ID   ISK1_BOVIN              Reviewed;          79 AA.
AC   P00996; Q56K02;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Serine protease inhibitor Kazal-type 1 {ECO:0000250|UniProtKB:P09036};
DE   AltName: Full=Pancreatic secretory trypsin inhibitor {ECO:0000303|PubMed:5769997};
DE   Flags: Precursor;
GN   Name=SPINK1; Synonyms=PSTI;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lymphoid epithelium;
RA   Yu J., Meng Y., Wang Z., Hansen C., Li C., Moore S.S.;
RT   "Analysis of sequences obtained from constructed full-length bovine cDNA
RT   libraries.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 24-79.
RX   PubMed=5769997; DOI=10.1016/s0021-9258(18)83448-2;
RA   Greene L.J., Bartelt D.C.;
RT   "The structure of the bovine pancreatic scretory trypsin inhibitor
RT   -- Kazal's inhibitor. II. The order of the tryptic peptides.";
RL   J. Biol. Chem. 244:2646-2657(1969).
RN   [4]
RP   DISULFIDE BONDS.
RX   PubMed=5135319; DOI=10.1016/s0021-9258(19)45837-7;
RA   Guy O., Shapanka R., Greene L.J.;
RT   "The structure of the bovine pancreatic secretory trypsin inhibitor
RT   -- Kazal's inhibitor. 3. Determination of the disulfide bonds and
RT   proteolysis by thermolysin.";
RL   J. Biol. Chem. 246:7740-7747(1971).
CC   -!- FUNCTION: Serine protease inhibitor which exhibits anti-trypsin
CC       activity. In the pancreas, protects against trypsin-catalyzed premature
CC       activation of zymogens. {ECO:0000250|UniProtKB:P09036}.
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. {ECO:0000250|UniProtKB:P09036}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P09036}.
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DR   EMBL; AY911325; AAW82093.1; -; mRNA.
DR   EMBL; BC102485; AAI02486.1; -; mRNA.
DR   PIR; A01230; TIBOA.
DR   RefSeq; NP_001020519.1; NM_001025348.1.
DR   AlphaFoldDB; P00996; -.
DR   SMR; P00996; -.
DR   STRING; 9913.ENSBTAP00000020673; -.
DR   MEROPS; I01.011; -.
DR   PaxDb; P00996; -.
DR   Ensembl; ENSBTAT00000020673; ENSBTAP00000020673; ENSBTAG00000015558.
DR   GeneID; 574092; -.
DR   KEGG; bta:574092; -.
DR   CTD; 6690; -.
DR   VEuPathDB; HostDB:ENSBTAG00000015558; -.
DR   VGNC; VGNC:35219; SPINK1.
DR   eggNOG; KOG3649; Eukaryota.
DR   GeneTree; ENSGT00530000064228; -.
DR   HOGENOM; CLU_169765_2_1_1; -.
DR   InParanoid; P00996; -.
DR   OMA; EPSCENF; -.
DR   OrthoDB; 1591004at2759; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0090281; P:negative regulation of calcium ion import; IEA:Ensembl.
DR   GO; GO:0010751; P:negative regulation of nitric oxide mediated signal transduction; IEA:Ensembl.
DR   GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:1900004; P:negative regulation of serine-type endopeptidase activity; IEA:Ensembl.
DR   GO; GO:0007263; P:nitric oxide mediated signal transduction; IEA:Ensembl.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0060046; P:regulation of acrosome reaction; IEA:Ensembl.
DR   GO; GO:2001256; P:regulation of store-operated calcium entry; IEA:Ensembl.
DR   GO; GO:0048240; P:sperm capacitation; IEA:Ensembl.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   InterPro; IPR001239; Prot_inh_Kazal-m.
DR   Pfam; PF00050; Kazal_1; 1.
DR   PRINTS; PR00290; KAZALINHBTR.
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..23
FT                   /evidence="ECO:0000269|PubMed:5769997"
FT   CHAIN           24..79
FT                   /note="Serine protease inhibitor Kazal-type 1"
FT                   /id="PRO_0000073023"
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                   ECO:0000255|PROSITE-ProRule:PRU00798"
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                   ECO:0000269|PubMed:5135319"
FT   DISULFID        39..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798,
FT                   ECO:0000269|PubMed:5135319"
FT   DISULFID        47..79
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798,
FT                   ECO:0000269|PubMed:5135319"
SQ   SEQUENCE   79 AA;  8467 MW;  869E94453EB24053 CRC64;
     MKVASIFLLT ALVLMSLSGN SGANILGREA KCTNEVNGCP RIYNPVCGTD GVTYSNECLL
     CMENKERQTP VLIQKSGPC