ID   CYT_CHIGU               Reviewed;         134 AA.
AC   B1P1J3;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Cystatin-1;
DE   AltName: Full=Cystatin JZTX-75 {ECO:0000303|PubMed:18581053};
DE   Flags: Precursor;
OS   Chilobrachys guangxiensis (Chinese earth tiger tarantula) (Chilobrachys
OS   jingzhao).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Theraphosidae; Chilobrachys.
OX   NCBI_TaxID=278060;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=18581053; DOI=10.1007/s00018-008-8135-x;
RA   Chen J., Deng M., He Q., Meng E., Jiang L., Liao Z., Rong M., Liang S.;
RT   "Molecular diversity and evolution of cystine knot toxins of the tarantula
RT   Chilobrachys jingzhao.";
RL   Cell. Mol. Life Sci. 65:2431-2444(2008).
CC   -!- FUNCTION: Inhibits various C1 cysteine proteases. This protein has no
CC       toxic activity and its function in the venom is unknown. It may play a
CC       role as a housekeeping or regulatory protein (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cystatin family. {ECO:0000305}.
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DR   EMBL; EU233924; ABY71743.1; -; mRNA.
DR   AlphaFoldDB; B1P1J3; -.
DR   SMR; B1P1J3; -.
DR   MEROPS; I25.043; -.
DR   PRIDE; B1P1J3; -.
DR   ArachnoServer; AS001996; Cystatin-1-Chilobrachys guangxiensis.
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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..134
FT                   /note="Cystatin-1"
FT                   /id="PRO_0000423036"
FT   DOMAIN          21..116
FT                   /note="Cystatin"
FT   MOTIF           65..69
FT                   /note="Secondary area of contact"
FT                   /evidence="ECO:0000250"
FT   SITE            21
FT                   /note="Reactive site"
FT                   /evidence="ECO:0000250"
FT   DISULFID        83..96
FT                   /evidence="ECO:0000250"
FT   DISULFID        107..127
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   134 AA;  14879 MW;  8F092B71CEC4362D CRC64;
     MKAIYLILTV LCGFSASTKT GGWRDKDVDD EDIRKFATLA ASENSKMSNS LYFEKLVKVI
     EAKSQVVSGV KYNITFEIAP TECKKNGKGY DKLSECPLLE SAPHQTCTAI IWTRSWLNDT
     QILKLKCKEG GSSC