ID   PI15_XENLA              Reviewed;         258 AA.
AC   Q3KPV7;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Peptidase inhibitor 15;
DE   Flags: Precursor;
GN   Name=pi15;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serine protease inhibitor which displays weak inhibitory
CC       activity against trypsin (By similarity). May be involved in facial
CC       patterning during embryonic development (By similarity).
CC       {ECO:0000250|UniProtKB:O43692, ECO:0000250|UniProtKB:Q98ST6}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O43692}.
CC   -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR   EMBL; BC106529; AAI06530.1; -; mRNA.
DR   RefSeq; NP_001089770.1; NM_001096301.1.
DR   AlphaFoldDB; Q3KPV7; -.
DR   SMR; Q3KPV7; -.
DR   DNASU; 734834; -.
DR   GeneID; 734834; -.
DR   KEGG; xla:734834; -.
DR   CTD; 734834; -.
DR   Xenbase; XB-GENE-989407; pi15.S.
DR   OMA; CSPNEVY; -.
DR   OrthoDB; 1528782at2759; -.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 734834; Expressed in internal ear and 8 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030414; F:peptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0010466; P:negative regulation of peptidase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.33.10; -; 1.
DR   InterPro; IPR018244; Allrgn_V5/Tpx1_CS.
DR   InterPro; IPR014044; CAP_domain.
DR   InterPro; IPR035940; CAP_sf.
DR   InterPro; IPR001283; CRISP-related.
DR   PANTHER; PTHR10334; PTHR10334; 1.
DR   Pfam; PF00188; CAP; 1.
DR   PRINTS; PR00837; V5TPXLIKE.
DR   SMART; SM00198; SCP; 1.
DR   SUPFAM; SSF55797; SSF55797; 1.
DR   PROSITE; PS01010; CRISP_2; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Glycoprotein; Protease inhibitor;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..60
FT                   /evidence="ECO:0000250|UniProtKB:O43692"
FT                   /id="PRO_0000287630"
FT   CHAIN           61..258
FT                   /note="Peptidase inhibitor 15"
FT                   /id="PRO_0000287631"
FT   DOMAIN          71..211
FT                   /note="SCP"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   258 AA;  29195 MW;  F8B9378FB3BFE30A CRC64;
     MIEMISISAA FLLSLLCETC GLVLPKSSDL AIAASNYTII KPDLSARLDP VKAPKARRKR
     YISQNDMIEI VEYHNQVRGK VFPPAANMEY MVWDDNLAKL AEAWAATCIW DHGPSYLLKF
     LGQNLSVRTG RYKSILQLVK PWYDEVKDYA FPYPQECNPR CPLRCYGPMC THYTQMVWAT
     TNRIGCAIHT CHNINVWGAV WRRAVYLVCN YSPKGNWIGE APYTIGVPCS ACPPSYGGSC
     SDNQCFPGIT SNYLHWFK