ISK6_BOVIN
ID ISK6_BOVIN Reviewed; 80 AA.
AC P01001;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 3.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=Serine protease inhibitor Kazal-type 6;
DE AltName: Full=Acrosin inhibitor 2;
DE AltName: Full=Acrosin inhibitor IIA;
DE AltName: Full=BUSI-II;
DE Flags: Precursor;
GN Name=SPINK6;
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=Seminal vesicle;
RA McCulloch A., Wilson T., Molenaar A., Grigor M., Davis S., Glenn M.,
RA Havukkala I., Watson J., Crawford A., Wheeler T., Hagemann L., Lee R.,
RA Hein W., Johnstone P., Maqbool N., McMahon C., McCracken J., Stelwagen K.,
RA Farr V., Singh K., Whitley J., Nicholas K., Savin K., Mather A.,
RA McPartlan H., Whitley J., Wells M., Bowman P., Goddard M., Langford C.,
RA McEwan J., Atkinson P.;
RT "AgResearch, genesis and primary industry Victoria bovine EST project.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 24-80, PYROGLUTAMATE FORMATION AT GLN-24, AND VARIANT
RP IIB.
RX PubMed=500016;
RA Cechova D., Meloun B.;
RT "Differences in the evolution of seminal plasma acrosin inhibitors and
RT pancreatic secretory trypsin inhibitors.";
RL Hoppe-Seyler's Z. Physiol. Chem. 360:1497-1500(1979).
RN [3]
RP SEQUENCE REVISION TO 79-80.
RX PubMed=6864793; DOI=10.1016/s0022-2836(83)80290-3;
RA Frank G.;
RT "Reinvestigation of the C-terminal end in the amino acid sequence of the
RT proteinase inhibitor IIA from bull seminal plasma.";
RL J. Mol. Biol. 166:665-668(1983).
RN [4]
RP STRUCTURE BY NMR OF 24-80.
RX PubMed=6306249; DOI=10.1016/s0022-2836(83)80288-5;
RA Strop P., Wuethrich K.;
RT "Characterization of the proteinase inhibitor IIA from bull seminal plasma
RT by 1H nuclear magnetic resonance. Stability, amide proton exchange and
RT mobility of aromatic residues.";
RL J. Mol. Biol. 166:631-640(1983).
RN [5]
RP STRUCTURE BY NMR OF 24-80, AND SEQUENCE REVISION.
RX PubMed=6306250; DOI=10.1016/s0022-2836(83)80289-7;
RA Strop P., Wider G., Wuethrich K.;
RT "Assignment of the 1H nuclear magnetic resonance spectrum of the proteinase
RT inhibitor IIA from bull seminal plasma by two-dimensional nuclear magnetic
RT resonance at 500 MHz.";
RL J. Mol. Biol. 166:641-665(1983).
RN [6]
RP STRUCTURE BY NMR OF 24-80 OF VARIANT IIB.
RX PubMed=6864794; DOI=10.1016/s0022-2836(83)80291-5;
RA Strop P., Cechova D., Wuethrich K.;
RT "Preliminary structural comparison of the proteinase isoinhibitors IIA and
RT IIB from bull seminal plasma based on individual assignments of the 1H
RT nuclear magnetic resonance spectra by two-dimensional nuclear magnetic
RT resonance at 500 MHz.";
RL J. Mol. Biol. 166:669-676(1983).
RN [7]
RP STRUCTURE BY NMR OF 24-80.
RX PubMed=6699915; DOI=10.1016/0022-2836(84)90125-6;
RA Williamson M.P., Marion D., Wuethrich K.;
RT "Secondary structure in the solution conformation of the proteinase
RT inhibitor IIA from bull seminal plasma by nuclear magnetic resonance.";
RL J. Mol. Biol. 173:341-359(1984).
RN [8]
RP STRUCTURE BY NMR OF 24-80.
RX PubMed=3839023; DOI=10.1016/0022-2836(85)90347-x;
RA Williamson M.P., Havel T.F., Wuethrich K.;
RT "Solution conformation of proteinase inhibitor IIA from bull seminal plasma
RT by 1H nuclear magnetic resonance and distance geometry.";
RL J. Mol. Biol. 182:295-315(1985).
CC -!- FUNCTION: Serine protease inhibitor selective for kallikreins.
CC Efficiently inhibits KLK4, KLK5, KLK6, KLK7, KLK12, KLK13 and KLK14.
CC Doesn't inhibit KLK8. Inhibits acrosin, trypsin, and chymotrypsin.
CC {ECO:0000250|UniProtKB:Q6UWN8}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8BT20}.
CC -!- TISSUE SPECIFICITY: Seminal plasma.
CC -!- MISCELLANEOUS: The sequence of BUSI-IIA is shown.
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DR EMBL; DY218174; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A01235; XTBO.
DR RefSeq; XP_002706142.1; XM_002706096.4.
DR RefSeq; XP_015327798.1; XM_015472312.1.
DR PDB; 1BUS; NMR; -; A=25-80.
DR PDB; 2BUS; NMR; -; A=25-80.
DR PDBsum; 1BUS; -.
DR PDBsum; 2BUS; -.
DR AlphaFoldDB; P01001; -.
DR SMR; P01001; -.
DR STRING; 9913.ENSBTAP00000044797; -.
DR MEROPS; I01.015; -.
DR PaxDb; P01001; -.
DR Ensembl; ENSBTAT00000047606; ENSBTAP00000044797; ENSBTAG00000033470.
DR GeneID; 100335759; -.
DR KEGG; bta:100335759; -.
DR CTD; 404203; -.
DR VEuPathDB; HostDB:ENSBTAG00000033470; -.
DR eggNOG; KOG3649; Eukaryota.
DR GeneTree; ENSGT00530000064225; -.
DR HOGENOM; CLU_169765_1_0_1; -.
DR InParanoid; P01001; -.
DR OMA; DCGEFRD; -.
DR OrthoDB; 1636538at2759; -.
DR EvolutionaryTrace; P01001; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000033470; Expressed in surface of tongue and 26 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:1902572; P:negative regulation of serine-type peptidase activity; IBA:GO_Central.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
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 Protease inhibitor; Pyrrolidone carboxylic acid; Reference proteome;
KW Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:500016"
FT CHAIN 24..80
FT /note="Serine protease inhibitor Kazal-type 6"
FT /id="PRO_0000073033"
FT DOMAIN 24..80
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 42..43
FT /note="Reactive bond"
FT MOD_RES 24
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:500016"
FT DISULFID 30..62
FT DISULFID 40..59
FT DISULFID 48..80
FT VARIANT 24..26
FT /note="QGA -> LF (in IIB)"
FT CONFLICT 51..53
FT /note="DGQ -> NGE (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:2BUS"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:1BUS"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:2BUS"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:1BUS"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:2BUS"
FT HELIX 58..66
FT /evidence="ECO:0007829|PDB:1BUS"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2BUS"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:2BUS"
SQ SEQUENCE 80 AA; 8663 MW; 91E3215704596CD1 CRC64;
MKTSGVFLLL SLALFCFFSG VFGQGAQVDC AEFKDPKVYC TRESNPHCGS DGQTYGNKCA
FCKAVMKSGG KINLKHRGKC
