DR   Pfam; PF00090; TSP_1; 1.
DR   PRINTS; PR01857; ADAMTSFAMILY.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00209; TSP1; 6.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 4.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50092; TSP1; 4.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Disulfide bond; Glycoprotein; Hemostasis; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Repeat; Secreted; Signal;
KW   Zinc; Zymogen.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   PROPEP          34..76
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000247512"
FT   CHAIN           77..1426
FT                   /note="A disintegrin and metalloproteinase with
FT                   thrombospondin motifs 13"
FT                   /id="PRO_0000247513"
FT   DOMAIN          74..291
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          295..388
FT                   /note="Disintegrin"
FT   DOMAIN          389..444
FT                   /note="TSP type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          687..746
FT                   /note="TSP type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          747..810
FT                   /note="TSP type-1 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          808..871
FT                   /note="TSP type-1 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          904..957
FT                   /note="TSP type-1 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          958..1019
FT                   /note="TSP type-1 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1020..1078
FT                   /note="TSP type-1 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1079..1137
FT                   /note="TSP type-1 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          1195..1302
FT                   /note="CUB 1"
FT   DOMAIN          1293..1426
FT                   /note="CUB 2"
FT   REGION          445..561
FT                   /note="Cysteine-rich"
FT   REGION          556..685
FT                   /note="Spacer"
FT   MOTIF           503..505
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        227
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         85
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000250|UniProtKB:Q76LX8"
FT   BINDING         186
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000250|UniProtKB:Q76LX8"
FT   BINDING         189
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000250|UniProtKB:Q76LX8"
FT   BINDING         214
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000250|UniProtKB:Q76LX8"
FT   BINDING         226
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UNA0"
FT   BINDING         230
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UNA0"
FT   BINDING         236
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UNA0"
FT   BINDING         281
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         289
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        144
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        148
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        557
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        564
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        584
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        619
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        703
FT                   /note="O-linked (Fuc...) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        762
FT                   /note="O-linked (Fuc...) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        834
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        914
FT                   /note="O-linked (Fuc...) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        973
FT                   /note="O-linked (Fuc...) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        1033
FT                   /note="O-linked (Fuc...) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        1057
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1093
FT                   /note="O-linked (Fuc...) serine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        157..210
FT                   /evidence="ECO:0000250"
FT   DISULFID        204..286
FT                   /evidence="ECO:0000250"
FT   DISULFID        246..270
FT                   /evidence="ECO:0000250"
FT   DISULFID        316..342
FT                   /evidence="ECO:0000250"
FT   DISULFID        327..352
FT                   /evidence="ECO:0000250"
FT   DISULFID        337..371
FT                   /evidence="ECO:0000250"
FT   DISULFID        365..376
FT                   /evidence="ECO:0000250"
FT   DISULFID        401..438
FT                   /evidence="ECO:0000250"
FT   DISULFID        405..443
FT                   /evidence="ECO:0000250"
FT   DISULFID        416..428
FT                   /evidence="ECO:0000250"
FT   DISULFID        488..527
FT                   /evidence="ECO:0000250"
FT   DISULFID        513..532
FT                   /evidence="ECO:0000250"
FT   DISULFID        537..553
FT                   /evidence="ECO:0000250"
FT   DISULFID        550..560
FT                   /evidence="ECO:0000250"
FT   VARIANT         1022..1037
FT                   /note="WKVLSLGPCSASCGLG -> ALVWEAAPTFAVTRWR (in Adamts13S)"
FT   VARIANT         1038..1426
FT                   /note="Missing (in Adamts13S)"
FT   CONFLICT        354
FT                   /note="R -> H (in Ref. 1; BAC55159)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1426 AA;  155357 MW;  62E9F672B91F6772 CRC64;
     MSQLCLWLTC QPCYAVSVRG ILTGAIFILG CWGLSDFQKS LLQDLEPKDV SSYFGHHAAP
     FTGHPPSHLQ RLRRRRTLED ILHLELLVAV GPDVSRAHQE DTERYVLTNL NIGSELLRNP
     SLGVQFQVHL VKLITLSDSE STPNITANIT SSLMSVCEWS QTINPHDDRD PSHADLILYI
     TRFDLELPDG NQQVRGVTQL GGACSLSWSC LITEDTGFDL GVTIAHEIGH SFGLDHDGAP
     GSGSTCKASG HVMAADGATP TGGTLEWSAC SQRQLQHLLS TGQMHCFQDP PGLQSGLTRH
     QLMAQPGLYY SADDQCRVAF GSGAVACTFS REGLDVCQAL SCHTDPLDQS SCSRLLVPLL
     DGTECGVEKW CSKARCRSLA ELAPVAAVHG HWSSWGPHSP CSRSCGGGVI TRRRWCNNPR
     PAFGGRACVG EDLQAKMCNT QACEKTQLEF MSEQCAQTDR QPLQLSQGTA SFYHWDAAVQ
     YSQGDTLCRH MCWAVGESFI VSRGDRFLDG TRCVPSGPQD DGTLSLCLLG SCRTFGCDGR
     MDSQKVWDAC QVCGGDNSTC SSRNGSFTAG RAREYVTFLI VTPNMTNAHI VNRRPLFTHL
     AVRIQGHYIV AGKTSISPNT TYPSLLEDYR VEYRVTLTED QLPHLEEIHI RGPVRDDIEI
     QVYRRYGGEY GDLTHPDITF SYFQLKQQAA WVWTAKRGPC SVSCGAGLRW VTYSCQDQAQ
     DKWVKNAQCQ GSPQPPAWQE PCVSAPCSPY WVAGDFSPCS VSCGGGLRER SLRCVETQDG
     FLKTLPPARC RAVAQQPAAE VENCNSQPCP TRWEVSDPGP CMSSACEAGL DSRNVTCVSR
     AGDPEKPETA GPCRTDEMSA MLEPCSRSLC SPGLGQVDNT MSLGEEAPSP VGSDKPGAQA
     EHVWTPLVGL CSISCGRGLK ELYFLCMDSV LKMPVQEELC GLASKPPSRW EVCRARPCPA
     RWETQVLAPC PVTCGGGRVP LSVRCVQLDR GHPISVPHSK CSPVPKPGSF EDCSPEPCPA
     RWKVLSLGPC SASCGLGTAT QMVACMQLDQ GHDNEVNETF CKALVRPQAS VPCLIADCAF
     RWHISAWTEC SVSCGDGIQR RHDTCLGPQA QVPVPANFCQ HLPKPMTVRG CWAGPCAGQE
     TSSSLPHKEA TLPSQTQAAA TVASLQWSQP RARTPTLFSA SQSLGLQENL EEHGACGRQY
     LEPTGTIHMR DQGRLDCVVA IGRPLGEVVT LQILESSLKC SAGEQLLLWG RFTWRKTCRK
     MPGMTFSTKT NTVVVKQHRV LPGGGVLLRY WSQPAPGTFY KECDRQLFGP RGEIVSPSLS
     PDGRKAGTCR VFISVAPQAR IAIRALASDM GTASEGTNAN YVSIRDIHSL RTTTFWGQQV
     LYWESEGSEA ELEFSPGFLE AHASLQGEYW TISPRTSEQD DSLALS
//