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Serine protease inhibitor Kazal-type 1 (Cholecystokinin-releasing peptide) (Monitor peptide) (Pancreatic secretory trypsin inhibitor) (PSTI-I)

 ISK1_RAT                Reviewed;          79 AA.
P09655; P13072;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 2.
23-MAY-2018, entry version 144.
RecName: Full=Serine protease inhibitor Kazal-type 1 {ECO:0000312|RGD:3749};
AltName: Full=Cholecystokinin-releasing peptide {ECO:0000303|PubMed:2602119};
AltName: Full=Monitor peptide {ECO:0000303|PubMed:2602119};
AltName: Full=Pancreatic secretory trypsin inhibitor {ECO:0000303|PubMed:2751646};
Short=PSTI-I {ECO:0000303|PubMed:2751646};
Flags: Precursor;
Name=Spink1 {ECO:0000312|RGD:3749};
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 [MRNA].
TISSUE=Pancreas;
PubMed=2602119; DOI=10.1093/nar/17.23.10111;
Fukuoka S., Scheele G.A.;
"Complementary nucleotide sequence for monitor peptide, a novel
cholecystokinin-releasing peptide in the rat.";
Nucleic Acids Res. 17:10111-10111(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Pancreas;
PubMed=2293709;
Fukuoka S., Scheele G.A.;
"Rapid and selective cloning of monitor peptide, a novel
cholecystokinin-releasing peptide, using minimal amino acid sequence
and the polymerase chain reaction.";
Pancreas 5:1-7(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pancreas;
PubMed=2751646; DOI=10.1016/0006-291X(89)91975-X;
Horii A., Tomita N., Yokouchi H., Doi S., Uda K., Ogawa M., Mori T.,
Matsubara K.;
"On the cDNA's for two types of rat pancreatic secretory trypsin
inhibitor.";
Biochem. Biophys. Res. Commun. 162:151-159(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2065678; DOI=10.1111/j.1432-1033.1991.tb16116.x;
Tsuzuki S., Fushiki T., Kondo A., Murayama H., Sugimoto E.;
"Effect of a high-protein diet on the gene expression of a trypsin-
sensitive, cholecystokinin-releasing peptide (monitor peptide) in the
pancreas.";
Eur. J. Biochem. 199:245-252(1991).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1390891; DOI=10.1016/0167-4781(92)90012-O;
Tsuzuki S., Miura Y., Fushiki T., Oomori T., Satoh T., Natori Y.,
Sugimoto E.;
"Molecular cloning and characterization of genes encoding rat
pancreatic cholecystokinin (CCK)-releasing peptide (monitor peptide)
and pancreatic secretory trypsin inhibitor (PSTI).";
Biochim. Biophys. Acta 1132:199-202(1992).
[6]
PROTEIN SEQUENCE OF 19-79, AND FUNCTION.
STRAIN=Wistar; TISSUE=Pancreas;
PubMed=3202973;
Uda K., Ogawa M., Shibita T., Murata A., Mori T., Kikuchi N.,
Yoshida N., Tsunasawa S., Sakiyama F.;
"Purification, characterization and amino-acid sequencing of two
pancreatic secretory trypsin inhibitors in rat pancreatic juice.";
Biol. Chem. Hoppe-Seyler 369:55-61(1988).
[7]
PROTEIN SEQUENCE OF 19-79, FUNCTION, AND SUBCELLULAR LOCATION.
TISSUE=Pancreas;
PubMed=3597401;
Iwai K., Fukuoka S., Fushiki T., Tsujikawa M., Hirose M.,
Tsunasawa S., Sakiyama F.;
"Purification and sequencing of a trypsin-sensitive cholecystokinin-
releasing peptide from rat pancreatic juice. Its homology with
pancreatic secretory trypsin inhibitor.";
J. Biol. Chem. 262:8956-8959(1987).
-!- FUNCTION: Serine protease inhibitor which exhibits anti-trypsin
activity (PubMed:3202973, PubMed:3597401). In the pancreas,
protects against trypsin-catalyzed premature activation of
zymogens (By similarity). {ECO:0000250|UniProtKB:P09036,
ECO:0000269|PubMed:3202973, ECO:0000269|PubMed:3597401}.
-!- FUNCTION: In the male reproductive tract, binds to sperm heads
where it modulates sperm capacitance by inhibiting calcium uptake
and nitrogen oxide (NO) production (By similarity).
{ECO:0000250|UniProtKB:P09036}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3597401}.
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EMBL; X59696; CAA42217.1; -; mRNA.
EMBL; M22162; AAA41629.1; -; mRNA.
EMBL; M35299; AAA74479.1; -; mRNA.
EMBL; M35300; AAA41977.1; -; mRNA.
EMBL; M27882; AAA41975.1; -; mRNA.
EMBL; D11321; BAA01944.1; -; Genomic_DNA.
PIR; S09602; TIRT1.
RefSeq; NP_036806.1; NM_012674.2.
UniGene; Rn.1658; -.
UniGene; Rn.9767; -.
ProteinModelPortal; P09655; -.
SMR; P09655; -.
STRING; 10116.ENSRNOP00000018110; -.
iPTMnet; P09655; -.
PhosphoSitePlus; P09655; -.
PaxDb; P09655; -.
PRIDE; P09655; -.
Ensembl; ENSRNOT00000018110; ENSRNOP00000018110; ENSRNOG00000013464.
GeneID; 24833; -.
KEGG; rno:24833; -.
UCSC; RGD:3749; rat.
CTD; 24833; -.
RGD; 3749; Spink1.
eggNOG; ENOG410IP06; Eukaryota.
eggNOG; ENOG410ZBM0; LUCA.
GeneTree; ENSGT00530000064228; -.
HOGENOM; HOG000090244; -.
HOVERGEN; HBG006182; -.
InParanoid; P09655; -.
OMA; PICNREY; -.
OrthoDB; EOG091G14HG; -.
PhylomeDB; P09655; -.
PRO; PR:P09655; -.
Proteomes; UP000002494; Chromosome 18.
Bgee; ENSRNOG00000013464; -.
Genevisible; P09655; RN.
GO; GO:0001669; C:acrosomal vesicle; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:RGD.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEP:RGD.
GO; GO:1900004; P:negative regulation of serine-type endopeptidase activity; IDA:RGD.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:RGD.
GO; GO:0090187; P:positive regulation of pancreatic juice secretion; IDA:RGD.
GO; GO:0090277; P:positive regulation of peptide hormone secretion; IDA:RGD.
GO; GO:0060046; P:regulation of acrosome reaction; IBA:GO_Central.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
InterPro; IPR002350; Kazal_dom.
InterPro; IPR036058; Kazal_dom_sf.
Pfam; PF00050; Kazal_1; 1.
SMART; SM00280; KAZAL; 1.
SUPFAM; SSF100895; SSF100895; 1.
PROSITE; PS00282; KAZAL_1; 1.
PROSITE; PS51465; KAZAL_2; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Protease inhibitor; Reference proteome; Secreted;
Serine protease inhibitor; Signal.
SIGNAL 1 18 {ECO:0000269|PubMed:3202973,
ECO:0000269|PubMed:3597401}.
CHAIN 19 79 Serine protease inhibitor Kazal-type 1.
/FTId=PRO_0000016558.
DOMAIN 26 79 Kazal-like. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
SITE 41 42 Reactive bond for trypsin.
{ECO:0000250|UniProtKB:P09036}.
SITE 43 44 Necessary for sperm binding.
{ECO:0000250|UniProtKB:P09036}.
DISULFID 32 61 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 39 58 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 47 79 {ECO:0000255|PROSITE-ProRule:PRU00798}.
CONFLICT 78 78 T -> G (in Ref. 7; AA sequence).
{ECO:0000305}.
SEQUENCE 79 AA; 8528 MW; 5816D55DF7B57874 CRC64;
MKVAIIFLLS ALALLSLAGN PPAEVNGKTP NCPKQIMGCP RIYDPVCGTN GITYPSECSL
CFENRKFGTS IHIQRRGTC


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