CYSP_BLOTA
ID CYSP_BLOTA Reviewed; 333 AA.
AC A1KXI0;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Cysteine protease {ECO:0000305};
DE EC=3.4.22.- {ECO:0000305};
DE AltName: Allergen=Blo t 1 {ECO:0000303|PubMed:12911421};
DE Flags: Precursor;
OS Blomia tropicalis (Mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Glycyphagoidea; Echimyopodidae;
OC Blomia.
OX NCBI_TaxID=40697 {ECO:0000312|EMBL:AAQ24541.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RX PubMed=12911421; DOI=10.1034/j.1398-9995.2003.00215.x;
RA Cheong N., Soon S.C., Ramos J.D., Kuo I.C., Kolatkar P.R., Lee B.W.,
RA Chua K.Y., Kolortkar P.R.;
RT "Lack of human IgE cross-reactivity between mite allergens Blo t 1 and Der
RT p 1.";
RL Allergy 58:912-920(2003).
RN [2] {ECO:0000312|EMBL:AAQ24541.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chew F.T., Wang W.-L., Shang H.S., Kuay K.T., Lim S.H., Lee B.W.;
RT "Identification and cloning of group 1 allergen from Blomia tropicalis.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007744|PDB:5JT8}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 24-333, SUBUNIT, DISULFIDE BONDS,
RP AND GLYCOSYLATION AT ASN-93.
RX PubMed=27997997; DOI=10.1111/all.13111;
RA Meno K.H., Kastrup J.S., Kuo I.C., Chua K.Y., Gajhede M.;
RT "The structure of the mite allergen Blo t 1 explains the limited antibody
RT cross-reactivity to Der p 1.";
RL Allergy 72:665-670(2017).
CC -!- FUNCTION: Cysteine protease. {ECO:0000250|UniProtKB:A5HII1}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:27997997}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC {ECO:0000269|PubMed:12911421}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255,
CC ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-
CC ProRule:PRU10090, ECO:0000255|RuleBase:RU362133}.
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DR EMBL; AY291322; AAQ24541.1; -; mRNA.
DR PDB; 5JT8; X-ray; 2.10 A; A/B=1-333.
DR PDBsum; 5JT8; -.
DR AlphaFoldDB; A1KXI0; -.
DR SMR; A1KXI0; -.
DR Allergome; 146; Blo t 1.
DR iPTMnet; A1KXI0; -.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Signal; Thiol protease; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..108
FT /note="Activation peptide"
FT /evidence="ECO:0000305|PubMed:27997997"
FT /id="PRO_0000444427"
FT CHAIN 109..333
FT /note="Cysteine protease"
FT /evidence="ECO:0000305|PubMed:27997997"
FT /id="PRO_0000444428"
FT ACT_SITE 137
FT /evidence="ECO:0000250|UniProtKB:P00784"
FT ACT_SITE 281
FT /evidence="ECO:0000250|UniProtKB:P00784"
FT ACT_SITE 301
FT /evidence="ECO:0000250|UniProtKB:P00784"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:27997997, ECO:0007744|PDB:5JT8"
FT DISULFID 134..182
FT /evidence="ECO:0000269|PubMed:27997997,
FT ECO:0007744|PDB:5JT8"
FT DISULFID 168..214
FT /evidence="ECO:0000269|PubMed:27997997,
FT ECO:0007744|PDB:5JT8"
FT CONFLICT 133
FT /note="S -> A (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="E -> G (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="S -> P (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="E -> R (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="N -> D (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="Q -> H (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="F -> Y (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:5JT8"
FT HELIX 42..62
FT /evidence="ECO:0007829|PDB:5JT8"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:5JT8"
FT TURN 74..77
FT /evidence="ECO:0007829|PDB:5JT8"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:5JT8"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:5JT8"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:5JT8"
FT HELIX 137..154
FT /evidence="ECO:0007829|PDB:5JT8"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:5JT8"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:5JT8"
FT HELIX 187..196
FT /evidence="ECO:0007829|PDB:5JT8"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:5JT8"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:5JT8"
FT HELIX 237..247
FT /evidence="ECO:0007829|PDB:5JT8"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:5JT8"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:5JT8"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:5JT8"
FT STRAND 281..291
FT /evidence="ECO:0007829|PDB:5JT8"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:5JT8"
FT TURN 305..308
FT /evidence="ECO:0007829|PDB:5JT8"
FT STRAND 312..319
FT /evidence="ECO:0007829|PDB:5JT8"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:5JT8"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:5JT8"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:5JT8"
SQ SEQUENCE 333 AA; 38102 MW; 8C62C882C0CB4AC9 CRC64;
MKFLLVAALC ALVAIGSCKP TREEIKTFEQ FKKVFGKVYR NAEEEARREH HFKEQLKWVE
EHNGIDGVEY AINEYSDMSE QEFSFHLSGG GLNFTYMKME AAKEPLINTY GSLPQNFDWR
QKARLTRIRQ QGSCGSCWAF AAAGVAESLY SIQKQQSIEL SEQELVDCTY NRYDSSYQCN
GCGSGYSTEA FKYMIRTGLV EEENYPYNMR TQWCNPDVEG QRYHVSGYQQ LRYQSSDEDV
MYTIQQHGPV VIYMHGSNNY FRNLGNGVLR GVAYNDAYTD HAVILVGWGT VQGVDYWIIR
NSWGTGWGNG GYGYVERGHN SLGINNFVTY ATL
