CELA1_PIG
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 03-AUG-2022, entry version 200.
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.
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.
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.
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]
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: Acts upon elastin.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins, including elastin. Preferential
CC cleavage: Ala-|-Xaa.; EC=3.4.21.36;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 1 Ca(2+) ion per subunit.;
CC -!- INTERACTION:
CC P00772; P01009: SERPINA1; Xeno; NbExp=2; IntAct=EBI-986248, EBI-986224;
CC -!- SUBCELLULAR LOCATION: Secreted.
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/";
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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; 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; 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.ENSSSCP00000026330; -.
DR BindingDB; P00772; -.
DR ChEMBL; CHEMBL3517; -.
DR MEROPS; S01.153; -.
DR PaxDb; P00772; -.
DR Ensembl; ENSSSCT00015102157; ENSSSCP00015042352; ENSSSCG00015075833.
DR Ensembl; ENSSSCT00045006201; ENSSSCP00045004195; ENSSSCG00045003737.
DR Ensembl; ENSSSCT00065060127; ENSSSCP00065026074; ENSSSCG00065043957.
DR Ensembl; ENSSSCT00070061127; ENSSSCP00070052099; ENSSSCG00070030376.
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; 1314811at2759; -.
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 Genevisible; P00772; SS.
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; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 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 Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
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 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 BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT DISULFID 56..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:4578945"
FT DISULFID 153..220
FT DISULFID 184..200
FT DISULFID 210..240
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
