ISK4_PIG
ID ISK4_PIG Reviewed; 86 AA.
AC P37109;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Serine protease inhibitor Kazal-type 4;
DE AltName: Full=Peptide PEC-60;
DE Flags: Precursor;
GN Name=SPINK4;
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 NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1400298; DOI=10.1016/s0021-9258(19)88629-5;
RA Metsis M., Cintra A., Solfrini V., Ernfors P., Bortolotti F.,
RA Morrasutti D.G., Oestenson C.-G., Efendic S., Agerberth B., Mutt V.,
RA Persson H., Fuxe K.;
RT "Molecular cloning of PEC-60 and expression of its mRNA and peptide in the
RT gastrointestinal tract and immune system.";
RL J. Biol. Chem. 267:19829-19832(1992).
RN [2]
RP PROTEIN SEQUENCE OF 27-86.
RC TISSUE=Intestine;
RX PubMed=2573065; DOI=10.1073/pnas.86.21.8590;
RA Agerberth B., Soederling-Barros J., Joernvall H., Chen Z., Oestenson C.G.,
RA Efendic S., Mutt V.;
RT "Isolation and characterization of a 60-residue intestinal peptide
RT structurally related to the pancreatic secretory type of trypsin inhibitor:
RT influence on insulin secretion.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:8590-8594(1989).
RN [3]
RP STRUCTURE BY NMR OF 27-86.
RX PubMed=8196042; DOI=10.1006/jmbi.1994.1356;
RA Liepinsh E., Berndt K.D., Sillard R., Mutt V., Otting G.;
RT "Solution structure and dynamics of PEC-60, a protein of the Kazal type
RT inhibitor family, determined by nuclear magnetic resonance spectroscopy.";
RL J. Mol. Biol. 239:137-153(1994).
CC -!- FUNCTION: Inhibits the glucose-induced insulin secretion from perfused
CC pancreas; also plays a role in the immune system. Does not inhibit
CC trypsin.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Synthesized in duodenal goblet cells and in
CC monocytes in bone marrow and blood.
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DR EMBL; S46866; AAB23691.2; -; mRNA.
DR EMBL; X67109; CAA47482.1; -; mRNA.
DR PIR; A44041; A34427.
DR RefSeq; NP_999029.1; NM_213864.1.
DR PDB; 1PCE; NMR; -; A=27-86.
DR PDBsum; 1PCE; -.
DR AlphaFoldDB; P37109; -.
DR SMR; P37109; -.
DR STRING; 9823.ENSSSCP00000011731; -.
DR MEROPS; I01.970; -.
DR PaxDb; P37109; -.
DR PeptideAtlas; P37109; -.
DR Ensembl; ENSSSCT00005051461; ENSSSCP00005031826; ENSSSCG00005032240.
DR Ensembl; ENSSSCT00015066081; ENSSSCP00015026467; ENSSSCG00015049625.
DR Ensembl; ENSSSCT00025087573; ENSSSCP00025038171; ENSSSCG00025063921.
DR Ensembl; ENSSSCT00030068143; ENSSSCP00030031169; ENSSSCG00030048829.
DR Ensembl; ENSSSCT00035001915; ENSSSCP00035000621; ENSSSCG00035001542.
DR Ensembl; ENSSSCT00040037502; ENSSSCP00040015616; ENSSSCG00040027988.
DR Ensembl; ENSSSCT00045001615; ENSSSCP00045000985; ENSSSCG00045001065.
DR Ensembl; ENSSSCT00055028083; ENSSSCP00055022377; ENSSSCG00055014267.
DR Ensembl; ENSSSCT00060105096; ENSSSCP00060046118; ENSSSCG00060076589.
DR Ensembl; ENSSSCT00065044216; ENSSSCP00065018852; ENSSSCG00065032615.
DR GeneID; 396872; -.
DR KEGG; ssc:396872; -.
DR CTD; 27290; -.
DR eggNOG; KOG3649; Eukaryota.
DR InParanoid; P37109; -.
DR OrthoDB; 1588023at2759; -.
DR EvolutionaryTrace; P37109; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR039932; Spink4-like.
DR PANTHER; PTHR21179; PTHR21179; 1.
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 3D-structure; Direct protein sequencing; Disulfide bond;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:2573065"
FT CHAIN 27..86
FT /note="Serine protease inhibitor Kazal-type 4"
FT /id="PRO_0000016571"
FT DOMAIN 31..86
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 48..49
FT /note="Reactive bond homolog"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 37..68
FT DISULFID 46..65
FT DISULFID 54..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798,
FT ECO:0000269|PubMed:2573065"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1PCE"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1PCE"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:1PCE"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:1PCE"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:1PCE"
SQ SEQUENCE 86 AA; 9635 MW; 5D513142CF3A4B4D CRC64;
MAVRLWVVAL ALAALFIVDR EVPVSAEKQV FSRMPICEHM TESPDCSRIY DPVCGTDGVT
YESECKLCLA RIENKQDIQI VKDGEC