ID CELA1_PIG Reviewed; 266 AA. AC P00772; Q29625; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1988, sequence version 1. DT 24-JAN-2024, entry version 206. DE RecName: Full=Chymotrypsin-like elastase family member 1; DE EC=3.4.21.36; DE AltName: Full=Elastase-1; DE Flags: Precursor; GN Name=CELA1; Synonyms=ELA1; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3528137; DOI=10.1093/oxfordjournals.jbchem.a135646; RA Shirasu Y., Yoshida H., Mikayama T., Matsuki S., Tanaka J., Ikenaga H.; RT "Isolation and expression in Escherichia coli of a cDNA clone encoding RT porcine pancreatic elastase."; RL J. Biochem. 99:1707-1712(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3648024; DOI=10.1093/jb/101.3.591; RA Tani T., Kawashima I., Furukawa H., Ohmine T., Takiguchi Y.; RT "Characterization of a silent gene for human pancreatic elastase I: RT structure of the 5'-flanking region."; RL J. Biochem. 101:591-599(1987). RN [3] RP PROTEIN SEQUENCE OF 27-266, AND SUBCELLULAR LOCATION. RX PubMed=4578945; DOI=10.1042/bj1310643; RA Shotton D.M., Hartley B.S.; RT "Evidence for the amino acid sequence of porcine pancreatic elastase."; RL Biochem. J. 131:643-675(1973). RN [4] RP PROTEIN SEQUENCE OF 27-266, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=5415108; DOI=10.1038/225802a0; RA Shotton D.M., Hartley B.S.; RT "Amino-acid sequence of porcine pancreatic elastase and its homologies with RT other serine proteinases."; RL Nature 225:802-806(1970). RN [5] RP TISSUE SPECIFICITY. RX PubMed=10620133; DOI=10.1046/j.1523-1747.2000.00825.x; RA Talas U., Dunlop J., Khalaf S., Leigh I.M., Kelsell D.P.; RT "Human elastase 1: evidence for expression in the skin and the RT identification of a frequent frameshift polymorphism."; RL J. Invest. Dermatol. 114:165-170(2000). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=628010; DOI=10.1016/0022-2836(78)90412-6; RA Sawyer L., Shotton D.M., Campbell J.W., Wendell P.L., Muirhead H., RA Watson H.C., Diamond R., Ladner R.C.; RT "The atomic structure of crystalline porcine pancreatic elastase at 2.5-A RT resolution: comparisons with the structure of alpha-chymotrypsin."; RL J. Mol. Biol. 118:137-208(1978). RN [7] RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), AND ACTIVE SITE. RX PubMed=5415110; DOI=10.1038/225811a0; RA Shotton D.M., Watson H.C.; RT "Three-dimensional structure of tosyl-elastase."; RL Nature 225:811-816(1970). RN [8] {ECO:0007744|PDB:1ELA, ECO:0007744|PDB:1ELB, ECO:0007744|PDB:1ELC} RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 27-266 IN COMPLEX WITH CA(2+), RP AND COFACTOR. RX PubMed=7656008; DOI=10.1038/nsb0194-55; RA Mattos C., Rasmussen B., Ding X., Petsko G.A., Ringe D.; RT "Analogous inhibitors of elastase do not always bind analogously."; RL Nat. Struct. Biol. 1:55-58(1994). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF COMPLEX WITH INHIBITOR. RX PubMed=7922044; DOI=10.1016/s0969-2126(00)00068-x; RA Huang K., Strynadka N.C., Bernard V.D., Peanasky R.J., James M.N.; RT "The molecular structure of the complex of Ascaris chymotrypsin/elastase RT inhibitor with porcine elastase."; RL Structure 2:679-689(1994). CC -!- FUNCTION: Serine proteases that hydrolyze many proteins in addition to CC elastin. {ECO:0000269|PubMed:5415108}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of proteins, including elastin. Preferential CC cleavage: Ala-|-Xaa.; EC=3.4.21.36; CC Evidence={ECO:0000269|PubMed:5415108}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:7656008}; CC -!- INTERACTION: CC P00772; P01009: SERPINA1; Xeno; NbExp=2; IntAct=EBI-986248, EBI-986224; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4578945, CC ECO:0000269|PubMed:5415108}. CC -!- TISSUE SPECIFICITY: Pancreas. Basal layers of the epidermis, hair CC follicle and sebaceous gland epithelia (at protein level). CC {ECO:0000269|PubMed:10620133}. CC -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00274}. CC -!- WEB RESOURCE: Name=Worthington enzyme manual; CC URL="https://www.worthington-biochem.com/ES/"; 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; X04036; CAA27670.1; -; Transcribed_RNA. DR EMBL; D00160; BAA00118.1; -; mRNA. DR PIR; JS0013; ELPG. DR RefSeq; NP_998988.1; NM_213823.1. DR RefSeq; XP_005655631.1; XM_005655574.2. DR PDB; 1B0E; X-ray; 1.80 A; A=27-266. DR PDB; 1BMA; X-ray; 1.80 A; A=27-266. DR PDB; 1BTU; X-ray; 1.60 A; A=27-266. DR PDB; 1C1M; X-ray; 2.20 A; A=27-266. DR PDB; 1E34; X-ray; 1.80 A; B=27-266. DR PDB; 1E35; X-ray; 1.90 A; B=27-266. DR PDB; 1E36; X-ray; 1.70 A; B=27-266. DR PDB; 1E37; X-ray; 1.75 A; B=27-266. DR PDB; 1E38; X-ray; 1.70 A; B=27-266. DR PDB; 1EAI; X-ray; 2.40 A; A/B=27-266. DR PDB; 1EAS; X-ray; 1.80 A; A=27-266. DR PDB; 1EAT; X-ray; 2.00 A; A=27-266. DR PDB; 1EAU; X-ray; 2.00 A; A=27-266. DR PDB; 1ELA; X-ray; 2.00 A; A=27-266. DR PDB; 1ELB; X-ray; 2.10 A; A=27-266. DR PDB; 1ELC; X-ray; 1.75 A; A=27-266. DR PDB; 1ELD; X-ray; 2.00 A; E=27-266. DR PDB; 1ELE; X-ray; 2.00 A; E=27-266. DR PDB; 1ELF; X-ray; 1.70 A; A=27-266. DR PDB; 1ELG; X-ray; 1.65 A; A=27-266. DR PDB; 1ESA; X-ray; 1.65 A; A=27-266. DR PDB; 1ESB; X-ray; 2.30 A; A=27-266. DR PDB; 1EST; X-ray; 2.50 A; A=27-266. DR PDB; 1FLE; X-ray; 1.90 A; E=27-266. DR PDB; 1FZZ; X-ray; 1.86 A; A=27-266. DR PDB; 1GVK; X-ray; 0.94 A; B=27-266. DR PDB; 1GWA; X-ray; 1.85 A; A=27-266. DR PDB; 1H9L; X-ray; 1.67 A; B=27-266. DR PDB; 1HAX; X-ray; 1.60 A; B=27-266. DR PDB; 1HAY; X-ray; 1.70 A; B=27-266. DR PDB; 1HAZ; X-ray; 1.40 A; B=27-266. DR PDB; 1HB0; X-ray; 2.05 A; B=27-266. DR PDB; 1HV7; X-ray; 1.70 A; A=27-266. DR PDB; 1INC; X-ray; 1.94 A; A=27-266. DR PDB; 1JIM; X-ray; 2.31 A; A=27-266. DR PDB; 1L0Z; X-ray; 1.50 A; A=27-266. DR PDB; 1L1G; X-ray; 1.50 A; A=27-266. DR PDB; 1LKA; X-ray; 1.70 A; A=27-266. DR PDB; 1LKB; X-ray; 1.70 A; A=27-266. DR PDB; 1LVY; X-ray; 1.87 A; A=27-266. DR PDB; 1MCV; X-ray; 1.80 A; A=27-266. DR PDB; 1MMJ; X-ray; 2.20 A; N=27-266. DR PDB; 1NES; X-ray; 1.65 A; E=27-266. DR PDB; 1OKX; X-ray; 2.80 A; A/B=27-266. DR PDB; 1QGF; X-ray; 1.70 A; A=27-266. DR PDB; 1QIX; X-ray; 1.90 A; B=27-266. DR PDB; 1QNJ; X-ray; 1.10 A; A=27-266. DR PDB; 1QR3; X-ray; 1.60 A; E=27-266. DR PDB; 1UO6; X-ray; 1.65 A; A=27-266. DR PDB; 1UVO; X-ray; 1.85 A; A=27-266. DR PDB; 1UVP; X-ray; 1.85 A; A=27-266. DR PDB; 2A7C; X-ray; 1.65 A; A=27-266. DR PDB; 2A7J; X-ray; 1.65 A; A=27-266. DR PDB; 2BB4; X-ray; 1.60 A; A=27-266. DR PDB; 2BD2; X-ray; 1.70 A; A=27-266. DR PDB; 2BD3; X-ray; 1.60 A; A=27-266. DR PDB; 2BD4; X-ray; 1.70 A; A=27-266. DR PDB; 2BD5; X-ray; 1.80 A; A=27-266. DR PDB; 2BD7; X-ray; 1.60 A; A=27-266. DR PDB; 2BD8; X-ray; 1.70 A; A=27-266. DR PDB; 2BD9; X-ray; 1.90 A; A=27-266. DR PDB; 2BDA; X-ray; 1.80 A; A=27-266. DR PDB; 2BDB; X-ray; 1.70 A; A=27-266. DR PDB; 2BDC; X-ray; 1.80 A; A=27-266. DR PDB; 2BLO; X-ray; 1.33 A; A=27-266. DR PDB; 2BLQ; X-ray; 1.33 A; A=27-266. DR PDB; 2CV3; X-ray; 1.90 A; A=27-266. DR PDB; 2D26; X-ray; 3.30 A; C=27-266. DR PDB; 2DE8; X-ray; 1.50 A; A=27-266. DR PDB; 2DE9; X-ray; 1.30 A; A=27-266. DR PDB; 2EST; X-ray; 2.50 A; E=27-266. DR PDB; 2FO9; X-ray; 2.00 A; A=27-266. DR PDB; 2FOA; X-ray; 1.90 A; A=27-266. DR PDB; 2FOB; X-ray; 1.90 A; A=27-266. DR PDB; 2FOC; X-ray; 2.00 A; A=27-266. DR PDB; 2FOD; X-ray; 2.00 A; A=27-266. DR PDB; 2FOE; X-ray; 2.20 A; A=27-266. DR PDB; 2FOF; X-ray; 2.20 A; A=27-266. DR PDB; 2FOG; X-ray; 1.90 A; A=27-266. DR PDB; 2FOH; X-ray; 1.80 A; A=27-266. DR PDB; 2G4T; X-ray; 2.15 A; A=27-266. DR PDB; 2G4U; X-ray; 1.84 A; A=27-266. DR PDB; 2H1U; X-ray; 1.60 A; A=27-266. DR PDB; 2IOT; X-ray; 1.60 A; A=27-266. DR PDB; 2OQU; X-ray; 1.80 A; A=27-266. DR PDB; 2V0B; X-ray; 1.65 A; A=27-266. DR PDB; 2V35; X-ray; 1.67 A; A=27-266. DR PDB; 3E3T; X-ray; 1.60 A; A=27-266. DR PDB; 3EST; X-ray; 1.65 A; A=27-266. DR PDB; 3HGN; Other; 1.65 A; A=27-266. DR PDB; 3HGP; X-ray; 0.94 A; A=27-266. DR PDB; 3MNB; X-ray; 1.20 A; A=27-266. DR PDB; 3MNC; X-ray; 1.12 A; A=27-266. DR PDB; 3MNS; X-ray; 1.50 A; A=27-266. DR PDB; 3MNX; X-ray; 1.39 A; A=27-266. DR PDB; 3MO3; X-ray; 1.80 A; A=27-266. DR PDB; 3MO6; X-ray; 1.66 A; A=27-266. DR PDB; 3MO9; X-ray; 2.00 A; A=27-266. DR PDB; 3MOC; X-ray; 1.82 A; A=27-266. DR PDB; 3MTY; X-ray; 1.10 A; A=27-266. DR PDB; 3MU0; X-ray; 1.40 A; A=27-266. DR PDB; 3MU1; X-ray; 1.74 A; A=27-266. DR PDB; 3MU4; X-ray; 1.10 A; A=27-266. DR PDB; 3MU5; X-ray; 1.40 A; A=27-266. DR PDB; 3MU8; X-ray; 1.55 A; A=27-266. DR PDB; 3ODD; X-ray; 1.10 A; A=27-266. DR PDB; 3ODF; X-ray; 1.10 A; A=27-266. DR PDB; 3UOU; X-ray; 2.00 A; A=27-266. DR PDB; 4EST; X-ray; 1.78 A; E=27-266. DR PDB; 4GVU; X-ray; 1.55 A; A=27-266. DR PDB; 4YM9; X-ray; 1.80 A; A=27-266. DR PDB; 5AVD; X-ray; 0.86 A; A=27-266. DR PDB; 5EST; X-ray; 2.09 A; E=27-266. DR PDB; 6EST; X-ray; 1.80 A; A=27-266. DR PDB; 6Q8S; X-ray; 1.80 A; A=27-266. DR PDB; 6QBU; X-ray; 1.38 A; A=27-266. DR PDB; 6QEN; X-ray; 1.20 A; A=27-266. DR PDB; 6QEO; X-ray; 1.30 A; A=27-266. DR PDB; 6TH7; X-ray; 2.20 A; A/B=27-266. DR PDB; 7EST; X-ray; 1.80 A; E=27-266. DR PDB; 7FAG; X-ray; 1.30 A; A=27-266. DR PDB; 8B04; X-ray; 1.60 A; A=1-266. DR PDB; 8B1Y; X-ray; 1.12 A; A=1-266. DR PDB; 8B49; X-ray; 1.19 A; A=1-266. DR PDB; 8B53; X-ray; 1.25 A; A=1-266. DR PDB; 8EST; X-ray; 1.78 A; E=27-266. DR PDB; 9EST; X-ray; 1.90 A; A=27-266. DR PDBsum; 1B0E; -. DR PDBsum; 1BMA; -. DR PDBsum; 1BTU; -. DR PDBsum; 1C1M; -. DR PDBsum; 1E34; -. DR PDBsum; 1E35; -. DR PDBsum; 1E36; -. DR PDBsum; 1E37; -. DR PDBsum; 1E38; -. DR PDBsum; 1EAI; -. DR PDBsum; 1EAS; -. DR PDBsum; 1EAT; -. DR PDBsum; 1EAU; -. DR PDBsum; 1ELA; -. DR PDBsum; 1ELB; -. DR PDBsum; 1ELC; -. DR PDBsum; 1ELD; -. DR PDBsum; 1ELE; -. DR PDBsum; 1ELF; -. DR PDBsum; 1ELG; -. DR PDBsum; 1ESA; -. DR PDBsum; 1ESB; -. DR PDBsum; 1EST; -. DR PDBsum; 1FLE; -. DR PDBsum; 1FZZ; -. DR PDBsum; 1GVK; -. DR PDBsum; 1GWA; -. DR PDBsum; 1H9L; -. DR PDBsum; 1HAX; -. DR PDBsum; 1HAY; -. DR PDBsum; 1HAZ; -. DR PDBsum; 1HB0; -. DR PDBsum; 1HV7; -. DR PDBsum; 1INC; -. DR PDBsum; 1JIM; -. DR PDBsum; 1L0Z; -. DR PDBsum; 1L1G; -. DR PDBsum; 1LKA; -. DR PDBsum; 1LKB; -. DR PDBsum; 1LVY; -. DR PDBsum; 1MCV; -. DR PDBsum; 1MMJ; -. DR PDBsum; 1NES; -. DR PDBsum; 1OKX; -. DR PDBsum; 1QGF; -. DR PDBsum; 1QIX; -. DR PDBsum; 1QNJ; -. DR PDBsum; 1QR3; -. DR PDBsum; 1UO6; -. DR PDBsum; 1UVO; -. DR PDBsum; 1UVP; -. DR PDBsum; 2A7C; -. DR PDBsum; 2A7J; -. DR PDBsum; 2BB4; -. DR PDBsum; 2BD2; -. DR PDBsum; 2BD3; -. DR PDBsum; 2BD4; -. DR PDBsum; 2BD5; -. DR PDBsum; 2BD7; -. DR PDBsum; 2BD8; -. DR PDBsum; 2BD9; -. DR PDBsum; 2BDA; -. DR PDBsum; 2BDB; -. DR PDBsum; 2BDC; -. DR PDBsum; 2BLO; -. DR PDBsum; 2BLQ; -. DR PDBsum; 2CV3; -. DR PDBsum; 2D26; -. DR PDBsum; 2DE8; -. DR PDBsum; 2DE9; -. DR PDBsum; 2EST; -. DR PDBsum; 2FO9; -. DR PDBsum; 2FOA; -. DR PDBsum; 2FOB; -. DR PDBsum; 2FOC; -. DR PDBsum; 2FOD; -. DR PDBsum; 2FOE; -. DR PDBsum; 2FOF; -. DR PDBsum; 2FOG; -. DR PDBsum; 2FOH; -. DR PDBsum; 2G4T; -. DR PDBsum; 2G4U; -. DR PDBsum; 2H1U; -. DR PDBsum; 2IOT; -. DR PDBsum; 2OQU; -. DR PDBsum; 2V0B; -. DR PDBsum; 2V35; -. DR PDBsum; 3E3T; -. DR PDBsum; 3EST; -. DR PDBsum; 3HGN; -. DR PDBsum; 3HGP; -. DR PDBsum; 3MNB; -. DR PDBsum; 3MNC; -. DR PDBsum; 3MNS; -. DR PDBsum; 3MNX; -. DR PDBsum; 3MO3; -. DR PDBsum; 3MO6; -. DR PDBsum; 3MO9; -. DR PDBsum; 3MOC; -. DR PDBsum; 3MTY; -. DR PDBsum; 3MU0; -. DR PDBsum; 3MU1; -. DR PDBsum; 3MU4; -. DR PDBsum; 3MU5; -. DR PDBsum; 3MU8; -. DR PDBsum; 3ODD; -. DR PDBsum; 3ODF; -. DR PDBsum; 3UOU; -. DR PDBsum; 4EST; -. DR PDBsum; 4GVU; -. DR PDBsum; 4YM9; -. DR PDBsum; 5AVD; -. DR PDBsum; 5EST; -. DR PDBsum; 6EST; -. DR PDBsum; 6Q8S; -. DR PDBsum; 6QBU; -. DR PDBsum; 6QEN; -. DR PDBsum; 6QEO; -. DR PDBsum; 6TH7; -. DR PDBsum; 7EST; -. DR PDBsum; 7FAG; -. DR PDBsum; 8B04; -. DR PDBsum; 8B1Y; -. DR PDBsum; 8B49; -. DR PDBsum; 8B53; -. DR PDBsum; 8EST; -. DR PDBsum; 9EST; -. DR AlphaFoldDB; P00772; -. DR PCDDB; P00772; -. DR SMR; P00772; -. DR BioGRID; 1148920; 1. DR DIP; DIP-378N; -. DR IntAct; P00772; 1. DR MINT; P00772; -. DR STRING; 9823.ENSSSCP00000064311; -. DR BindingDB; P00772; -. DR ChEMBL; CHEMBL3517; -. DR MEROPS; S01.153; -. DR PaxDb; 9823-ENSSSCP00000026330; -. DR Ensembl; ENSSSCT00015102157.1; ENSSSCP00015042352.1; ENSSSCG00015075833.1. DR Ensembl; ENSSSCT00045006201.1; ENSSSCP00045004195.1; ENSSSCG00045003737.1. DR Ensembl; ENSSSCT00065060127.1; ENSSSCP00065026074.1; ENSSSCG00065043957.1. DR Ensembl; ENSSSCT00070061127.1; ENSSSCP00070052099.1; ENSSSCG00070030376.1. DR GeneID; 396766; -. DR KEGG; ssc:396766; -. DR CTD; 1990; -. DR eggNOG; KOG3627; Eukaryota. DR HOGENOM; CLU_006842_0_4_1; -. DR InParanoid; P00772; -. DR OrthoDB; 4629979at2759; -. DR TreeFam; TF330455; -. DR BRENDA; 3.4.21.36; 6170. DR EvolutionaryTrace; P00772; -. DR PRO; PR:P00772; -. DR Proteomes; UP000008227; Unplaced. DR Proteomes; UP000314985; Chromosome 5. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB. DR GO; GO:0006508; P:proteolysis; IBA:GO_Central. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR InterPro; IPR033116; TRYPSIN_SER. DR PANTHER; PTHR24257; CHYMOTRYPSIN-LIKE ELASTASE FAMILY MEMBER; 1. DR PANTHER; PTHR24257:SF0; CHYMOTRYPSIN-LIKE ELASTASE FAMILY MEMBER 1; 1. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. DR Genevisible; P00772; SS. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Direct protein sequencing; Disulfide bond; KW Hydrolase; Metal-binding; Protease; Reference proteome; Secreted; KW Serine protease; Signal; Zymogen. FT SIGNAL 1..16 FT /evidence="ECO:0000269|PubMed:4578945, FT ECO:0000269|PubMed:5415108" FT PROPEP 17..26 FT /note="Activation peptide" FT /evidence="ECO:0000269|PubMed:4578945, FT ECO:0000269|PubMed:5415108" FT /id="PRO_0000027681" FT CHAIN 27..266 FT /note="Chymotrypsin-like elastase family member 1" FT /id="PRO_0000027682" FT DOMAIN 27..264 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 71 FT /note="Charge relay system" FT /evidence="ECO:0000269|PubMed:4578945, FT ECO:0000269|PubMed:5415110" FT ACT_SITE 119 FT /note="Charge relay system" FT /evidence="ECO:0000269|PubMed:5415110" FT ACT_SITE 214 FT /note="Charge relay system" FT /evidence="ECO:0000269|PubMed:5415110" FT BINDING 85 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:7656008, FT ECO:0007744|PDB:1ELA, ECO:0007744|PDB:1ELB, FT ECO:0007744|PDB:1ELC" FT BINDING 87 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:7656008, FT ECO:0007744|PDB:1ELA, ECO:0007744|PDB:1ELB, FT ECO:0007744|PDB:1ELC" FT BINDING 90 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:7656008, FT ECO:0007744|PDB:1ELA, ECO:0007744|PDB:1ELB, FT ECO:0007744|PDB:1ELC" FT BINDING 95 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:7656008, FT ECO:0007744|PDB:1ELA, ECO:0007744|PDB:1ELB, FT ECO:0007744|PDB:1ELC" FT DISULFID 56..72 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274, FT ECO:0000269|PubMed:4578945, ECO:0000269|PubMed:7656008, FT ECO:0007744|PDB:1ELA, ECO:0007744|PDB:1ELB, FT ECO:0007744|PDB:1ELC" FT DISULFID 153..220 FT /evidence="ECO:0000269|PubMed:7656008, FT ECO:0007744|PDB:1ELA, ECO:0007744|PDB:1ELB, FT ECO:0007744|PDB:1ELC" FT DISULFID 184..200 FT /evidence="ECO:0000269|PubMed:7656008, FT ECO:0007744|PDB:1ELA, ECO:0007744|PDB:1ELB, FT ECO:0007744|PDB:1ELC" FT DISULFID 210..240 FT /evidence="ECO:0000269|PubMed:7656008, FT ECO:0007744|PDB:1ELA, ECO:0007744|PDB:1ELB, FT ECO:0007744|PDB:1ELC" FT CONFLICT 92 FT /note="D -> N (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 126 FT /note="A -> G (in Ref. 2; BAA00118)" FT /evidence="ECO:0000305" FT CONFLICT 184 FT /note="C -> L (in Ref. 2; BAA00118)" FT /evidence="ECO:0000305" FT CONFLICT 204 FT /note="D -> N (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT TURN 35..37 FT /evidence="ECO:0007829|PDB:3HGP" FT STRAND 41..48 FT /evidence="ECO:0007829|PDB:5AVD" FT STRAND 51..62 FT /evidence="ECO:0007829|PDB:5AVD" FT STRAND 65..68 FT /evidence="ECO:0007829|PDB:5AVD" FT HELIX 70..73 FT /evidence="ECO:0007829|PDB:5AVD" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:3HGP" FT STRAND 79..84 FT /evidence="ECO:0007829|PDB:5AVD" FT STRAND 87..90 FT /evidence="ECO:0007829|PDB:2DE9" FT STRAND 96..105 FT /evidence="ECO:0007829|PDB:5AVD" FT STRAND 111..113 FT /evidence="ECO:0007829|PDB:2D26" FT HELIX 114..116 FT /evidence="ECO:0007829|PDB:5AVD" FT STRAND 121..127 FT /evidence="ECO:0007829|PDB:5AVD" FT STRAND 132..134 FT /evidence="ECO:0007829|PDB:1EAS" FT STRAND 153..158 FT /evidence="ECO:0007829|PDB:5AVD" FT STRAND 160..162 FT /evidence="ECO:0007829|PDB:5AVD" FT STRAND 172..175 FT /evidence="ECO:0007829|PDB:5AVD" FT HELIX 181..184 FT /evidence="ECO:0007829|PDB:5AVD" FT TURN 187..190 FT /evidence="ECO:0007829|PDB:5AVD" FT HELIX 191..193 FT /evidence="ECO:0007829|PDB:5AVD" FT STRAND 198..201 FT /evidence="ECO:0007829|PDB:5AVD" FT STRAND 204..206 FT /evidence="ECO:0007829|PDB:5AVD" FT TURN 211..215 FT /evidence="ECO:0007829|PDB:2V0B" FT STRAND 217..222 FT /evidence="ECO:0007829|PDB:5AVD" FT STRAND 225..234 FT /evidence="ECO:0007829|PDB:5AVD" FT STRAND 239..242 FT /evidence="ECO:0007829|PDB:5AVD" FT STRAND 247..251 FT /evidence="ECO:0007829|PDB:5AVD" FT HELIX 252..254 FT /evidence="ECO:0007829|PDB:5AVD" FT HELIX 256..264 FT /evidence="ECO:0007829|PDB:5AVD" SQ SEQUENCE 266 AA; 28821 MW; BF07D6855BB50FE2 CRC64; MLRLLVVASL VLYGHSTQDF PETNARVVGG TEAQRNSWPS QISLQYRSGS SWAHTCGGTL IRQNWVMTAA HCVDRELTFR VVVGEHNLNQ NDGTEQYVGV QKIVVHPYWN TDDVAAGYDI ALLRLAQSVT LNSYVQLGVL PRAGTILANN SPCYITGWGL TRTNGQLAQT LQQAYLPTVD YAICSSSSYW GSTVKNSMVC AGGDGVRSGC QGDSGGPLHC LVNGQYAVHG VTSFVSRLGC NVTRKPTVFT RVSAYISWIN NVIASN //