ID   CYSP_HEMSP              Reviewed;         360 AA.
AC   P43156;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Thiol protease SEN102;
DE            EC=3.4.22.- {ECO:0000250|UniProtKB:P80884};
DE   Flags: Precursor;
GN   Name=SEN102;
OS   Hemerocallis sp. (Daylily).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Asphodelaceae;
OC   Hemerocallidoideae; Hemerocallis.
OX   NCBI_TaxID=29711;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Craddle Song; TISSUE=Petal;
RX   PubMed=7632925; DOI=10.1007/bf00020403;
RA   Valpuesta V., Lange N., Guerrero C., Reid M.;
RT   "Up-regulation of a cysteine protease accompanies the ethylene-insensitive
RT   senescence of daylily (Hemerocallis) flowers.";
RL   Plant Mol. Biol. 28:575-582(1995).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC       ProRule:PRU10138}.
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; X74406; CAA52425.1; -; mRNA.
DR   PIR; S57777; S57777.
DR   AlphaFoldDB; P43156; -.
DR   SMR; P43156; -.
DR   MEROPS; C01.168; -.
DR   MEROPS; I29.003; -.
DR   GlyCosmos; P43156; 1 site, No reported glycans.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
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   Gene3D; 3.90.70.10; Cysteine proteinases; 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; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR   PANTHER; PTHR12411:SF1001; KDEL-TAILED CYSTEINE ENDOPEPTIDASE CEP1; 1.
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; Cysteine proteinases; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase; Protease;
KW   Signal; Thiol protease; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..133
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:P00785"
FT                   /id="PRO_0000026449"
FT   CHAIN           134..360
FT                   /note="Thiol protease SEN102"
FT                   /id="PRO_0000026450"
FT   MOTIF           357..360
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   ACT_SITE        154
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT   ACT_SITE        289
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT   ACT_SITE        310
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT   CARBOHYD        353
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        151..193
FT                   /evidence="ECO:0000250|UniProtKB:P07858"
FT   DISULFID        185..225
FT                   /evidence="ECO:0000250|UniProtKB:P25250"
FT   DISULFID        283..335
FT                   /evidence="ECO:0000250|UniProtKB:P25250"
SQ   SEQUENCE   360 AA;  39915 MW;  808A3D252D2A2C63 CRC64;
     MAKPKFIALA LVALSFLSIA QSIPFTEKDL ASEDSLWNLY EKWRTHHTVA RDLDEKNRRF
     NVFKENVKFI HEFNQKKDAP YKLALNKFGD MTNQEFRSKY AGSKIQHHRS QRGIQKNTGS
     FMYENVGSLP AASIDWRAKG AVTGVKDQGQ CGSCWAFSTI ASVEGINQIK TGELVSLSEQ
     ELVDCDTSYN EGCNGGLMDY AFEFIQKNGI TTEDSYPYAE QDGTCASNLL NSPVVSIDGH
     QDVPANNENA LMQAVANQPI SVSIEASGYG FQFYSEGVFT GRCGTELDHG VAIVGYGATR
     DGTKYWIVKN SWGEEWGESG YIRMQRGISD KRGKCGIAME ASYPIKTSAN PKNSSTRDEL
//