ID PAPP1_HUMAN Reviewed; 1627 AA.
AC Q13219; B1AMF9; Q08371; Q68G52; Q9UDK7;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 3.
DT 24-JAN-2024, entry version 225.
DE RecName: Full=Pappalysin-1;
DE EC=3.4.24.79;
DE AltName: Full=Insulin-like growth factor-dependent IGF-binding protein 4 protease;
DE Short=IGF-dependent IGFBP-4 protease;
DE Short=IGFBP-4ase;
DE AltName: Full=Pregnancy-associated plasma protein A;
DE Short=PAPP-A;
DE Flags: Precursor;
GN Name=PAPPA;
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 [MRNA], INDUCTION, AND VARIANT ARG-944.
RC TISSUE=Placenta;
RX PubMed=8620868; DOI=10.1111/j.1432-1033.1996.0159n.x;
RA Haaning J., Oxvig C., Overgaard M.T., Ebbesen P., Kristensen T.,
RA Sottrup-Jensen L.;
RT "Complete cDNA sequence of the preproform of human pregnancy-associated
RT plasma protein-A. Evidence for expression in the brain and induction by
RT cAMP.";
RL Eur. J. Biochem. 237:159-163(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TYR-1224.
RC TISSUE=Placenta;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 77-1627, PROTEIN SEQUENCE OF 82-98; 117-126;
RP 210-224; 466-485; 507-519; 576-593; 609-621; 718-736; 742-754; 1006-1017;
RP 1259-1273; 1369-1374; 1389-1398; 1490-1509; 1524-1533 AND 1537-1544,
RP VARIANT ARG-944, AND TISSUE SPECIFICITY.
RC TISSUE=Placenta, and Serum;
RX PubMed=7508748; DOI=10.1021/bi00172a040;
RA Kristensen T., Oxvig C., Sand O., Moller N.P.H., Sottrup-Jensen L.;
RT "Amino acid sequence of human pregnancy-associated plasma protein-A derived
RT from cloned cDNA.";
RL Biochemistry 33:1592-1598(1994).
RN [5]
RP PROTEIN SEQUENCE OF 81-89; 117-126; 210-224; 460-485; 507-519; 576-593;
RP 718-736; 742-754; 1259-1273; 1369-1374; 1490-1509; 1524-1533 AND 1537-1544,
RP SUBUNIT, AND INTERCHAIN DISULFIDE BOND.
RC TISSUE=Serum;
RX PubMed=7685339; DOI=10.1016/s0021-9258(18)31378-4;
RA Oxvig C., Sand O., Kristensen T., Gleich G.J., Sottrup-Jensen L.;
RT "Circulating human pregnancy-associated plasma protein-A is disulfide-
RT bridged to the proform of eosinophil major basic protein.";
RL J. Biol. Chem. 268:12243-12246(1993).
RN [6]
RP PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-402; ASN-429; ASN-480;
RP ASN-601; ASN-619; ASN-725; ASN-1026; ASN-1226; ASN-1323 AND ASN-1519, AND
RP DISULFIDE BONDS.
RX PubMed=12421832; DOI=10.1074/jbc.m208777200;
RA Overgaard M.T., Sorensen E.S., Stachowiak D., Boldt H.B., Kristensen L.,
RA Sottrup-Jensen L., Oxvig C.;
RT "Complex of pregnancy-associated plasma protein-A and the proform of
RT eosinophil major basic protein. Disulfide structure and carbohydrate
RT attachment sites.";
RL J. Biol. Chem. 278:2106-2117(2003).
RN [7]
RP IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Fibroblast;
RX PubMed=10077652; DOI=10.1073/pnas.96.6.3149;
RA Lawrence J.B., Oxvig C., Overgaard M.T., Sottrup-Jensen L., Gleich G.J.,
RA Hays L.G., Yates J.R. III, Conover C.A.;
RT "The insulin-like growth factor (IGF)-dependent IGF binding protein-4
RT protease secreted by human fibroblasts is pregnancy-associated plasma
RT protein-A.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:3149-3153(1999).
RN [8]
RP FUNCTION, SUBUNIT, AND ACTIVITY REGULATION.
RX PubMed=10913121; DOI=10.1074/jbc.m001384200;
RA Overgaard M.T., Haaning J., Boldt H.B., Olsen I.M., Laursen L.S.,
RA Christiansen M., Gleich G.J., Sottrup-Jensen L., Conover C.A., Oxvig C.;
RT "Expression of recombinant human pregnancy-associated plasma protein-A and
RT identification of the proform of eosinophil major basic protein as its
RT physiological inhibitor.";
RL J. Biol. Chem. 275:31128-31133(2000).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=7526035;
RA Bonno M., Oxvig C., Kephart G.M., Wagner J.M., Kristensen T.,
RA Sottrup-Jensen L., Gleich G.J.;
RT "Localization of pregnancy-associated plasma protein-A and colocalization
RT of pregnancy-associated plasma protein-A messenger ribonucleic acid and
RT eosinophil granule major basic protein messenger ribonucleic acid in
RT placenta.";
RL Lab. Invest. 71:560-566(1994).
RN [10]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10491647; DOI=10.1095/biolreprod61.4.1083;
RA Overgaard M.T., Oxvig C., Christiansen M., Lawrence J.B., Conover C.A.,
RA Gleich G.J., Sottrup-Jensen L., Haaning J.;
RT "Messenger ribonucleic acid levels of pregnancy-associated plasma protein-A
RT and the proform of eosinophil major basic protein: expression in human
RT reproductive and nonreproductive tissues.";
RL Biol. Reprod. 61:1083-1089(1999).
RN [11]
RP DEVELOPMENTAL STAGE.
RX PubMed=7539791; DOI=10.1074/jbc.270.23.13645;
RA Oxvig C., Haaning J., Kristensen L., Wagner J.M., Rubin I., Stigbrand T.,
RA Gleich G.J., Sottrup-Jensen L.;
RT "Identification of angiotensinogen and complement C3dg as novel proteins
RT binding the proform of eosinophil major basic protein in human pregnancy
RT serum and plasma.";
RL J. Biol. Chem. 270:13645-13651(1995).
RN [12]
RP FUNCTION.
RX PubMed=11522292; DOI=10.1016/s0014-5793(01)02760-0;
RA Laursen L.S., Overgaard M.T., Soe R., Boldt H.B., Sottrup-Jensen L.,
RA Giudice L.C., Conover C.A., Oxvig C.;
RT "Pregnancy-associated plasma protein-A (PAPP-A) cleaves insulin-like growth
RT factor binding protein (IGFBP)-5 independent of IGF: implications for the
RT mechanism of IGFBP-4 proteolysis by PAPP-A.";
RL FEBS Lett. 504:36-40(2001).
RN [13]
RP VARIANT TYR-1224.
RX PubMed=11822024; DOI=10.1086/339083;
RA Frosk P., Weiler T., Nylen E., Sudha T., Greenberg C.R., Morgan K.,
RA Fujiwara T.M., Wrogemann K.;
RT "Limb-girdle muscular dystrophy type 2H associated with mutation in TRIM32,
RT a putative E3-ubiquitin-ligase gene.";
RL Am. J. Hum. Genet. 70:663-672(2002).
CC -!- FUNCTION: Metalloproteinase which specifically cleaves IGFBP-4 and
CC IGFBP-5, resulting in release of bound IGF. Cleavage of IGFBP-4 is
CC dramatically enhanced by the presence of IGF, whereas cleavage of
CC IGFBP-5 is slightly inhibited by the presence of IGF.
CC {ECO:0000269|PubMed:10077652, ECO:0000269|PubMed:10913121,
CC ECO:0000269|PubMed:11522292}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of the 135-Met-|-Lys-136 bond in insulin-like growth
CC factor binding protein (IGFBP)-4, and the 143-Ser-|-Lys-144 bond in
CC IGFBP-5.; EC=3.4.24.79;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by complexation with the proform of
CC PRG2. {ECO:0000269|PubMed:10913121}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. In pregnancy serum, predominantly
CC found as a disulfide-linked 2:2 heterotetramer with the proform of
CC PRG2. {ECO:0000269|PubMed:10913121, ECO:0000269|PubMed:12421832,
CC ECO:0000269|PubMed:7685339}.
CC -!- INTERACTION:
CC Q13219; P13727: PRG2; NbExp=2; IntAct=EBI-1221991, EBI-716689;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10077652}.
CC -!- TISSUE SPECIFICITY: High levels in placenta and pregnancy serum. In
CC placenta, expressed in X cells in septa and anchoring villi, and in
CC syncytiotrophoblasts in the chorionic villi. Lower levels are found in
CC a variety of other tissues including kidney, myometrium, endometrium,
CC ovaries, breast, prostate, bone marrow, colon, fibroblasts and
CC osteoblasts. {ECO:0000269|PubMed:10077652, ECO:0000269|PubMed:10491647,
CC ECO:0000269|PubMed:7508748, ECO:0000269|PubMed:7526035}.
CC -!- DEVELOPMENTAL STAGE: Present in serum and placenta during pregnancy;
CC levels increase throughout pregnancy. {ECO:0000269|PubMed:10491647,
CC ECO:0000269|PubMed:7539791}.
CC -!- INDUCTION: By 8-bromoadenosine-3',5'-phosphate.
CC {ECO:0000269|PubMed:8620868}.
CC -!- PTM: There appear to be no free sulfhydryl groups.
CC -!- SIMILARITY: Belongs to the peptidase M43B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50543.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U28727; AAC50543.1; ALT_FRAME; mRNA.
DR EMBL; AL137024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL691426; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC078657; AAH78657.1; -; mRNA.
DR EMBL; X68280; CAA48341.1; -; mRNA.
DR CCDS; CCDS6813.1; -.
DR PIR; S65464; S65464.
DR RefSeq; NP_002572.2; NM_002581.4.
DR PDB; 7UFG; EM; 3.28 A; A/B=81-1627.
DR PDB; 7Y5N; EM; 3.45 A; C/D=81-1627.
DR PDB; 7Y5Q; EM; 3.80 A; A/B=81-1627.
DR PDB; 8A7D; EM; 3.06 A; C/Q=82-1617.
DR PDB; 8A7E; EM; 5.02 A; C/Q=82-1617.
DR PDB; 8D8O; EM; 3.35 A; A/B=81-1627.
DR PDB; 8HGG; EM; 3.64 A; C/D=1-1627.
DR PDB; 8HGH; EM; 4.16 A; A/B=81-1627.
DR PDBsum; 7UFG; -.
DR PDBsum; 7Y5N; -.
DR PDBsum; 7Y5Q; -.
DR PDBsum; 8A7D; -.
DR PDBsum; 8A7E; -.
DR PDBsum; 8D8O; -.
DR PDBsum; 8HGG; -.
DR PDBsum; 8HGH; -.
DR AlphaFoldDB; Q13219; -.
DR EMDB; EMD-15217; -.
DR EMDB; EMD-15219; -.
DR EMDB; EMD-15220; -.
DR EMDB; EMD-15221; -.
DR EMDB; EMD-26475; -.
DR EMDB; EMD-27253; -.
DR EMDB; EMD-33621; -.
DR EMDB; EMD-34738; -.
DR SMR; Q13219; -.
DR BioGRID; 111104; 14.
DR CORUM; Q13219; -.
DR IntAct; Q13219; 10.
DR MINT; Q13219; -.
DR STRING; 9606.ENSP00000330658; -.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR MEROPS; M43.004; -.
DR GlyConnect; 1594; 1 N-Linked glycan (1 site).
DR GlyCosmos; Q13219; 14 sites, 1 glycan.
DR GlyGen; Q13219; 14 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q13219; -.
DR PhosphoSitePlus; Q13219; -.
DR BioMuta; PAPPA; -.
DR DMDM; 223590248; -.
DR EPD; Q13219; -.
DR jPOST; Q13219; -.
DR MassIVE; Q13219; -.
DR PaxDb; 9606-ENSP00000330658; -.
DR PeptideAtlas; Q13219; -.
DR ProteomicsDB; 59231; -.
DR Pumba; Q13219; -.
DR Antibodypedia; 3385; 937 antibodies from 33 providers.
DR DNASU; 5069; -.
DR Ensembl; ENST00000328252.4; ENSP00000330658.3; ENSG00000182752.10.
DR GeneID; 5069; -.
DR KEGG; hsa:5069; -.
DR MANE-Select; ENST00000328252.4; ENSP00000330658.3; NM_002581.5; NP_002572.2.
DR UCSC; uc004bjn.4; human.
DR AGR; HGNC:8602; -.
DR CTD; 5069; -.
DR DisGeNET; 5069; -.
DR GeneCards; PAPPA; -.
DR HGNC; HGNC:8602; PAPPA.
DR HPA; ENSG00000182752; Tissue enriched (placenta).
DR MIM; 176385; gene.
DR neXtProt; NX_Q13219; -.
DR OpenTargets; ENSG00000182752; -.
DR PharmGKB; PA32935; -.
DR VEuPathDB; HostDB:ENSG00000182752; -.
DR eggNOG; ENOG502QQ7Z; Eukaryota.
DR GeneTree; ENSGT00940000156654; -.
DR HOGENOM; CLU_002636_2_0_1; -.
DR InParanoid; Q13219; -.
DR OMA; KQVVCEP; -.
DR OrthoDB; 5483399at2759; -.
DR PhylomeDB; Q13219; -.
DR TreeFam; TF331636; -.
DR BioCyc; MetaCyc:ENSG00000119398-MONOMER; -.
DR BRENDA; 3.4.24.79; 2681.
DR PathwayCommons; Q13219; -.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR SignaLink; Q13219; -.
DR BioGRID-ORCS; 5069; 28 hits in 1147 CRISPR screens.
DR ChiTaRS; PAPPA; human.
DR GeneWiki; Pregnancy-associated_plasma_protein_A; -.
DR GenomeRNAi; 5069; -.
DR Pharos; Q13219; Tbio.
DR PRO; PR:Q13219; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q13219; Protein.
DR Bgee; ENSG00000182752; Expressed in decidua and 177 other cell types or tissues.
DR Genevisible; Q13219; HS.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004222; F:metalloendopeptidase activity; EXP:Reactome.
DR GO; GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007565; P:female pregnancy; TAS:ProtInc.
DR GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR GO; GO:0019538; P:protein metabolic process; TAS:Reactome.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl.
DR GO; GO:0032354; P:response to follicle-stimulating hormone; IEA:Ensembl.
DR CDD; cd00033; CCP; 4.
DR CDD; cd04275; ZnMc_pappalysin_like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 4.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006558; LamG-like.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR011936; Myxo_disulph_rpt.
DR InterPro; IPR000800; Notch_dom.
DR InterPro; IPR043543; PAPPA/PAPPA2.
DR InterPro; IPR008754; Peptidase_M43.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR NCBIfam; TIGR02232; myxo_disulf_rpt; 1.
DR PANTHER; PTHR46130; LAMGL DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46130:SF2; PAPPALYSIN-1; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR Pfam; PF05572; Peptidase_M43; 1.
DR Pfam; PF00084; Sushi; 2.
DR SMART; SM00032; CCP; 4.
DR SMART; SM00560; LamGL; 1.
DR SMART; SM00004; NL; 3.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 4.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50923; SUSHI; 5.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Repeat; Secreted; Signal; Sushi; Zinc; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..81
FT /evidence="ECO:0000269|PubMed:7508748,
FT ECO:0000269|PubMed:7685339"
FT /id="PRO_0000029245"
FT CHAIN 82..1627
FT /note="Pappalysin-1"
FT /id="PRO_0000029246"
FT DOMAIN 1213..1282
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1283..1344
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1345..1412
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1413..1473
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1476..1556
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 23..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..583
FT /note="Metalloprotease"
FT REGION 733..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 563
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 562
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 566
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 572
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12421832"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12421832"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12421832"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12421832"
FT CARBOHYD 619
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12421832"
FT CARBOHYD 725
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12421832"
FT CARBOHYD 825
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1026
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12421832"
FT CARBOHYD 1222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12421832"
FT CARBOHYD 1323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12421832"
FT CARBOHYD 1465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12421832"
FT DISULFID 144..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 327..622
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 332..657
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 414..428
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 424..440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 457..473
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 461
FT /note="Interchain (with C-51 in PRG2 proform)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 474..485
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 583..600
FT /note="Or C-583 with C-612"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 587..612
FT /note="Or C-587 with C-600"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 710..878
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 713..881
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 732
FT /note="Interchain (with C-169 in PRG2 proform)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 753..835
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 775..781
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 947..975
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 960..971
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 983..990
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 999..1011
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 1036..1070
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 1051..1139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 1192..1205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 1210
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 1215..1269
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 1227..1238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 1242..1280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 1285..1329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 1300..1310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 1314..1342
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 1346..1399
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 1362..1373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 1377..1410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 1415..1458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 1428..1438
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 1442..1471
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 1478..1539
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 1492..1502
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 1506..1554
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT DISULFID 1558..1576
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:12421832"
FT VARIANT 5
FT /note="S -> I (in dbSNP:rs417012)"
FT /id="VAR_057091"
FT VARIANT 325
FT /note="P -> L (in dbSNP:rs445159)"
FT /id="VAR_057092"
FT VARIANT 944
FT /note="S -> R (in dbSNP:rs117124330)"
FT /evidence="ECO:0000269|PubMed:7508748,
FT ECO:0000269|PubMed:8620868"
FT /id="VAR_011419"
FT VARIANT 1224
FT /note="S -> Y (in dbSNP:rs7020782)"
FT /evidence="ECO:0000269|PubMed:11822024,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_018726"
FT CONFLICT 107
FT /note="R -> RV (in Ref. 1; AAC50543 and 4; CAA48341)"
FT /evidence="ECO:0000305"
FT CONFLICT 511..512
FT /note="TH -> RD (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1622
FT /note="R -> Q (in Ref. 3; AAH78657)"
FT /evidence="ECO:0000305"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:7Y5N"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 195..203
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:7Y5N"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:7Y5N"
FT HELIX 265..273
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:7Y5N"
FT HELIX 293..296
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:7Y5N"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:7Y5N"
FT HELIX 335..343
FT /evidence="ECO:0007829|PDB:7Y5N"
FT TURN 345..348
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 351..361
FT /evidence="ECO:0007829|PDB:7Y5N"
FT HELIX 372..385
FT /evidence="ECO:0007829|PDB:7Y5N"
FT TURN 386..390
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 391..401
FT /evidence="ECO:0007829|PDB:7Y5N"
FT HELIX 403..406
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 407..413
FT /evidence="ECO:0007829|PDB:7Y5N"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 419..423
FT /evidence="ECO:0007829|PDB:7Y5N"
FT TURN 431..439
FT /evidence="ECO:0007829|PDB:7Y5N"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:7Y5N"
FT HELIX 467..470
FT /evidence="ECO:0007829|PDB:7Y5N"
FT TURN 471..474
FT /evidence="ECO:0007829|PDB:7Y5N"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:7Y5N"
FT HELIX 481..484
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 494..497
FT /evidence="ECO:0007829|PDB:7Y5N"
FT HELIX 498..505
FT /evidence="ECO:0007829|PDB:7Y5N"
FT TURN 509..511
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 512..517
FT /evidence="ECO:0007829|PDB:7Y5N"
FT TURN 535..538
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 543..546
FT /evidence="ECO:0007829|PDB:7Y5N"
FT TURN 548..552
FT /evidence="ECO:0007829|PDB:7Y5N"
FT HELIX 559..566
FT /evidence="ECO:0007829|PDB:7Y5N"
FT TURN 567..569
FT /evidence="ECO:0007829|PDB:7Y5N"
FT HELIX 573..575
FT /evidence="ECO:0007829|PDB:7Y5N"
FT TURN 576..578
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 579..582
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 594..599
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 610..613
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 619..623
FT /evidence="ECO:0007829|PDB:7Y5N"
FT TURN 641..643
FT /evidence="ECO:0007829|PDB:7Y5N"
FT HELIX 649..661
FT /evidence="ECO:0007829|PDB:7Y5N"
FT HELIX 664..666
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 680..684
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 689..692
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 715..717
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 719..722
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 725..728
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 731..733
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 741..746
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 764..766
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 768..770
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 777..779
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 781..791
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 793..802
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 812..820
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 825..828
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 835..837
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 839..842
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 850..858
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 863..871
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 878..880
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 885..892
FT /evidence="ECO:0007829|PDB:7Y5N"
FT HELIX 896..899
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 903..910
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 918..929
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 938..944
FT /evidence="ECO:0007829|PDB:7Y5N"
FT HELIX 954..956
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 969..971
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 981..983
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 985..987
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 990..992
FT /evidence="ECO:0007829|PDB:7Y5N"
FT TURN 1004..1006
FT /evidence="ECO:0007829|PDB:7Y5N"
FT TURN 1008..1010
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1019..1023
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1028..1031
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1034..1036
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1042..1044
FT /evidence="ECO:0007829|PDB:7Y5N"
FT TURN 1059..1061
FT /evidence="ECO:0007829|PDB:7Y5N"
FT TURN 1063..1065
FT /evidence="ECO:0007829|PDB:7Y5N"
FT HELIX 1074..1079
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1084..1094
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1097..1105
FT /evidence="ECO:0007829|PDB:7Y5N"
FT TURN 1110..1112
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1117..1124
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1129..1136
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1142..1147
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1159..1167
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1173..1183
FT /evidence="ECO:0007829|PDB:7Y5N"
FT HELIX 1186..1191
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1197..1199
FT /evidence="ECO:0007829|PDB:7Y5N"
FT TURN 1200..1203
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1204..1206
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1223..1228
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1237..1242
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1246..1252
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1261..1263
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1265..1270
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1273..1282
FT /evidence="ECO:0007829|PDB:7Y5N"
FT TURN 1290..1292
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1293..1299
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1309..1314
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1316..1323
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1326..1329
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1333..1335
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1339..1343
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1355..1357
FT /evidence="ECO:0007829|PDB:7Y5N"
FT HELIX 1360..1362
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1363..1365
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1372..1377
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1394..1398
FT /evidence="ECO:0007829|PDB:7Y5N"
FT HELIX 1420..1422
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1429..1433
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1454..1456
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1486..1491
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1501..1508
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1511..1515
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1536..1539
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1545..1547
FT /evidence="ECO:0007829|PDB:7Y5N"
FT TURN 1549..1551
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1552..1556
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1563..1565
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1569..1571
FT /evidence="ECO:0007829|PDB:7Y5N"
FT HELIX 1574..1581
FT /evidence="ECO:0007829|PDB:7Y5N"
FT TURN 1585..1587
FT /evidence="ECO:0007829|PDB:7Y5N"
FT STRAND 1595..1600
FT /evidence="ECO:0007829|PDB:7Y5N"
FT TURN 1602..1606
FT /evidence="ECO:0007829|PDB:7Y5N"
FT TURN 1614..1616
FT /evidence="ECO:0007829|PDB:7Y5N"
SQ SEQUENCE 1627 AA; 180973 MW; 202ECA62C1107207 CRC64;
MRLWSWVLHL GLLSAALGCG LAERPRRARR DPRAGRPPRP AAGPATCATR AARGRRASPP
PPPPPGGAWE AVRVPRRRQQ REARGATEEP SPPSRALYFS GRGEQLRLRA DLELPRDAFT
LQVWLRAEGG QRSPAVITGL YDKCSYISRD RGWVVGIHTI SDQDNKDPRY FFSLKTDRAR
QVTTINAHRS YLPGQWVYLA ATYDGQFMKL YVNGAQVATS GEQVGGIFSP LTQKCKVLML
GGSALNHNYR GYIEHFSLWK VARTQREILS DMETHGAHTA LPQLLLQENW DNVKHAWSPM
KDGSSPKVEF SNAHGFLLDT SLEPPLCGQT LCDNTEVIAS YNQLSSFRQP KVVRYRVVNL
YEDDHKNPTV TREQVDFQHH QLAEAFKQYN ISWELDVLEV SNSSLRRRLI LANCDISKIG
DENCDPECNH TLTGHDGGDC RHLRHPAFVK KQHNGVCDMD CNYERFNFDG GECCDPEITN
VTQTCFDPDS PHRAYLDVNE LKNILKLDGS THLNIFFAKS SEEELAGVAT WPWDKEALMH
LGGIVLNPSF YGMPGHTHTM IHEIGHSLGL YHVFRGISEI QSCSDPCMET EPSFETGDLC
NDTNPAPKHK SCGDPGPGND TCGFHSFFNT PYNNFMSYAD DDCTDSFTPN QVARMHCYLD
LVYQGWQPSR KPAPVALAPQ VLGHTTDSVT LEWFPPIDGH FFERELGSAC HLCLEGRILV
QYASNASSPM PCSPSGHWSP REAEGHPDVE QPCKSSVRTW SPNSAVNPHT VPPACPEPQG
CYLELEFLYP LVPESLTIWV TFVSTDWDSS GAVNDIKLLA VSGKNISLGP QNVFCDVPLT
IRLWDVGEEV YGIQIYTLDE HLEIDAAMLT STADTPLCLQ CKPLKYKVVR DPPLQMDVAS
ILHLNRKFVD MDLNLGSVYQ YWVITISGTE ESEPSPAVTY IHGSGYCGDG IIQKDQGEQC
DDMNKINGDG CSLFCRQEVS FNCIDEPSRC YFHDGDGVCE EFEQKTSIKD CGVYTPQGFL
DQWASNASVS HQDQQCPGWV IIGQPAASQV CRTKVIDLSE GISQHAWYPC TISYPYSQLA
QTTFWLRAYF SQPMVAAAVI VHLVTDGTYY GDQKQETISV QLLDTKDQSH DLGLHVLSCR
NNPLIIPVVH DLSQPFYHSQ AVRVSFSSPL VAISGVALRS FDNFDPVTLS SCQRGETYSP
AEQSCVHFAC EKTDCPELAV ENASLNCSSS DRYHGAQCTV SCRTGYVLQI RRDDELIKSQ
TGPSVTVTCT EGKWNKQVAC EPVDCSIPDH HQVYAASFSC PEGTTFGSQC SFQCRHPAQL
KGNNSLLTCM EDGLWSFPEA LCELMCLAPP PVPNADLQTA RCRENKHKVG SFCKYKCKPG
YHVPGSSRKS KKRAFKTQCT QDGSWQEGAC VPVTCDPPPP KFHGLYQCTN GFQFNSECRI
KCEDSDASQG LGSNVIHCRK DGTWNGSFHV CQEMQGQCSV PNELNSNLKL QCPDGYAIGS
ECATSCLDHN SESIILPMNV TVRDIPHWLN PTRVERVVCT AGLKWYPHPA LIHCVKGCEP
FMGDNYCDAI NNRAFCNYDG GDCCTSTVKT KKVTPFPMSC DLQGDCACRD PQAQEHSRKD
LRGYSHG
//
