ID   PRSN_PIEBR              Reviewed;         850 AA.
AC   Q9GV36;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Pierisin {ECO:0000303|PubMed:10971585};
DE            EC=2.4.2.- {ECO:0000250|UniProtKB:Q9U8Q4};
DE   AltName: Full=NAD--DNA ADP-ribosyltransferase;
DE   AltName: Full=Pierisin-2 {ECO:0000303|PubMed:10971585};
DE   AltName: Full=Pierisin-B;
OS   Pieris brassicae (White butterfly) (Large white butterfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Pieridae; Pierinae; Pieris.
OX   NCBI_TaxID=7116 {ECO:0000312|EMBL:BAB13774.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 125-134; 228-272; 278-282;
RP   517-526; 561-570; 786-795 AND 830-841, FUNCTION, AND MUTAGENESIS OF
RP   GLU-165.
RC   TISSUE=Fifth instar larvae, and Pupae;
RX   PubMed=10971585; DOI=10.1046/j.1432-1327.2000.01640.x;
RA   Matsushima-Hibiya Y., Watanabe M., Kono T., Kanazawa T., Koyama K.,
RA   Sugimura T., Wakabayashi K.;
RT   "Purification and cloning of pierisin-2, an apoptosis-inducing protein from
RT   the cabbage butterfly, Pieris brassicae.";
RL   Eur. J. Biochem. 267:5742-5750(2000).
CC   -!- FUNCTION: ADP-ribosylates double-stranded DNA by targeting the N2 amino
CC       group of dG residues. Induces apoptosis in a range of human cell lines
CC       (PubMed:10971585) (By similarity). May play a role in destroying cells
CC       during pupation and/or defense against parasites (By similarity).
CC       {ECO:0000250|UniProtKB:Q9U8Q4, ECO:0000269|PubMed:10971585}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyguanosine in DNA + NAD(+) = an N(2)-(ADP-L-ribosyl)-
CC         2'-deoxyguanosine in DNA + H(+) + nicotinamide; Xref=Rhea:RHEA:71807,
CC         Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:18062, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:85445,
CC         ChEBI:CHEBI:142722; Evidence={ECO:0000250|UniProtKB:Q9U8Q4};
CC   -!- SIMILARITY: Belongs to the pierisin ADP-ribosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AB037676; BAB13774.1; -; mRNA.
DR   AlphaFoldDB; Q9GV36; -.
DR   SMR; Q9GV36; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   GO; GO:0030591; F:2'-deoxyguanosine DNA ADP-ribosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
DR   GO; GO:0030592; P:DNA ADP-ribosylation; ISS:UniProtKB.
DR   CDD; cd00161; RICIN; 3.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   Pfam; PF14200; RicinB_lectin_2; 3.
DR   SMART; SM00458; RICIN; 3.
DR   SUPFAM; SSF50370; SSF50370; 4.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 3.
PE   1: Evidence at protein level;
KW   Apoptosis; Direct protein sequencing; Glycosyltransferase; NAD;
KW   Nucleotidyltransferase; Repeat; Transferase.
FT   CHAIN           1..850
FT                   /note="Pierisin"
FT                   /id="PRO_0000097051"
FT   DOMAIN          267..409
FT                   /note="Ricin B-type lectin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DOMAIN          413..560
FT                   /note="Ricin B-type lectin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DOMAIN          564..707
FT                   /note="Ricin B-type lectin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   MUTAGEN         165
FT                   /note="E->D: Reduced cytotoxic activity."
FT                   /evidence="ECO:0000269|PubMed:10971585"
FT   MUTAGEN         165
FT                   /note="E->Q: Complete loss of cytotoxic activity."
FT                   /evidence="ECO:0000269|PubMed:10971585"
SQ   SEQUENCE   850 AA;  97988 MW;  6E6044049D36FE73 CRC64;
     MSNNPPYMTN GIQAAVVEWI RALDLEIISL LLSRAWPLAL LTTTELRWRP TVLTDTDNVV
     RLDRRQRLVR WDRRPPNEIF LEGFVPIVTR EDPDWEETDL YGFAKNNHPS IFVSTTKTQR
     NKKKYVWTPR NANRGIVYQY EIYAPGGVDV NDSFSDASPW PNQMEVAFPG GIQNIYIRSA
     RELHNGRVQR IWINPNFLDP GDLEPIVSSS RTLQVIWRVN HPDGGNKDGR SERSTSSYDD
     LMYGGTGNVQ EDTFGDESNN PKPIADGEFM IESIKDKNSF LDLSKNVNGG IIHSNVYSGG
     DNQIWVFSYD DNKKAYKIKS YQNSSLYLSW DSNASSKEII LRGYTNSGSN NQYWQIEQTG
     KNYRLRNLLN LNMIITAQDK SSAFGGKEVI VNTEISNSNT KSSQEWNIIP FDFRPIMDGD
     YNIFNLDLPN QVVDFSNQPD LLVHGHEFCD NENQTWHFTY NSTYHAYKIW SGRKSNLLLT
     WDSNATSKEM VVRAYTESRS KNQYWRIEQT GSKSYKLRNL ENSNMILGLT NVSTSYGGLN
     LMVQDDSNGN SNLHSDWDIK PIIYQYVPDG DYNIFNDNFP NIAVDYTNQE GALVHGHNFC
     SNNNQKWSFV YDGKKKAYKI KSGVNSKLWL TWDSNASSKE MVLRAYTESG NWNQYWRLYQ
     ANDGSYIIRN LKEFKMLIAL TNIDTPYGGK QLIVTDTKES GNHWYLKKLG EVPLPNRKFR
     IATKLNYKKV IDSSTAYNLI ITHDLNFASS IWELVYDSNK KAYNIYSADI NNLGWVYQNK
     NFFVKLDNID GPDHGDLRYF WTIEYSMQTG CYLIRSLYDP AHAVGYTDKD SVITDTSTYS
     DNQLFHFILM