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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
 
 
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