ID   WFD12_MACMU             Reviewed;         111 AA.
AC   A4K2T3;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=WAP four-disulfide core domain protein 12;
DE   Flags: Precursor;
GN   Name=WFDC12;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=17267810; DOI=10.1101/gr.6004607;
RG   NISC comparative sequencing program;
RA   Hurle B., Swanson W., Green E.D.;
RT   "Comparative sequence analyses reveal rapid and divergent evolutionary
RT   changes of the WFDC locus in the primate lineage.";
RL   Genome Res. 17:276-286(2007).
CC   -!- FUNCTION: Antibacterial protein. Putative acid-stable proteinase
CC       inhibitor (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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; DP000043; ABO52968.1; -; Genomic_DNA.
DR   RefSeq; NP_001162152.1; NM_001168681.1.
DR   AlphaFoldDB; A4K2T3; -.
DR   SMR; A4K2T3; -.
DR   STRING; 9544.ENSMMUP00000017364; -.
DR   MEROPS; I17.003; -.
DR   Ensembl; ENSMMUT00000018540; ENSMMUP00000017364; ENSMMUG00000013217.
DR   GeneID; 711552; -.
DR   KEGG; mcc:711552; -.
DR   CTD; 128488; -.
DR   VEuPathDB; HostDB:ENSMMUG00000013217; -.
DR   VGNC; VGNC:79009; WFDC12.
DR   eggNOG; ENOG502TDXW; Eukaryota.
DR   GeneTree; ENSGT00390000012286; -.
DR   HOGENOM; CLU_172659_0_0_1; -.
DR   InParanoid; A4K2T3; -.
DR   Proteomes; UP000006718; Chromosome 10.
DR   Bgee; ENSMMUG00000013217; Expressed in fibroblast and 7 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.75.10; -; 1.
DR   InterPro; IPR036645; Elafin-like_sf.
DR   InterPro; IPR008197; WAP_dom.
DR   InterPro; IPR029718; WFDC12.
DR   PANTHER; PTHR19441:SF42; PTHR19441:SF42; 1.
DR   Pfam; PF00095; WAP; 1.
DR   PRINTS; PR00003; 4DISULPHCORE.
DR   SMART; SM00217; WAP; 1.
DR   SUPFAM; SSF57256; SSF57256; 1.
DR   PROSITE; PS51390; WAP; 1.
PE   3: Inferred from homology;
KW   Antibiotic; Antimicrobial; Disulfide bond; Protease inhibitor;
KW   Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..111
FT                   /note="WAP four-disulfide core domain protein 12"
FT                   /id="PRO_0000289651"
FT   DOMAIN          27..74
FT                   /note="WAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   REGION          80..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        34..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        41..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        49..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        55..70
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
SQ   SEQUENCE   111 AA;  11660 MW;  056C704B8C058E28 CRC64;
     MGSSSFLVLM VSLALVTLVA AEGVKGGIEK AGVCPADNIR CFKSDPPQCH TDQDCLGERK
     CCYLHCGFKC VIPVKKLEEG GNKDEDVSGP CPEPGWEAKS PGSSSTGCPQ K