WFDC2_MOUSE
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 03-AUG-2022, entry version 129.
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; Q9DAU7; -.
DR PeptideAtlas; Q9DAU7; -.
DR PRIDE; Q9DAU7; -.
DR ProteomicsDB; 297558; -.
DR Antibodypedia; 27648; 648 antibodies from 43 providers.
DR DNASU; 67701; -.
DR Ensembl; ENSMUST00000017867; ENSMUSP00000017867; ENSMUSG00000017723.
DR GeneID; 67701; -.
DR KEGG; mmu:67701; -.
DR UCSC; uc008nve.1; mouse.
DR CTD; 10406; -.
DR MGI; MGI:1914951; Wfdc2.
DR VEuPathDB; HostDB:ENSMUSG00000017723; -.
DR eggNOG; ENOG502SA8J; Eukaryota.
DR GeneTree; ENSGT00730000111410; -.
DR InParanoid; Q9DAU7; -.
DR OMA; NEKQGSC; -.
DR OrthoDB; 1409658at2759; -.
DR PhylomeDB; Q9DAU7; -.
DR BioGRID-ORCS; 67701; 0 hits in 73 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 151 other 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 Gene3D; 4.10.75.10; -; 2.
DR InterPro; IPR036645; Elafin-like_sf.
DR InterPro; IPR008197; WAP_dom.
DR Pfam; PF00095; WAP; 2.
DR PRINTS; PR00003; 4DISULPHCORE.
DR SMART; SM00217; WAP; 2.
DR SUPFAM; SSF57256; SSF57256; 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