CYT1_CROAD
ID CYT1_CROAD Reviewed; 139 AA.
AC J3RYX9;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 25-MAY-2022, entry version 20.
DE RecName: Full=Cystatin-1;
DE Flags: Precursor;
OS Crotalus adamanteus (Eastern diamondback rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8729;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=23025625; DOI=10.1186/1471-2164-13-312;
RA Rokyta D.R., Lemmon A.R., Margres M.J., Aronow K.;
RT "The venom-gland transcriptome of the eastern diamondback rattlesnake
RT (Crotalus adamanteus).";
RL BMC Genomics 13:312-312(2012).
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 housekeeping or
CC regulatory protein (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the cystatin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JU174278; AFJ49804.1; -; mRNA.
DR AlphaFoldDB; J3RYX9; -.
DR SMR; J3RYX9; -.
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 2: Evidence at transcript level;
KW Disulfide bond; Protease inhibitor; Secreted; Signal;
KW Thiol protease inhibitor.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..139
FT /note="Cystatin-1"
FT /id="PRO_0000423038"
FT DOMAIN 27..127
FT /note="Cystatin"
FT MOTIF 71..75
FT /note="Secondary area of contact"
FT /evidence="ECO:0000250"
FT SITE 27
FT /note="Reactive site"
FT /evidence="ECO:0000250"
FT DISULFID 89..105
FT /evidence="ECO:0000250"
FT DISULFID 118..138
FT /evidence="ECO:0000250"
SQ SEQUENCE 139 AA; 15623 MW; 21ADDAB04F1FBC46 CRC64;
MHSRLPVPAS LCLLLLLPSV LPASMPGGLS PRDVTDPEVQ EAAVFAVEEY NARSTNSNYF
KALRLVQAES QVVSGAKYYL TMELVKTSCR KTNGNPKGYQ EIQNCRLPPR NQQEKLTCHF
EVWSRPWLNK TLLTKVTCN