ISK1L_RAT
ID ISK1L_RAT Reviewed; 79 AA.
AC P09656;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Serine protease inhibitor Kazal-type 1-like {ECO:0000312|RGD:708468};
DE AltName: Full=Calcium transport inhibitor;
DE AltName: Full=Caltrin;
DE AltName: Full=Pancreatic secretory trypsin inhibitor II;
DE Short=PSTI-II;
DE Flags: Precursor;
GN Name=Spink1l {ECO:0000312|RGD:708468};
GN Synonyms=Spink3 {ECO:0000312|RGD:708468};
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=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 [2]
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 [3]
RP PROTEIN SEQUENCE OF 24-79, 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 [4]
RP PROTEIN SEQUENCE OF 24-79.
RC TISSUE=Hepatocyte;
RX PubMed=2110056; DOI=10.1111/j.1432-1033.1990.tb15428.x;
RA Kido H., Yokogoshi Y., Katunuma N.;
RT "A low-molecular-mass Kazal-type protease inhibitor isolated from rat
RT hepatocytes is identical to rat pancreatic secretory trypsin inhibitor II.
RT Purification and amino acid sequence.";
RL Eur. J. Biochem. 188:501-506(1990).
RN [5]
RP PROTEIN SEQUENCE OF 24-79, FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Seminal vesicle;
RX PubMed=1400406; DOI=10.1016/s0021-9258(19)36774-2;
RA Coronel C.E., Winnica D.E., Novella M.L., Lardy H.A.;
RT "Purification, structure, and characterization of caltrin proteins from
RT seminal vesicle of the rat and mouse.";
RL J. Biol. Chem. 267:20909-20915(1992).
CC -!- FUNCTION: Serine protease inhibitor which exhibits anti-trypsin
CC activity (PubMed:3202973, PubMed:2110056). In the pancreas, protects
CC against trypsin-catalyzed premature activation of zymogens (By
CC similarity). {ECO:0000250|UniProtKB:P09036, ECO:0000269|PubMed:2110056,
CC ECO:0000269|PubMed:3202973}.
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:0000269|PubMed:1400406}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Seminal vesicle. {ECO:0000269|PubMed:1400406}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M27883; AAA41976.1; ALT_SEQ; mRNA.
DR EMBL; D11325; BAA01945.1; -; Genomic_DNA.
DR PIR; B33292; TIRT2.
DR RefSeq; NP_690919.1; NM_152936.1.
DR AlphaFoldDB; P09656; -.
DR SMR; P09656; -.
DR IntAct; P09656; 1.
DR STRING; 10116.ENSRNOP00000017969; -.
DR MEROPS; I01.047; -.
DR PhosphoSitePlus; P09656; -.
DR PaxDb; P09656; -.
DR PRIDE; P09656; -.
DR GeneID; 266602; -.
DR KEGG; rno:266602; -.
DR UCSC; RGD:708468; rat.
DR CTD; 266602; -.
DR RGD; 708468; Spink1l.
DR eggNOG; KOG3649; Eukaryota.
DR HOGENOM; CLU_169765_2_1_1; -.
DR InParanoid; P09656; -.
DR OMA; EPSCENF; -.
DR OrthoDB; 1591004at2759; -.
DR PhylomeDB; P09656; -.
DR PRO; PR:P09656; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000013410; Expressed in pancreas and 15 other tissues.
DR Genevisible; P09656; RN.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0007568; P:aging; IEP:RGD.
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:1400406,
FT ECO:0000269|PubMed:2110056, ECO:0000269|PubMed:3202973"
FT CHAIN 24..79
FT /note="Serine protease inhibitor Kazal-type 1-like"
FT /id="PRO_0000016559"
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"
SQ SEQUENCE 79 AA; 8565 MW; 6782EBBB531F677C CRC64;
MKVAIIFLLS ALALLNLAGN TTAKVIGKKA NCPNTLVGCP RDYDPVCGTD GKTYANECIL
CFENRKFGTS IRIQRRGLC
