LSPI_CARPA
ID LSPI_CARPA Reviewed; 184 AA.
AC P80691;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Latex serine proteinase inhibitor;
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 PROTEIN SEQUENCE.
RC TISSUE=Latex;
RX PubMed=8898891; DOI=10.1111/j.1432-1033.1996.0077t.x;
RA Odani S., Yokokawa Y., Takeda H., Abe S., Odani S.;
RT "The primary structure and characterization of carbohydrate chains of the
RT extracellular glycoprotein proteinase inhibitor from latex of Carica
RT papaya.";
RL Eur. J. Biochem. 241:77-82(1996).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC type inhibitor) family. {ECO:0000305}.
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DR PIR; S74136; S74136.
DR PDB; 3S8J; X-ray; 2.60 A; A/B=1-184.
DR PDB; 3S8K; X-ray; 1.70 A; A/B=1-184.
DR PDBsum; 3S8J; -.
DR PDBsum; 3S8K; -.
DR AlphaFoldDB; P80691; -.
DR SMR; P80691; -.
DR MEROPS; I03.022; -.
DR EvolutionaryTrace; P80691; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00178; STI; 1.
DR InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR InterPro; IPR002160; Prot_inh_Kunz-lg.
DR PANTHER; PTHR33107; PTHR33107; 1.
DR Pfam; PF00197; Kunitz_legume; 1.
DR PRINTS; PR00291; KUNITZINHBTR.
DR SMART; SM00452; STI; 1.
DR SUPFAM; SSF50386; SSF50386; 1.
DR PROSITE; PS00283; SOYBEAN_KUNITZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Protease inhibitor; Secreted; Serine protease inhibitor.
FT CHAIN 1..184
FT /note="Latex serine proteinase inhibitor"
FT /id="PRO_0000083323"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 45..89
FT DISULFID 142..153
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:3S8K"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:3S8K"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:3S8K"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:3S8K"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:3S8K"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:3S8J"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:3S8K"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:3S8K"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:3S8K"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:3S8K"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:3S8K"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:3S8K"
FT HELIX 119..124
FT /evidence="ECO:0007829|PDB:3S8K"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:3S8K"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:3S8K"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:3S8K"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:3S8K"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:3S8K"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:3S8K"
SQ SEQUENCE 184 AA; 20646 MW; FCC609D0385E96AA CRC64;
VAPKPIVDID GKPVLYGVDY FVVSAIWGAG GGGLTVYGPG NKKKCPLSVV QDPFDNGEPI
IFSAIKNVKD NIVFESVDLN VKFNITINCN ETTAWKVDRF PGVIGWTVTL GGEKGYHGFE
STHSMFKIKK AGLPFSYKFH FCPSYPRTRL IPCNNVDIFF DKYRIRRLIL TNDAKEFVFI
KTNR
