CYSP_HEMSP
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 03-AUG-2022, entry version 84.
DE RecName: Full=Thiol protease SEN102;
DE EC=3.4.22.-;
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 PRIDE; P43156; -.
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 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; 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 Endoplasmic reticulum; Glycoprotein; Hydrolase; Protease; Signal;
KW Thiol protease; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..133
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
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:0000250"
FT ACT_SITE 289
FT /evidence="ECO:0000250"
FT ACT_SITE 310
FT /evidence="ECO:0000250"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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