ID   PEPT1_PSOOV             Reviewed;         322 AA.
AC   Q1EIQ3;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Peptidase 1;
DE            EC=3.4.22.65;
DE   AltName: Full=Mite group 1 allergen Pso o 1;
DE   AltName: Allergen=Pso o 1;
DE   Flags: Precursor;
OS   Psoroptes ovis (Sheep scab mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC   Psoroptidae; Psoroptes.
OX   NCBI_TaxID=83912;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Moredun;
RX   PubMed=16978441; DOI=10.1017/s0031182006001235;
RA   Nisbet A.J., MacKellar A., McLean K., Brennan G.P., Huntley J.F.;
RT   "Eukaryotic expression of recombinant Pso o 1, an allergen from Psoroptes
RT   ovis, and its localization in the mite.";
RL   Parasitology 134:83-89(2007).
CC   -!- FUNCTION: Probable thiol protease.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Broad endopeptidase specificity.; EC=3.4.22.65;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in the gut.
CC       {ECO:0000269|PubMed:16978441}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Common symptoms of mite
CC       allergy are bronchial asthma, allergic rhinitis and conjunctivitis.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR   EMBL; AM269885; CAK32515.1; -; mRNA.
DR   AlphaFoldDB; Q1EIQ3; -.
DR   SMR; Q1EIQ3; -.
DR   Allergome; 739; Pso o 1.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR025660; Pept_his_AS.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
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; PS00639; THIOL_PROTEASE_HIS; 1.
PE   1: Evidence at protein level;
KW   Allergen; Disulfide bond; Glycoprotein; Hydrolase; Protease; Secreted;
KW   Signal; Thiol protease; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..99
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000307766"
FT   CHAIN           100..322
FT                   /note="Peptidase 1"
FT                   /id="PRO_0000307767"
FT   ACT_SITE        134
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        270
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        290
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        152
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        131..171
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   322 AA;  36250 MW;  29FD93A5CE89D85B CRC64;
     MKFVLAIASL LVLSVVYAYP SEIRTFEEFK KAFNKHYVTP EAEQEARQNF LASLEHIEKA
     GKGRINQFSD MSLEEFKNQY LMSDQAYEAL KKEFDLDAGA QACQIGAVNI PNEIDLRALG
     YVTKIKNQVA CGSCWAFSGV ATVESNYLSY DNVSLDLSEQ ELVDCASQHG CGGDTVLNGL
     RYIQKNGVVE EQSYPYKARE GRCQRPNAKR YGIKDLCQIY PPNGDKIRTY LATKQAALSV
     IIGIRDLDSF RHYDGRTILQ SDNGGKRNFH AINIVGYGSK QGVRYWIIRN SWDTTWGDKG
     YGYFVADKNL MGIEKFPLAA ML