ASP2_BLAGE
ID ASP2_BLAGE Reviewed; 352 AA.
AC P54958; B0L0M0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Aspartic protease Bla g 2;
DE EC=3.4.23.-;
DE AltName: Full=Allergen Bla g II;
DE AltName: Allergen=Bla g 2;
DE Flags: Precursor;
OS Blattella germanica (German cockroach) (Blatta germanica).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blaberoidea; Ectobiidae;
OC Blattellinae; Blattella.
OX NCBI_TaxID=6973;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7642642; DOI=10.1074/jbc.270.33.19563;
RA Arruda L.K., Vailes L.D., Mann B.J., Shannon J., Fox J.W., Vedvick T.S.,
RA Hayden M.L., Chapman M.D.;
RT "Molecular cloning of a major cockroach (Blattella germanica) allergen, Bla
RT g 2. Sequence homology to the aspartic proteases.";
RL J. Biol. Chem. 270:19563-19568(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lee H., Jeong K.Y., Yong T.-S.;
RT "cDNA sequence encoding a Bla g 2 isoform.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 25-350 IN COMPLEX WITH ANTIBODY,
RP SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-295 AND ASN-340.
RX PubMed=18519566; DOI=10.1074/jbc.m800937200;
RA Li M., Gustchina A., Alexandratos J., Wlodawer A., Wunschmann S.,
RA Kepley C.L., Chapman M.D., Pomes A.;
RT "Crystal structure of a dimerized cockroach allergen Bla g 2 complexed with
RT a monoclonal antibody.";
RL J. Biol. Chem. 283:22806-22814(2008).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 29-348, DISULFIDE BONDS, ZINC
RP BINDING, AND GLYCOSYLATION AT ASN-295 AND ASN-340.
RX PubMed=15811379; DOI=10.1016/j.jmb.2005.02.062;
RA Gustchina A., Li M., Wunschmann S., Chapman M.D., Pomes A., Wlodawer A.;
RT "Crystal structure of cockroach allergen Bla g 2, an unusual zinc binding
RT aspartic protease with a novel mode of self-inhibition.";
RL J. Mol. Biol. 348:433-444(2005).
CC -!- FUNCTION: Functions as a digestive enzyme in the cockroach.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18519566}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; U28863; AAA86744.1; -; mRNA.
DR EMBL; EF203068; ABP35603.1; -; mRNA.
DR PIR; A57164; A57164.
DR PDB; 1YG9; X-ray; 1.30 A; A=25-348.
DR PDB; 2NR6; X-ray; 2.81 A; A/B=25-343.
DR PDB; 3LIZ; X-ray; 1.80 A; A=25-352.
DR PDB; 4RLD; X-ray; 2.90 A; A/B/C/D=25-350.
DR PDBsum; 1YG9; -.
DR PDBsum; 2NR6; -.
DR PDBsum; 3LIZ; -.
DR PDBsum; 4RLD; -.
DR AlphaFoldDB; P54958; -.
DR SMR; P54958; -.
DR Allergome; 141; Bla g 2.
DR Allergome; 3140; Bla g 2.0101.
DR Allergome; 4012; Bla g 2.0201.
DR MEROPS; A01.950; -.
DR iPTMnet; P54958; -.
DR ABCD; P54958; 2 sequenced antibodies.
DR EvolutionaryTrace; P54958; -.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; PTHR47966; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Aspartyl protease; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Protease; Signal;
KW Zinc; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..24
FT /note="Removed in mature form"
FT /id="PRO_0000025935"
FT CHAIN 25..352
FT /note="Aspartic protease Bla g 2"
FT /id="PRO_0000025936"
FT DOMAIN 39..346
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 55
FT /evidence="ECO:0000250"
FT ACT_SITE 239
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15811379,
FT ECO:0000269|PubMed:18519566"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15811379,
FT ECO:0000269|PubMed:18519566"
FT DISULFID 59..151
FT DISULFID 68..73
FT DISULFID 75..136
FT DISULFID 261..272
FT DISULFID 276..309
FT CONFLICT 6
FT /note="L -> I (in Ref. 2; ABP35603)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="K -> R (in Ref. 2; ABP35603)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="S -> F (in Ref. 2; ABP35603)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="V -> G (in Ref. 2; ABP35603)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="T -> A (in Ref. 2; ABP35603)"
FT /evidence="ECO:0000305"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1YG9"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:1YG9"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 102..115
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 118..131
FT /evidence="ECO:0007829|PDB:1YG9"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:2NR6"
FT HELIX 160..166
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:1YG9"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 200..210
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:2NR6"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:1YG9"
FT HELIX 249..259
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:1YG9"
FT HELIX 276..281
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:1YG9"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 308..316
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:1YG9"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 332..337
FT /evidence="ECO:0007829|PDB:1YG9"
FT TURN 338..341
FT /evidence="ECO:0007829|PDB:1YG9"
FT STRAND 342..348
FT /evidence="ECO:0007829|PDB:1YG9"
SQ SEQUENCE 352 AA; 38558 MW; EA334CEB5D060A81 CRC64;
MIGLKLVTVL FAVATITHAA ELQRVPLYKL VHVFINTQYA GITKIGNQNF LTVFDSTSCN
VVVASQECVG GACVCPNLQK YEKLKPKYIS DGNVQVKFFD TGSAVGRGIE DSLTISNLTT
SQQDIVLADE LSQEVCILSA DVVVGIAAPG CPNALKGKTV LENFVEENLI APVFSIHHAR
FQDGEHFGEI IFGGSDWKYV DGEFTYVPLV GDDSWKFRLD GVKIGDTTVA PAGTQAIIDT
SKAIIVGPKA YVNPINEAIG CVVEKTTTRR ICKLDCSKIP SLPDVTFVIN GRNFNISSQY
YIQQNGNLCY SGFQPCGHSD HFFIGDFFVD HYYSEFNWEN KTMGFGRSVE SV
