CYT_OXYSC
ID CYT_OXYSC Reviewed; 141 AA.
AC E3P6N6;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=Cystatin;
DE Flags: Precursor;
OS Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Oxyuranus.
OX NCBI_TaxID=8667;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND LEVEL OF PROTEIN EXPRESSION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=21172403; DOI=10.1016/j.biochi.2010.12.008;
RA Richards R., St Pierre L., Trabi M., Johnson L.A., de Jersey J.,
RA Masci P.P., Lavin M.F.;
RT "Cloning and characterisation of novel cystatins from elapid snake venom
RT glands.";
RL Biochimie 93:659-668(2011).
CC -!- FUNCTION: Inhibits various C1 cysteine proteases including cathepsin L,
CC papain and cathepsin B. This protein has no toxic activity and its
CC function in the venom is unknown. It may play a role as a housekeeping
CC or regulatory protein (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed at a low level by the venom gland (at
CC protein level). {ECO:0000305|PubMed:21172403}.
CC -!- MISCELLANEOUS: The recombinant protein does not inhibit calpain-1
CC (CAPN1), a C2 family cysteine protease and legumain (LGMN), a C13
CC family cysteine protease. Does not provoke cell death (PC3 prostrate
CC cancer cells) (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cystatin family. {ECO:0000305}.
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DR EMBL; FJ411281; ACR83842.1; -; mRNA.
DR AlphaFoldDB; E3P6N6; -.
DR SMR; E3P6N6; -.
DR MEROPS; I25.012; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00042; CY; 1.
DR InterPro; IPR000010; Cystatin_dom.
DR InterPro; IPR046350; Cystatin_sf.
DR InterPro; IPR018073; Prot_inh_cystat_CS.
DR Pfam; PF00031; Cystatin; 1.
DR SMART; SM00043; CY; 1.
DR SUPFAM; SSF54403; SSF54403; 1.
DR PROSITE; PS00287; CYSTATIN; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Protease inhibitor; Secreted; Signal;
KW Thiol protease inhibitor.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT CHAIN 27..141
FT /note="Cystatin"
FT /id="PRO_5000654415"
FT DOMAIN 29..129
FT /note="Cystatin"
FT MOTIF 73..77
FT /note="Secondary area of contact"
FT /evidence="ECO:0000250"
FT SITE 29
FT /note="Reactive site"
FT /evidence="ECO:0000250"
FT DISULFID 91..107
FT /evidence="ECO:0000250"
FT DISULFID 120..140
FT /evidence="ECO:0000250"
SQ SEQUENCE 141 AA; 15849 MW; F0B152B576F1027A CRC64;
MVHSQLPVAA PLRLLCALLL LPSATMIPGG LSPRSVTDPD VQKAAEFAVQ EYNALSTNAY
YYKQLRIVEA QSQVVAGAKY YLTMELMKTK CAKTTGKPKV YKEIQNCELP PKAQQEKLTC
HFQVWSRPWL EKVELTKMSC N