ID WFDC5_HUMAN Reviewed; 224 AA. AC Q8TCV5; Q5H981; Q6UWE4; DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 04-NOV-2026, entry version 176. DE RecName: Full=WAP four-disulfide core domain protein 5; DE AltName: Full=Putative protease inhibitor WAP1; DE AltName: Full=p53-responsive gene 5 protein; DE Flags: Precursor; GN Name=WFDC5; Synonyms=PRG5, WAP1; ORFNames=UNQ3036/PRO9842; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=12206714; DOI=10.1042/bj20020869; RA Clauss A., Lilja H., Lundwall A.; RT "A locus on human chromosome 20 contains several genes expressing protease RT inhibitor domains with homology to whey acidic protein."; RL Biochem. J. 368:233-242(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT TYR-97. RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 145-224 (ISOFORM 1), AND INDUCTION. RX PubMed=10441517; DOI=10.1006/bbrc.1999.1123; RA Horikoshi N., Cong J., Kley N., Shenk T.; RT "Isolation of differentially expressed cDNAs from p53-dependent apoptotic RT cells: activation of the human homologue of the Drosophila peroxidasin RT gene."; RL Biochem. Biophys. Res. Commun. 261:864-869(1999). CC -!- FUNCTION: Putative acid-stable proteinase inhibitor. CC -!- INTERACTION: CC Q8TCV5; Q12797-6: ASPH; NbExp=3; IntAct=EBI-12175871, EBI-12092171; CC Q8TCV5; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-12175871, EBI-2837444; CC Q8TCV5; P27658: COL8A1; NbExp=3; IntAct=EBI-12175871, EBI-747133; CC Q8TCV5; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-12175871, EBI-6426443; CC Q8TCV5; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12175871, EBI-16439278; CC Q8TCV5; O43765: SGTA; NbExp=3; IntAct=EBI-12175871, EBI-347996; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8TCV5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8TCV5-2; Sequence=VSP_006756; CC -!- INDUCTION: By p53/TP53. {ECO:0000269|PubMed:10441517}. 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; AY038181; AAK72468.1; -; mRNA. DR EMBL; AY358822; AAQ89181.1; -; mRNA. DR EMBL; Z93016; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC039173; AAH39173.1; -; mRNA. DR EMBL; AF147078; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS33475.1; -. [Q8TCV5-2] DR RefSeq; NP_001382435.1; NM_001395506.1. [Q8TCV5-2] DR RefSeq; NP_663627.1; NM_145652.4. [Q8TCV5-2] DR RefSeq; XP_011526903.1; XM_011528601.2. [Q8TCV5-2] DR RefSeq; XP_054179048.1; XM_054323073.1. [Q8TCV5-2] DR AlphaFoldDB; Q8TCV5; -. DR SMR; Q8TCV5; -. DR BioGRID; 127236; 12. DR IntAct; Q8TCV5; 7. DR NDEx; IQUERY-CP-WFDC5; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000361875; -. DR MEROPS; I17.003; -. DR BioMuta; WFDC5; -. DR DMDM; 26401313; -. DR MassIVE; Q8TCV5; -. DR PaxDb; 9606-ENSP00000361875; -. DR PeptideAtlas; Q8TCV5; -. DR ProteomicsDB; 74178; -. [Q8TCV5-1] DR ProteomicsDB; 74179; -. [Q8TCV5-2] DR Antibodypedia; 27523; 144 antibodies from 18 providers. DR DNASU; 149708; -. DR Ensembl; ENST00000307971.7; ENSP00000312381.4; ENSG00000175121.12. [Q8TCV5-1] DR Ensembl; ENST00000372789.6; ENSP00000361875.4; ENSG00000175121.12. [Q8TCV5-2] DR GeneID; 149708; -. DR KEGG; hsa:149708; -. DR MANE-Select; ENST00000372789.6; ENSP00000361875.4; NM_145652.4; NP_663627.1. [Q8TCV5-2] DR UCSC; uc002xne.2; human. [Q8TCV5-1] DR AGR; HGNC:20477; -. DR ClinPGx; PA134885667; -. DR CTD; 149708; -. DR DisGeNET; 149708; -. DR GeneCards; WFDC5; -. DR HGNC; HGNC:20477; WFDC5. DR HPA; ENSG00000175121; Tissue enriched (skin). DR MIM; 605161; gene. DR OpenTargets; ENSG00000175121; -. DR VEuPathDB; HostDB:ENSG00000175121; -. DR eggNOG; ENOG502S99V; Eukaryota. DR GeneTree; ENSGT00730000111369; -. DR HOGENOM; CLU_105901_2_0_1; -. DR InParanoid; Q8TCV5; -. DR OrthoDB; 4473401at2759; -. DR PAN-GO; Q8TCV5; 4 GO annotations based on evolutionary models. DR PhylomeDB; Q8TCV5; -. DR PathwayCommons; Q8TCV5; -. DR SignaLink; Q8TCV5; -. DR Agora; ENSG00000175121; -. DR BioGRID-ORCS; 149708; 7 hits in 1135 CRISPR screens. DR GeneWiki; WFDC5; -. DR GenomeRNAi; 149708; -. DR Pharos; Q8TCV5; Tbio. DR PRO; PR:Q8TCV5; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; Q8TCV5; protein. DR Bgee; ENSG00000175121; Expressed in upper arm skin and 90 other cell types or tissues. DR GO; GO:0005576; C:extracellular region; IBA:GO_Central. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central. DR GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central. DR GO; GO:0045087; P:innate immune response; IBA:GO_Central. DR CDD; cd00199; WAP; 1. DR Gene3D; 4.10.75.10; Elafin-like; 2. DR InterPro; IPR036645; Elafin-like_sf. DR InterPro; IPR008197; WAP_dom. DR PANTHER; PTHR19441:SF39; WAP FOUR-DISULFIDE CORE DOMAIN PROTEIN 5; 1. DR PANTHER; PTHR19441; WHEY ACDIC PROTEIN WAP; 1. DR Pfam; PF00095; WAP; 2. DR PRINTS; PR00003; 4DISULPHCORE. DR SMART; SM00217; WAP; 2. DR SUPFAM; SSF57256; Elafin-like; 2. DR PROSITE; PS51390; WAP; 2. PE 1: Evidence at protein level; KW Alternative splicing; Disulfide bond; Protease inhibitor; KW Proteomics identification; Reference proteome; Repeat; Secreted; KW Serine protease inhibitor; Signal. FT SIGNAL 1..24 FT /evidence="ECO:0000255" FT CHAIN 25..224 FT /note="WAP four-disulfide core domain protein 5" FT /id="PRO_0000041382" FT DOMAIN 27..73 FT /note="WAP 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722" FT DOMAIN 74..121 FT /note="WAP 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722" 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" FT DISULFID 81..109 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722" FT DISULFID 88..113 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722" FT DISULFID 96..108 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722" FT DISULFID 102..117 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722" FT VAR_SEQ 124..224 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12206714, FT ECO:0000303|PubMed:12975309, ECO:0000303|PubMed:15489334" FT /id="VSP_006756" FT VARIANT 97 FT /note="H -> Y (in dbSNP:rs17422688)" FT /evidence="ECO:0000269|PubMed:12975309" FT /id="VAR_057474" FT CONFLICT 172 FT /note="Q -> R (in Ref. 5; AF147078)" FT /evidence="ECO:0000305" SQ SEQUENCE 224 AA; 24238 MW; 305CC59024058F15 CRC64; MRTQSLLLLG ALLAVGSQLP AVFGRKKGEK SGGCPPDDGP CLLSVPDQCV EDSQCPLTRK CCYRACFRQC VPRVSVKLGS CPEDQLRCLS PMNHLCHKDS DCSGKKRCCH SACGRDCRDP ARGTAPGCPG QANSDLGSVA LHLSWGPTER VHDGRPGALP AGQHYLYQRW FQPSDNHWPA DTSLQPIHPW FLLLGVKVHS LSSEEGLCIT PVLCTTAIRA SHPS //