PAPA4_CARPA
ID PAPA4_CARPA Reviewed; 348 AA.
AC P05994;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 3.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Papaya proteinase 4;
DE EC=3.4.22.25;
DE AltName: Full=Glycyl endopeptidase;
DE AltName: Full=Papaya peptidase B;
DE AltName: Full=Papaya proteinase IV;
DE Short=PPIV;
DE Flags: Precursor;
OS Carica papaya (Papaya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Caricaceae; Carica.
OX NCBI_TaxID=3649;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=7770454; DOI=10.1093/protein/8.1.59;
RA Taylor M.A., Baker K.C., Briggs G.S., Connerton I.F., Cummings N.J.,
RA Pratt K.A., Revell D.F., Freedman R.B., Goodenough P.W.;
RT "Recombinant pro-regions from papain and papaya proteinase IV-are selective
RT high affinity inhibitors of the mature papaya enzymes.";
RL Protein Eng. 8:59-62(1995).
RN [2]
RP PROTEIN SEQUENCE OF 133-348.
RX PubMed=2591528; DOI=10.1016/0014-5793(89)81627-8;
RA Ritonja A., Buttle D.J., Rawlings N.D., Turk V., Barrett A.J.;
RT "Papaya proteinase IV amino acid sequence.";
RL FEBS Lett. 258:109-112(1989).
RN [3]
RP PROTEIN SEQUENCE OF 133-150.
RX PubMed=518921; DOI=10.1016/0005-2795(79)90257-5;
RA Lynn K.R., Yaguchi M.;
RT "N-terminal homology in three cysteinyl proteases from Papaya latex.";
RL Biochim. Biophys. Acta 581:363-364(1979).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 287-348.
RX PubMed=3541893; DOI=10.1042/bj2370105;
RA McKee R.A., Adams S., Matthews J.A., Smith C.J., Smith H.;
RT "Molecular cloning of two cysteine proteinases from paw-paw (Carica
RT papaya).";
RL Biochem. J. 237:105-110(1986).
RN [5]
RP SUBSTRATE SPECIFICITY.
RX PubMed=2404797; DOI=10.1016/0014-5793(90)80101-n;
RA Buttle D.J., Ritonja A., Pearl L.H., Turk V., Barrett A.J.;
RT "Selective cleavage of glycyl bonds by papaya proteinase IV.";
RL FEBS Lett. 260:195-197(1990).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=7548082; DOI=10.1021/bi00040a034;
RA O'Hara B.P., Hemmings A.M., Buttle D.J., Pearl L.H.;
RT "Crystal structure of glycyl endopeptidase from Carica papaya: a cysteine
RT endopeptidase of unusual substrate specificity.";
RL Biochemistry 34:13190-13195(1995).
CC -!- FUNCTION: Thiol protease with a substrate specificity very different
CC from the other thiol proteases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Gly-|-Xaa, in proteins and in small
CC molecule substrates.; EC=3.4.22.25;
CC -!- ACTIVITY REGULATION: Not inhibited by cystatin.
CC -!- MISCELLANEOUS: Substitution of the conserved Gly residue by Glu-155
CC could possibly explain the unusual specificity.
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; X78056; CAA54974.1; -; mRNA.
DR EMBL; X03970; CAA27608.1; -; mRNA.
DR PIR; S06837; S06837.
DR PIR; T09798; T09798.
DR PDB; 1GEC; X-ray; 2.10 A; E=133-348.
DR PDBsum; 1GEC; -.
DR AlphaFoldDB; P05994; -.
DR SMR; P05994; -.
DR Allergome; 1539; Cari p Endoproteinase.
DR MEROPS; C01.004; -.
DR MEROPS; I29.003; -.
DR KEGG; ag:CAA54974; -.
DR BRENDA; 3.4.22.25; 1191.
DR SABIO-RK; P05994; -.
DR EvolutionaryTrace; P05994; -.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Protease; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..132
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:2591528,
FT ECO:0000269|PubMed:518921"
FT /id="PRO_0000026412"
FT CHAIN 133..348
FT /note="Papaya proteinase 4"
FT /id="PRO_0000026413"
FT ACT_SITE 157
FT /evidence="ECO:0000250"
FT ACT_SITE 291
FT /evidence="ECO:0000250"
FT ACT_SITE 311
FT /evidence="ECO:0000250"
FT DISULFID 154..195
FT DISULFID 188..227
FT DISULFID 285..336
FT CONFLICT 190
FT /note="K -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 139..143
FT /evidence="ECO:0007829|PDB:1GEC"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:1GEC"
FT HELIX 157..174
FT /evidence="ECO:0007829|PDB:1GEC"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:1GEC"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:1GEC"
FT HELIX 200..210
FT /evidence="ECO:0007829|PDB:1GEC"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:1GEC"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:1GEC"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:1GEC"
FT HELIX 250..257
FT /evidence="ECO:0007829|PDB:1GEC"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:1GEC"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:1GEC"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:1GEC"
FT STRAND 291..301
FT /evidence="ECO:0007829|PDB:1GEC"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:1GEC"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:1GEC"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:1GEC"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:1GEC"
SQ SEQUENCE 348 AA; 39024 MW; 40855EDD37F68A8E CRC64;
MAIICSFSKL LFVAICLFGH MSLSYCDFSI VGYSQDDLTS TERLIQLFNS WMLKHNKNYK
NVDEKLYRFE IFKDNLKYID ERNKMINGYW LGLNEFSDLS NDEFKEKYVG SLPEDYTNQP
YDEEFVNEDI VDLPESVDWR AKGAVTPVKH QGYCESCWAF STVATVEGIN KIKTGNLVEL
SEQELVDCDK QSYGCNRGYQ STSLQYVAQN GIHLRAKYPY IAKQQTCRAN QVGGPKVKTN
GVGRVQSNNE GSLLNAIAHQ PVSVVVESAG RDFQNYKGGI FEGSCGTKVD HAVTAVGYGK
SGGKGYILIK NSWGPGWGEN GYIRIRRASG NSPGVCGVYR SSYYPIKN
