ID   CYSP_PEA                Reviewed;         363 AA.
AC   P25804;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Cysteine proteinase 15A;
DE            EC=3.4.22.-;
DE   AltName: Full=Turgor-responsive protein 15A;
DE   Flags: Precursor;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Progress No. 9;
RX   PubMed=1715781; DOI=10.1007/bf00017720;
RA   Guerrero F.D., Jones J.T., Mullet J.E.;
RT   "Turgor-responsive gene transcription and RNA levels increase rapidly when
RT   pea shoots are wilted. Sequence and expression of three inducible genes.";
RL   Plant Mol. Biol. 15:11-26(1990).
CC   -!- INDUCTION: By dehydration of shoots but not roots and not by heat shock
CC       or ABA.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC       ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR   EMBL; X54358; CAA38242.1; -; mRNA.
DR   PIR; S11862; S11862.
DR   AlphaFoldDB; P25804; -.
DR   SMR; P25804; -.
DR   MEROPS; C01.022; -.
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; 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; 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.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Signal; Stress response;
KW   Thiol protease; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..131
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026451"
FT   CHAIN           132..363
FT                   /note="Cysteine proteinase 15A"
FT                   /id="PRO_0000026452"
FT   ACT_SITE        156
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        299
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        326
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        249
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        153..203
FT                   /evidence="ECO:0000250"
FT   DISULFID        187..236
FT                   /evidence="ECO:0000250"
FT   DISULFID        292..347
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   363 AA;  40126 MW;  4B0892679C387E16 CRC64;
     MDRRFLFALF LFAAVATAVT DDTNNDDFII RQVVDNEEDH LLNAEHHFTS FKSKFSKSYA
     TKEEHDYRFG VFKSNLIKAK LHQNRDPTAE HGITKFSDLT ASEFRRQFLG LKKRLRLPAH
     AQKAPILPTT NLPEDFDWRE KGAVTPVKDQ GSCGSCWAFS TTGALEGAHY LATGKLVSLS
     EQQLVDCDHV CDPEQAGSCD SGCNGGLMNN AFEYLLESGG VVQEKDYAYT GRDGSCKFDK
     SKVVASVSNF SVVTLDEDQI AANLVKNGPL AVAINAAWMQ TYMSGVSCPY VCAKSRLDHG
     VLLVGFGKGA YAPIRLKEKP YWIIKNSWGQ NWGEQGYYKI CRGRNVCGVD SMVSTVAAAQ
     SNH