ID   CYTS_RAT                Reviewed;         141 AA.
AC   P19313;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Cystatin-S;
DE   AltName: Full=Cystatin-1;
DE   AltName: Full=Protein LM;
DE   Flags: Precursor;
GN   Name=Cst4; Synonyms=Cyss;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1537554; DOI=10.1016/0378-1119(92)90645-6;
RA   Cox J.L., Shaw P.A.;
RT   "Structure, organization and regulation of a rat cysteine proteinase
RT   inhibitor-encoding gene.";
RL   Gene 110:175-180(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-141.
RC   STRAIN=Sprague-Dawley; TISSUE=Submandibular gland;
RX   PubMed=3263967; DOI=10.1016/s0021-9258(19)81334-0;
RA   Shaw P.A., Cox J.L., Barka T., Naito Y.;
RT   "Cloning and sequencing of cDNA encoding a rat salivary cysteine proteinase
RT   inhibitor inducible by beta-adrenergic agonists.";
RL   J. Biol. Chem. 263:18133-18137(1988).
RN   [3]
RP   PROTEIN SEQUENCE OF 28-132, AND DISULFIDE BONDS.
RC   TISSUE=Submandibular gland;
RX   PubMed=2757396; DOI=10.1016/0003-9861(89)90185-9;
RA   Bedi G.S.;
RT   "Amino acid sequence of an inducible cysteine proteinase inhibitor
RT   (cystatin) from submandibular glands of isoproterenol-treated rats.";
RL   Arch. Biochem. Biophys. 273:245-253(1989).
CC   -!- FUNCTION: This protein strongly inhibits papain and ficin, partially
CC       inhibits stem bromelain and bovine cathepsin C, but does not inhibit
CC       porcine cathepsin B or clostripain. Papain is inhibited non-
CC       competitively.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Found in saliva, tears, urine and seminal fluid.
CC   -!- SIMILARITY: Belongs to the cystatin family. {ECO:0000305}.
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DR   EMBL; M75281; AAA41068.1; -; Genomic_DNA.
DR   EMBL; J04206; AAB59703.1; -; mRNA.
DR   PIR; JQ1470; JQ1470.
DR   RefSeq; NP_941958.1; NM_198685.1.
DR   AlphaFoldDB; P19313; -.
DR   SMR; P19313; -.
DR   STRING; 10116.ENSRNOP00000044719; -.
DR   PaxDb; P19313; -.
DR   Ensembl; ENSRNOT00000044345; ENSRNOP00000044719; ENSRNOG00000030857.
DR   GeneID; 296234; -.
DR   KEGG; rno:296234; -.
DR   UCSC; RGD:735160; rat.
DR   CTD; 296234; -.
DR   RGD; 735160; Cyss.
DR   eggNOG; ENOG502SC50; Eukaryota.
DR   GeneTree; ENSGT00940000154755; -.
DR   HOGENOM; CLU_118168_0_1_1; -.
DR   InParanoid; P19313; -.
DR   OMA; AVNEYNE; -.
DR   OrthoDB; 1565344at2759; -.
DR   PhylomeDB; P19313; -.
DR   PRO; PR:P19313; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Genevisible; P19313; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0030141; C:secretory granule; IDA:RGD.
DR   GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:RGD.
DR   GO; GO:0002020; F:protease binding; IDA:RGD.
DR   GO; GO:0048468; P:cell development; IEP:RGD.
DR   GO; GO:0001906; P:cell killing; IDA:RGD.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:RGD.
DR   GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0010466; P:negative regulation of peptidase activity; IDA:RGD.
DR   GO; GO:0046677; P:response to antibiotic; IEP:RGD.
DR   GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR   GO; GO:0046687; P:response to chromate; IEP:RGD.
DR   GO; GO:0009725; P:response to hormone; IEP:RGD.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR   GO; GO:0001562; P:response to protozoan; IEP:RGD.
DR   GO; GO:0009611; P:response to wounding; IEP:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR   GO; GO:0007431; P:salivary gland development; IEP:RGD.
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   Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW   Reference proteome; Secreted; Signal; Thiol protease inhibitor.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:2757396"
FT   CHAIN           28..141
FT                   /note="Cystatin-S"
FT                   /id="PRO_0000006651"
FT   MOTIF           76..80
FT                   /note="Secondary area of contact"
FT   SITE            32
FT                   /note="Reactive site"
FT   DISULFID        94..104
FT                   /evidence="ECO:0000269|PubMed:2757396"
FT   DISULFID        118..138
FT                   /evidence="ECO:0000269|PubMed:2757396"
FT   CONFLICT        114..115
FT                   /note="EH -> QE (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   141 AA;  15949 MW;  D7632905541C8266 CRC64;
     MAYLLHAQLF LLTTFILVLN MRLCPVLGHF LGGIEKSSME EEGASEALNY AVNEYNEKNS
     DLYLSRVVEV KDVQKQVVAG TKFFFDVILG KTICLKTQGD LTNCPLNEEA DQQEHEFCSF
     VVHDIPWENY IVLLSSSCHS I