ISK1_PIG
ID ISK1_PIG Reviewed; 56 AA.
AC P00998;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Serine protease inhibitor Kazal-type 1 {ECO:0000250|UniProtKB:P09036};
DE AltName: Full=Pancreatic secretory trypsin inhibitor {ECO:0000303|PubMed:5466061};
GN Name=SPINK1; Synonyms=PSTI;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=5466061; DOI=10.1111/j.1432-1033.1970.tb01071.x;
RA Tschesche H., Wachter E.;
RT "The structure of the porcine pancreatic secretory trypsin inhibitor. I. A
RT sequence determination by Edman degradation and mass spectral
RT identification of the p-bromophenyl-thiohydantoins.";
RL Eur. J. Biochem. 16:187-198(1970).
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=5103069; DOI=10.1016/s0021-9258(19)77211-1;
RA Bartelt D.C., Greene L.J.;
RT "The primary structure of the porcine pancreatic secretory trypsin
RT inhibitor. I. Amino acid sequence of the reduced S-aminoethylated
RT protein.";
RL J. Biol. Chem. 246:2218-2229(1971).
RN [3]
RP DISULFIDE BONDS.
RX PubMed=4672150;
RA Tschesche H., Schneider M., Reidel G., Klein H.;
RT "Disulfide bridges of the secretory trypsin inhibitor from procine pancreas
RT and the degradation of covalent structure during the temporary
RT inhibition.";
RL Hoppe-Seyler's Z. Physiol. Chem. 353:763-764(1972).
RN [4]
RP PROTEIN SEQUENCE OF A SECOND INHIBITOR.
RX PubMed=5531651;
RA Tschesche H., Wachter E.;
RT "Trypsin inhibitors. VII. Primary structure of the specific trypsin
RT inhibitor II (Kazal-type) from porcine pancreas. Sequence analysis with
RT mass spectrometry identification of the p-bromophenylthio-hydantoins from
RT the Edman degradation.";
RL Hoppe-Seyler's Z. Physiol. Chem. 351:1449-1459(1970).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=7169635; DOI=10.1016/0022-2836(82)90550-2;
RA Bolognesi M., Gatti G., Menegatti E., Guarneri M., Marquart M.,
RA Papamokos E., Huber R.;
RT "Three-dimensional structure of the complex between pancreatic secretory
RT trypsin inhibitor (Kazal type) and trypsinogen at 1.8-A resolution.
RT Structure solution, crystallographic refinement and preliminary structural
RT interpretation.";
RL J. Mol. Biol. 162:839-868(1982).
CC -!- FUNCTION: Serine protease inhibitor which exhibits anti-trypsin
CC activity (PubMed:5466061). In the pancreas, protects against trypsin-
CC catalyzed premature activation of zymogens (By similarity).
CC {ECO:0000250|UniProtKB:P09036, ECO:0000269|PubMed:5466061}.
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:0000269|PubMed:5466061,
CC ECO:0000269|PubMed:7169635}.
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DR PIR; A91174; TIPG.
DR PDB; 1TGS; X-ray; 1.80 A; I=1-56.
DR PDBsum; 1TGS; -.
DR AlphaFoldDB; P00998; -.
DR SMR; P00998; -.
DR MINT; P00998; -.
DR STRING; 9823.ENSSSCP00000022179; -.
DR MEROPS; I01.011; -.
DR PaxDb; P00998; -.
DR PeptideAtlas; P00998; -.
DR Ensembl; ENSSSCT00005038608; ENSSSCP00005023696; ENSSSCG00005024363.
DR eggNOG; KOG3649; Eukaryota.
DR HOGENOM; CLU_169765_6_0_1; -.
DR InParanoid; P00998; -.
DR EvolutionaryTrace; P00998; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P00998; SS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
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 3D-structure; Direct protein sequencing; Disulfide bond;
KW Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor.
FT CHAIN 1..56
FT /note="Serine protease inhibitor Kazal-type 1"
FT /id="PRO_0000073027"
FT DOMAIN 3..56
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 18..19
FT /note="Reactive bond for trypsin"
FT /evidence="ECO:0000250|UniProtKB:P09036,
FT ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 20..21
FT /note="Necessary for sperm binding"
FT /evidence="ECO:0000250|UniProtKB:P09036"
FT DISULFID 9..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798,
FT ECO:0000269|PubMed:4672150"
FT DISULFID 16..35
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798,
FT ECO:0000269|PubMed:4672150"
FT DISULFID 24..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798,
FT ECO:0000269|PubMed:4672150"
FT VARIANT 1..4
FT /note="Missing (in a second inhibitor)"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:1TGS"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1TGS"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1TGS"
FT HELIX 34..42
FT /evidence="ECO:0007829|PDB:1TGS"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1TGS"
SQ SEQUENCE 56 AA; 6023 MW; 39A3649DADF16D25 CRC64;
TSPQREATCT SEVSGCPKIY NPVCGTDGIT YSNECVLCSE NKKRQTPVLI QKSGPC
