ID   P34_SOYBN               Reviewed;         379 AA.
AC   P22895;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=P34 probable thiol protease;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 123-147.
RC   STRAIN=cv. Century; TISSUE=Seed;
RX   PubMed=2380191; DOI=10.1016/s0021-9258(18)77425-5;
RA   Kalinski A., Weisemann J.M., Matthews B.F., Herman E.M.;
RT   "Molecular cloning of a protein associated with soybean seed oil bodies
RT   that is similar to thiol proteases of the papain family.";
RL   J. Biol. Chem. 265:13843-13848(1990).
RN   [2]
RP   PROTEOLYTIC PROCESSING, AND SUBCELLULAR LOCATION.
RX   PubMed=1601876; DOI=10.1016/s0021-9258(19)49807-4;
RA   Kalinski A., Melroy D.L., Dwivedi R.S., Herman E.M.;
RT   "A soybean vacuolar protein (P34) related to thiol proteases is synthesized
RT   as a glycoprotein precursor during seed maturation.";
RL   J. Biol. Chem. 267:12068-12076(1992).
CC   -!- FUNCTION: Probable thiol protease.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:1601876}.
CC       Note=Protein storage vacuoles of seeds. This protein was wrongly
CC       thought to be associated with seed oil bodies.
CC   -!- PTM: N-glycosylated on its propeptide.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10090}.
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DR   EMBL; J05560; AAB09252.1; ALT_SEQ; mRNA.
DR   PIR; A37126; KHSYO4.
DR   RefSeq; NP_001238219.1; NM_001251290.1.
DR   AlphaFoldDB; P22895; -.
DR   SMR; P22895; -.
DR   STRING; 3847.GLYMA08G12270.1; -.
DR   Allergome; 1103; Gly m Bd30K.
DR   MEROPS; I29.003; -.
DR   PRIDE; P22895; -.
DR   GeneID; 548062; -.
DR   KEGG; gmx:548062; -.
DR   eggNOG; KOG1543; Eukaryota.
DR   OrthoDB; 1275401at2759; -.
DR   Proteomes; UP000008827; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR   CDD; cd02248; Peptidase_C1A; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025661; Pept_asp_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.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Protease; Reference proteome; Signal; Thiol protease; Vacuole; Zymogen.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..122
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:2380191"
FT                   /id="PRO_0000026471"
FT   CHAIN           123..379
FT                   /note="P34 probable thiol protease"
FT                   /id="PRO_0000026472"
FT   ACT_SITE        301
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT   ACT_SITE        321
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT   SITE            200
FT                   /note="Ancestral active site"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        292
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        190..230
FT                   /evidence="ECO:0000250"
FT   DISULFID        293..346
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   379 AA;  42794 MW;  CC63BA943F3B922D CRC64;
     MGFLVLLLFS LLGLSSSSSI STHRSILDLD LTKFTTQKQV SSLFQLWKSE HGRVYHNHEE
     EAKRLEIFKN NSNYIRDMNA NRKSPHSHRL GLNKFADITP QEFSKKYLQA PKDVSQQIKM
     ANKKMKKEQY SCDHPPASWD WRKKGVITQV KYQGGCGRGW AFSATGAIEA AHAIATGDLV
     SLSEQELVDC VEESEGSYNG WQYQSFEWVL EHGGIATDDD YPYRAKEGRC KANKIQDKVT
     IDGYETLIMS DESTESETEQ AFLSAILEQP ISVSIDAKDF HLYTGGIYDG ENCTSPYGIN
     HFVLLVGYGS ADGVDYWIAK NSWGFDWGED GYIWIQRNTG NLLGVCGMNY FASYPTKEES
     ETLVSARVKG HRRVDHSPL