ID   YL15_CAEEL              Reviewed;         176 AA.
AC   Q11101; A3FPJ1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 3.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=BPTI/Kunitz inhibitor domain-containing protein C02F12.5;
DE   Flags: Precursor;
GN   ORFNames=C02F12.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-34, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=12754521; DOI=10.1038/nbt829;
RA   Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA   Kasai K., Takahashi N., Isobe T.;
RT   "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT   identify N-linked glycoproteins.";
RL   Nat. Biotechnol. 21:667-672(2003).
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-34, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA   Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA   Taoka M., Takahashi N., Isobe T.;
RT   "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT   elegans and suggests an atypical translocation mechanism for integral
RT   membrane proteins.";
RL   Mol. Cell. Proteomics 6:2100-2109(2007).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FO080254; CCD62378.1; -; Genomic_DNA.
DR   RefSeq; NP_508632.2; NM_076231.3.
DR   AlphaFoldDB; Q11101; -.
DR   SMR; Q11101; -.
DR   STRING; 6239.C02F12.5; -.
DR   iPTMnet; Q11101; -.
DR   PaxDb; Q11101; -.
DR   PeptideAtlas; Q11101; -.
DR   EnsemblMetazoa; C02F12.5.1; C02F12.5.1; WBGene00015355.
DR   GeneID; 180656; -.
DR   KEGG; cel:CELE_C02F12.5; -.
DR   UCSC; C02F12.5; c. elegans.
DR   CTD; 180656; -.
DR   WormBase; C02F12.5; CE40681; WBGene00015355; -.
DR   eggNOG; KOG4295; Eukaryota.
DR   GeneTree; ENSGT00970000196297; -.
DR   HOGENOM; CLU_105995_0_0_1; -.
DR   InParanoid; Q11101; -.
DR   OMA; CKPADQF; -.
DR   OrthoDB; 1373305at2759; -.
DR   PhylomeDB; Q11101; -.
DR   PRO; PR:Q11101; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00015355; Expressed in adult organism and 2 other tissues.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.410.10; -; 1.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   Pfam; PF00014; Kunitz_BPTI; 1.
DR   SMART; SM00131; KU; 1.
DR   SUPFAM; SSF57362; SSF57362; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Protease inhibitor; Reference proteome;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..176
FT                   /note="BPTI/Kunitz inhibitor domain-containing protein
FT                   C02F12.5"
FT                   /id="PRO_0000417920"
FT   DOMAIN          21..74
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   CARBOHYD        34
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754521,
FT                   ECO:0000269|PubMed:17761667"
FT   DISULFID        21..74
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        31..57
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        49..70
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ   SEQUENCE   176 AA;  19578 MW;  0E90E9D921F399F3 CRC64;
     MLFFTLLIQL FLVPVLCQYA CSSELKFGTA CSENKTSTKW YYDSKLLFCY PYKYLGCGEG
     SNSFESNENC LESCKPADQF SCGGNTGPDG VCFAHGDQGC KKGTVCVMGG MVGFCCDKKI
     QDEWNKENSP KCLKGQVVQF KQWFGMTPLI GRSCSHNFCP EKSTCVQGKW TAYCCQ