ISK1_RAT
ID ISK1_RAT Reviewed; 79 AA.
AC P09655; P13072;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Serine protease inhibitor Kazal-type 1 {ECO:0000312|RGD:3749};
DE AltName: Full=Cholecystokinin-releasing peptide {ECO:0000303|PubMed:2602119};
DE AltName: Full=Monitor peptide {ECO:0000303|PubMed:2602119};
DE AltName: Full=Pancreatic secretory trypsin inhibitor {ECO:0000303|PubMed:2751646};
DE Short=PSTI-I {ECO:0000303|PubMed:2751646};
DE Flags: Precursor;
GN Name=Spink1 {ECO:0000312|RGD:3749};
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 [MRNA].
RC TISSUE=Pancreas;
RX PubMed=2602119; DOI=10.1093/nar/17.23.10111;
RA Fukuoka S., Scheele G.A.;
RT "Complementary nucleotide sequence for monitor peptide, a novel
RT cholecystokinin-releasing peptide in the rat.";
RL Nucleic Acids Res. 17:10111-10111(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Pancreas;
RX PubMed=2293709; DOI=10.1097/00006676-199001000-00001;
RA Fukuoka S., Scheele G.A.;
RT "Rapid and selective cloning of monitor peptide, a novel cholecystokinin-
RT releasing peptide, using minimal amino acid sequence and the polymerase
RT chain reaction.";
RL Pancreas 5:1-7(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RX PubMed=2751646; DOI=10.1016/0006-291x(89)91975-x;
RA Horii A., Tomita N., Yokouchi H., Doi S., Uda K., Ogawa M., Mori T.,
RA Matsubara K.;
RT "On the cDNA's for two types of rat pancreatic secretory trypsin
RT inhibitor.";
RL Biochem. Biophys. Res. Commun. 162:151-159(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2065678; DOI=10.1111/j.1432-1033.1991.tb16116.x;
RA Tsuzuki S., Fushiki T., Kondo A., Murayama H., Sugimoto E.;
RT "Effect of a high-protein diet on the gene expression of a trypsin-
RT sensitive, cholecystokinin-releasing peptide (monitor peptide) in the
RT pancreas.";
RL Eur. J. Biochem. 199:245-252(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1390891; DOI=10.1016/0167-4781(92)90012-o;
RA Tsuzuki S., Miura Y., Fushiki T., Oomori T., Satoh T., Natori Y.,
RA Sugimoto E.;
RT "Molecular cloning and characterization of genes encoding rat pancreatic
RT cholecystokinin (CCK)-releasing peptide (monitor peptide) and pancreatic
RT secretory trypsin inhibitor (PSTI).";
RL Biochim. Biophys. Acta 1132:199-202(1992).
RN [6]
RP PROTEIN SEQUENCE OF 19-79, AND FUNCTION.
RC STRAIN=Wistar; TISSUE=Pancreas;
RX PubMed=3202973;
RA Uda K., Ogawa M., Shibita T., Murata A., Mori T., Kikuchi N., Yoshida N.,
RA Tsunasawa S., Sakiyama F.;
RT "Purification, characterization and amino-acid sequencing of two pancreatic
RT secretory trypsin inhibitors in rat pancreatic juice.";
RL Biol. Chem. Hoppe-Seyler 369:55-61(1988).
RN [7]
RP PROTEIN SEQUENCE OF 19-79, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Pancreas;
RX PubMed=3597401; DOI=10.1016/s0021-9258(18)48028-3;
RA Iwai K., Fukuoka S., Fushiki T., Tsujikawa M., Hirose M., Tsunasawa S.,
RA Sakiyama F.;
RT "Purification and sequencing of a trypsin-sensitive cholecystokinin-
RT releasing peptide from rat pancreatic juice. Its homology with pancreatic
RT secretory trypsin inhibitor.";
RL J. Biol. Chem. 262:8956-8959(1987).
CC -!- FUNCTION: Serine protease inhibitor which exhibits anti-trypsin
CC activity (PubMed:3202973, PubMed:3597401). In the pancreas, protects
CC against trypsin-catalyzed premature activation of zymogens (By
CC similarity). {ECO:0000250|UniProtKB:P09036, ECO:0000269|PubMed:3202973,
CC ECO:0000269|PubMed:3597401}.
CC -!- FUNCTION: In the male reproductive tract, binds to sperm heads where it
CC modulates sperm capacitance by inhibiting calcium uptake and nitrogen
CC oxide (NO) production (By similarity). {ECO:0000250|UniProtKB:P09036}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3597401}.
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DR EMBL; X59696; CAA42217.1; -; mRNA.
DR EMBL; M22162; AAA41629.1; -; mRNA.
DR EMBL; M35299; AAA74479.1; -; mRNA.
DR EMBL; M35300; AAA41977.1; -; mRNA.
DR EMBL; M27882; AAA41975.1; -; mRNA.
DR EMBL; D11321; BAA01944.1; -; Genomic_DNA.
DR PIR; S09602; TIRT1.
DR RefSeq; NP_036806.1; NM_012674.2.
DR AlphaFoldDB; P09655; -.
DR SMR; P09655; -.
DR BioGRID; 246952; 1.
DR STRING; 10116.ENSRNOP00000018110; -.
DR iPTMnet; P09655; -.
DR PhosphoSitePlus; P09655; -.
DR PaxDb; P09655; -.
DR Ensembl; ENSRNOT00000095851; ENSRNOP00000095930; ENSRNOG00000068869.
DR GeneID; 24833; -.
DR KEGG; rno:24833; -.
DR UCSC; RGD:3749; rat.
DR CTD; 6690; -.
DR RGD; 3749; Spink1.
DR eggNOG; KOG3649; Eukaryota.
DR GeneTree; ENSGT00530000064228; -.
DR HOGENOM; CLU_169765_2_1_1; -.
DR InParanoid; P09655; -.
DR OMA; REDHTHI; -.
DR OrthoDB; 1591004at2759; -.
DR PhylomeDB; P09655; -.
DR PRO; PR:P09655; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000013464; Expressed in pancreas and 12 other tissues.
DR Genevisible; P09655; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0030414; F:peptidase inhibitor activity; ISO:RGD.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:RGD.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEP:RGD.
DR GO; GO:0090281; P:negative regulation of calcium ion import; ISO:RGD.
DR GO; GO:0010751; P:negative regulation of nitric oxide mediated signal transduction; ISO:RGD.
DR GO; GO:0010466; P:negative regulation of peptidase activity; ISO:RGD.
DR GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:1900004; P:negative regulation of serine-type endopeptidase activity; IDA:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:RGD.
DR GO; GO:0090187; P:positive regulation of pancreatic juice secretion; IDA:RGD.
DR GO; GO:0090277; P:positive regulation of peptide hormone secretion; IDA:RGD.
DR GO; GO:0060046; P:regulation of acrosome reaction; ISO:RGD.
DR GO; GO:2001256; P:regulation of store-operated calcium entry; ISO:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0048240; P:sperm capacitation; ISO:RGD.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR Pfam; PF00050; Kazal_1; 1.
DR SMART; SM00280; KAZAL; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR PROSITE; PS00282; KAZAL_1; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:3202973,
FT ECO:0000269|PubMed:3597401"
FT CHAIN 19..79
FT /note="Serine protease inhibitor Kazal-type 1"
FT /id="PRO_0000016558"
FT DOMAIN 26..79
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 41..42
FT /note="Reactive bond for trypsin"
FT /evidence="ECO:0000250|UniProtKB:P09036"
FT SITE 43..44
FT /note="Necessary for sperm binding"
FT /evidence="ECO:0000250|UniProtKB:P09036"
FT DISULFID 32..61
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 39..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 47..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT CONFLICT 78
FT /note="T -> G (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 79 AA; 8528 MW; 5816D55DF7B57874 CRC64;
MKVAIIFLLS ALALLSLAGN PPAEVNGKTP NCPKQIMGCP RIYDPVCGTN GITYPSECSL
CFENRKFGTS IHIQRRGTC
