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}; 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; 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 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. DR Genevisible; Q13219; HS. 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 //