ID   BROM2_ANACO             Reviewed;         212 AA.
AC   P14518;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Stem bromelain;
DE            EC=3.4.22.32;
OS   Ananas comosus (Pineapple) (Ananas ananas).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Bromeliaceae;
OC   Bromelioideae; Ananas.
OX   NCBI_TaxID=4615;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=2714443; DOI=10.1016/0014-5793(89)81383-3;
RA   Ritonja A., Rowan A.D., Buttle D.J., Rawlings N.D., Turk V., Barrett A.J.;
RT   "Stem bromelain: amino acid sequence and implications for weak binding of
RT   cystatin.";
RL   FEBS Lett. 247:419-424(1989).
RN   [2]
RP   STRUCTURE OF CARBOHYDRATE.
RA   van Kuik J.A., Hoffmann R.A., Mutsaers J.H.G.M., van Halbeek H.,
RA   Kamerling J.P., Vliegenthart J.F.G.;
RT   "A 500-MHz 1H-NMR study on the N-linked carbohydrate chain of bromelain.
RT   1H-NMR structural-reporter-groups of fucose alpha(1-3)-linked to
RT   asparagine-bound N-acetylglucosamine.";
RL   Glycoconj. J. 3:27-34(1986).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Broad specificity for cleavage of proteins, but strong
CC         preference for Z-Arg-Arg-|-NHMec among small molecule substrates.;
CC         EC=3.4.22.32;
CC   -!- MISCELLANEOUS: The geometry and the reactivity of the catalytic site
CC       are different from those of other cysteine proteinases.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089}.
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DR   PIR; S03964; S03964.
DR   AlphaFoldDB; P14518; -.
DR   SMR; P14518; -.
DR   Allergome; 3076; Ana c 2.0101.
DR   MEROPS; C01.005; -.
DR   GlyConnect; 75; 2 N-Linked glycans (1 site).
DR   BRENDA; 3.4.22.32; 333.
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; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Protease; Thiol protease.
FT   CHAIN           1..212
FT                   /note="Stem bromelain"
FT                   /id="PRO_0000050555"
FT   ACT_SITE        26
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        158
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /id="CAR_000134"
FT   DISULFID        23..63
FT                   /evidence="ECO:0000250"
FT   DISULFID        57..96
FT                   /evidence="ECO:0000250"
FT   DISULFID        152..199
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   212 AA;  22831 MW;  94EBADB72AAFA556 CRC64;
     AVPQSIDWRD YGAVTSVKNQ NPCGACWAFA AIATVESIYK IKKGILEPLS EQQVLDCAKG
     YGCKGGWEFR AFEFIISNKG VASGAIYPYK AAKGTCKTDG VPNSAYITGY ARVPRNNESS
     MMYAVSKQPI TVAVDANANF QYYKSGVFNG PCGTSLNHAV TAIGYGQDSI IYPKKWGAKW
     GEAGYIRMAR DVSSSSGICG IAIDPLYPTL EE