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Cystatin-S (Cystatin-1) (Protein LM)

 CYTS_RAT                Reviewed;         141 AA.
P19313;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
25-OCT-2017, entry version 136.
RecName: Full=Cystatin-S;
AltName: Full=Cystatin-1;
AltName: Full=Protein LM;
Flags: Precursor;
Name=Cst4; Synonyms=Cyss;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1537554; DOI=10.1016/0378-1119(92)90645-6;
Cox J.L., Shaw P.A.;
"Structure, organization and regulation of a rat cysteine proteinase
inhibitor-encoding gene.";
Gene 110:175-180(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 10-141.
STRAIN=Sprague-Dawley; TISSUE=Submandibular gland;
PubMed=3263967;
Shaw P.A., Cox J.L., Barka T., Naito Y.;
"Cloning and sequencing of cDNA encoding a rat salivary cysteine
proteinase inhibitor inducible by beta-adrenergic agonists.";
J. Biol. Chem. 263:18133-18137(1988).
[3]
PROTEIN SEQUENCE OF 28-132, AND DISULFIDE BONDS.
TISSUE=Submandibular gland;
PubMed=2757396; DOI=10.1016/0003-9861(89)90185-9;
Bedi G.S.;
"Amino acid sequence of an inducible cysteine proteinase inhibitor
(cystatin) from submandibular glands of isoproterenol-treated rats.";
Arch. Biochem. Biophys. 273:245-253(1989).
-!- FUNCTION: This protein strongly inhibits papain and ficin,
partially inhibits stem bromelain and bovine cathepsin C, but does
not inhibit porcine cathepsin B or clostripain. Papain is
inhibited non-competitively.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Found in saliva, tears, urine and seminal
fluid.
-!- SIMILARITY: Belongs to the cystatin family. {ECO:0000305}.
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EMBL; M75281; AAA41068.1; -; Genomic_DNA.
EMBL; J04206; AAB59703.1; -; mRNA.
PIR; JQ1470; JQ1470.
RefSeq; NP_941958.1; NM_198685.1.
UniGene; Rn.214033; -.
ProteinModelPortal; P19313; -.
SMR; P19313; -.
STRING; 10116.ENSRNOP00000044719; -.
PaxDb; P19313; -.
PRIDE; P19313; -.
Ensembl; ENSRNOT00000044345; ENSRNOP00000044719; ENSRNOG00000030857.
GeneID; 296234; -.
KEGG; rno:296234; -.
UCSC; RGD:735160; rat.
CTD; 296234; -.
RGD; 735160; Cyss.
eggNOG; ENOG410IZZH; Eukaryota.
eggNOG; ENOG4112CFJ; LUCA.
GeneTree; ENSGT00900000140934; -.
HOGENOM; HOG000231754; -.
HOVERGEN; HBG009556; -.
InParanoid; P19313; -.
OrthoDB; EOG091G0TP1; -.
PhylomeDB; P19313; -.
PRO; PR:P19313; -.
Proteomes; UP000002494; Chromosome 3.
Genevisible; P19313; RN.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0030141; C:secretory granule; IDA:RGD.
GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:RGD.
GO; GO:0002020; F:protease binding; IDA:RGD.
GO; GO:0048468; P:cell development; IEP:RGD.
GO; GO:0001906; P:cell killing; IDA:RGD.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:RGD.
GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0010466; P:negative regulation of peptidase activity; IDA:RGD.
GO; GO:0046677; P:response to antibiotic; IEP:RGD.
GO; GO:0048678; P:response to axon injury; IEP:RGD.
GO; GO:0046687; P:response to chromate; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0009725; P:response to hormone; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0001562; P:response to protozoan; IEP:RGD.
GO; GO:0009611; P:response to wounding; IEP:RGD.
GO; GO:0007431; P:salivary gland development; IEP:RGD.
CDD; cd00042; CY; 1.
InterPro; IPR027214; Cystatin.
InterPro; IPR000010; Cystatin_dom.
InterPro; IPR018073; Prot_inh_cystat_CS.
PANTHER; PTHR11413; PTHR11413; 1.
Pfam; PF00031; Cystatin; 1.
SMART; SM00043; CY; 1.
PROSITE; PS00287; CYSTATIN; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Protease inhibitor; Reference proteome; Secreted; Signal;
Thiol protease inhibitor.
SIGNAL 1 27 {ECO:0000269|PubMed:2757396}.
CHAIN 28 141 Cystatin-S.
/FTId=PRO_0000006651.
MOTIF 76 80 Secondary area of contact.
SITE 32 32 Reactive site.
DISULFID 94 104 {ECO:0000269|PubMed:2757396}.
DISULFID 118 138 {ECO:0000269|PubMed:2757396}.
CONFLICT 114 115 EH -> QE (in Ref. 3; AA sequence).
{ECO:0000305}.
SEQUENCE 141 AA; 15949 MW; D7632905541C8266 CRC64;
MAYLLHAQLF LLTTFILVLN MRLCPVLGHF LGGIEKSSME EEGASEALNY AVNEYNEKNS
DLYLSRVVEV KDVQKQVVAG TKFFFDVILG KTICLKTQGD LTNCPLNEEA DQQEHEFCSF
VVHDIPWENY IVLLSSSCHS I


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