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Database: UniProt
Entry: WFDC2_MOUSE
LinkDB: WFDC2_MOUSE
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ID   WFDC2_MOUSE             Reviewed;         174 AA.
AC   Q9DAU7;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=WAP four-disulfide core domain protein 2;
DE   AltName: Full=WAP domain-containing protein HE4;
DE   Flags: Precursor;
GN   Name=Wfdc2; Synonyms=He4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Bingle C.D.;
RT   "Cloning of mouse HE4.";
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Broad range protease inhibitor. {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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DR   EMBL; AF334269; AAL73189.1; -; mRNA.
DR   EMBL; AK005519; BAB24094.1; -; mRNA.
DR   CCDS; CCDS17040.1; -.
DR   RefSeq; NP_080599.1; NM_026323.2.
DR   AlphaFoldDB; Q9DAU7; -.
DR   SMR; Q9DAU7; -.
DR   STRING; 10090.ENSMUSP00000017867; -.
DR   MEROPS; I17.004; -.
DR   MaxQB; Q9DAU7; -.
DR   PaxDb; 10090-ENSMUSP00000017867; -.
DR   PeptideAtlas; Q9DAU7; -.
DR   ProteomicsDB; 297558; -.
DR   Antibodypedia; 27648; 746 antibodies from 43 providers.
DR   DNASU; 67701; -.
DR   Ensembl; ENSMUST00000017867.10; ENSMUSP00000017867.4; ENSMUSG00000017723.12.
DR   GeneID; 67701; -.
DR   KEGG; mmu:67701; -.
DR   UCSC; uc008nve.1; mouse.
DR   AGR; MGI:1914951; -.
DR   CTD; 10406; -.
DR   MGI; MGI:1914951; Wfdc2.
DR   VEuPathDB; HostDB:ENSMUSG00000017723; -.
DR   eggNOG; ENOG502SA8J; Eukaryota.
DR   GeneTree; ENSGT00730000111410; -.
DR   InParanoid; Q9DAU7; -.
DR   OMA; GECADNL; -.
DR   OrthoDB; 2963895at2759; -.
DR   PhylomeDB; Q9DAU7; -.
DR   BioGRID-ORCS; 67701; 0 hits in 78 CRISPR screens.
DR   ChiTaRS; Wfdc2; mouse.
DR   PRO; PR:Q9DAU7; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q9DAU7; Protein.
DR   Bgee; ENSMUSG00000017723; Expressed in right lung lobe and 154 other cell types or tissues.
DR   ExpressionAtlas; Q9DAU7; baseline and differential.
DR   Genevisible; Q9DAU7; MM.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; ISO:MGI.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; ISO:MGI.
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:SF34; WAP FOUR-DISULFIDE CORE DOMAIN PROTEIN 2; 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   Aspartic protease inhibitor; Disulfide bond; Protease inhibitor;
KW   Reference proteome; Repeat; Secreted; Serine protease inhibitor; Signal;
KW   Thiol protease inhibitor.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..174
FT                   /note="WAP four-disulfide core domain protein 2"
FT                   /id="PRO_0000041371"
FT   DOMAIN          29..74
FT                   /note="WAP 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DOMAIN          125..173
FT                   /note="WAP 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   REGION          68..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        36..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        45..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        132..160
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        143..164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        147..159
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        153..169
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
SQ   SEQUENCE   174 AA;  18032 MW;  82484E28ED6F1E20 CRC64;
     MPACRLCLLA AGLLLGLLLF TPISATGTDA EKPGECPQLE PITDCVLECT LDKDCADNRK
     CCQAGCSSVC SKPNGPSEGE LSGTDTKLSE TGTTTQSAGL DHTTKPPGGQ VSTKPPAVTR
     EGLGVREKQG TCPSVDIPKL GLCEDQCQVD SQCSGNMKCC RNGCGKMACT TPKF
//
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