ID   ASPR_CUCPE              Reviewed;         513 AA.
AC   O04057;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Aspartic proteinase;
DE            EC=3.4.23.-;
DE   Flags: Precursor;
OS   Cucurbita pepo (Vegetable marrow) (Summer squash).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX   NCBI_TaxID=3663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9210475; DOI=10.1111/j.1432-1033.1997.00133.x;
RA   Hiraiwa N., Kondo M., Nishimura M., Hara-Nishimura I.;
RT   "An aspartic endopeptidase is involved in the breakdown of propeptides of
RT   storage proteins in protein-storage vacuoles of plants.";
RL   Eur. J. Biochem. 246:133-141(1997).
CC   -!- FUNCTION: Involved in the breakdown of propeptides of storage proteins
CC       in protein-storage vacuoles. {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of a 32 kDa subunit and a 16 kDa subunit.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; AB002695; BAA19607.1; -; mRNA.
DR   PIR; T09739; T09739.
DR   AlphaFoldDB; O04057; -.
DR   SMR; O04057; -.
DR   MEROPS; A01.A02; -.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR007856; SapB_1.
DR   InterPro; IPR008138; SapB_2.
DR   InterPro; IPR011001; Saposin-like.
DR   InterPro; IPR008139; SaposinB_dom.
DR   PANTHER; PTHR47966; PTHR47966; 1.
DR   Pfam; PF00026; Asp; 1.
DR   Pfam; PF05184; SapB_1; 1.
DR   Pfam; PF03489; SapB_2; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF47862; SSF47862; 1.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
DR   PROSITE; PS50015; SAP_B; 2.
PE   2: Evidence at transcript level;
KW   Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Signal; Vacuole; Zymogen.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..72
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000025901"
FT   CHAIN           73..513
FT                   /note="Aspartic proteinase"
FT                   /id="PRO_0000025902"
FT   DOMAIN          90..510
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   DOMAIN          319..424
FT                   /note="Saposin B-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   ACT_SITE        108
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        294
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        143
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   CARBOHYD        404
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   DISULFID        120..126
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   DISULFID        285..289
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   DISULFID        324..418
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   DISULFID        349..390
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   DISULFID        355..387
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   DISULFID        432..469
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
SQ   SEQUENCE   513 AA;  55856 MW;  083FB7064CE02DC2 CRC64;
     MASYHSKAAF LCLFLLVSFN IVSSASNDGL LRVGLKKIKL DPENRLAARV ESKDAEILKA
     AFRKYNPKGN LGESSDTDIV ALKNYLDAQY YGEIAIGTPP QKFTVIFDTG SSNLWVLCEC
     LFSVACHFHA RYKSSRSSSY KKNGTSASIR YGTGAVSGFF SYDNVKVGDL VVKEQVFIEA
     TREPSLTFLV AKFDGLLGLG FQEIAVGNAV PVWYNMVEQG LVKEPVFSFW LNRNVEEEEG
     GEIVFGGVDP KHYRGKHTYV PVTQKGYWQF DMGDVLIDGE PTGFCDGGCS AIADSGTSLL
     AGPTPVITMI NHAIGAKGVV SQQCKAVVAQ YGQTIMDLLL SEADPKKICS QINLCTFDGT
     RGVSMGIESV VDENAGKSSD SLHDGMCSVC EMTVVWMQNQ LRQNQTKERI INYINELCDR
     MPSPMGQSAV DCGQLSSMPT VSFTIGGKIF DLAPEEYILK VGEGPVAQCI SGFTAFDIPP
     PRGPLWILGD VFMGRYHTVF DFGKLRVGSA EAA