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IKP1_PHYSA
ID   IKP1_PHYSA              Reviewed;          58 AA.
AC   P83578;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2004, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Proteinase inhibitor PSKP-1;
OS   Phyllomedusa sauvagei (Sauvage's leaf frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Phyllomedusa.
OX   NCBI_TaxID=8395;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MASS
RP   SPECTROMETRY, MUTAGENESIS OF 11-GLY--PRO-16, AND CIRCULAR DICHROISM
RP   ANALYSIS.
RC   TISSUE=Skin;
RX   PubMed=15153102; DOI=10.1111/j.1432-1033.2004.04127.x;
RA   Gebhard L.G., Carrizo F.U., Stern A.L., Burgardt N.I., Faivovich J.,
RA   Lavilla E., Ermacora M.R.;
RT   "A Kazal prolyl endopeptidase inhibitor isolated from the skin of
RT   Phyllomedusa sauvagii.";
RL   Eur. J. Biochem. 271:2117-2126(2004).
CC   -!- FUNCTION: Has antibacterial activity against Gram-negative bacterium
CC       E.coli ATCC 11229. Shows hemagglutinating activity. Inhibits prolyl
CC       endopeptidase, but not trypsin, chymotrypsin, V8 protease and
CC       proteinase K. May have a role in mucosal defense against microbes by
CC       interacting directly with their membranes.
CC       {ECO:0000269|PubMed:15153102}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15153102}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15153102}.
CC   -!- TISSUE SPECIFICITY: Skin.
CC   -!- MASS SPECTROMETRY: Mass=7332.0; Mass_error=0.7; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15153102};
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DR   AlphaFoldDB; P83578; -.
DR   SMR; P83578; -.
DR   MEROPS; I01.035; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
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   Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW   Protease inhibitor; Secreted.
FT   CHAIN           1..58
FT                   /note="Proteinase inhibitor PSKP-1"
FT                   /id="PRO_0000073043"
FT   DOMAIN          1..58
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        6..36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        14..33
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        22..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   MUTAGEN         11..16
FT                   /note="GKKCPP->LPGCPK: Significant inhibitory activity
FT                   against trypsin."
FT                   /evidence="ECO:0000269|PubMed:15153102"
SQ   SEQUENCE   58 AA;  6702 MW;  DD75B9FB9A8D7322 CRC64;
     VIEPKCYKYE GKKCPPDINP VCGTDKRTYY NECALCVFIR QSTKKADKAI KIKKWGKC
 
 
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