WAP_MOUSE
ID WAP_MOUSE Reviewed; 134 AA.
AC P01173; P70230; Q61023;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 04-MAY-2001, sequence version 3.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Whey acidic protein;
DE Short=WAP;
DE Flags: Precursor;
GN Name=Wap;
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].
RX PubMed=6896234; DOI=10.1093/nar/10.8.2677;
RA Hennighausen L.G., Sippel A.E.;
RT "Mouse whey acidic protein is a novel member of the family of 'four-
RT disulfide core' proteins.";
RL Nucleic Acids Res. 10:2677-2684(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6095207; DOI=10.1093/nar/12.22.8685;
RA Campbell S.M., Rosen J.M., Hennighausen L.G., Strech-Jurk U., Sippel A.E.;
RT "Comparison of the whey acidic protein genes of the rat and mouse.";
RL Nucleic Acids Res. 12:8685-8697(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GR;
RA Hennighausen L.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP CHARACTERIZATION.
RC STRAIN=YBR;
RX PubMed=6975276; DOI=10.1016/s0021-9258(19)68430-9;
RA Piletz J.E., Heinlen M., Ganschow R.E.;
RT "Biochemical characterization of a novel whey protein from murine milk.";
RL J. Biol. Chem. 256:11509-11516(1981).
CC -!- FUNCTION: Could be a protease inhibitor. May play an important role in
CC mammary gland development and tissue remodeling.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Milk-specific; major protein component of milk
CC whey.
CC -!- PTM: No phosphate or carbohydrate binding could be detected; however,
CC both cholesterol and triglyceride are associated with the mouse
CC protein.
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; V00856; CAA24224.1; -; mRNA.
DR EMBL; X01157; CAA25604.1; -; Genomic_DNA.
DR EMBL; X01158; CAA25604.1; JOINED; Genomic_DNA.
DR EMBL; X01159; CAA25604.1; JOINED; Genomic_DNA.
DR EMBL; X01160; CAA25604.1; JOINED; Genomic_DNA.
DR EMBL; U38816; AAA91321.1; -; Genomic_DNA.
DR CCDS; CCDS24424.1; -.
DR PIR; A93423; WYMS.
DR AlphaFoldDB; P01173; -.
DR SMR; P01173; -.
DR STRING; 10090.ENSMUSP00000099974; -.
DR PaxDb; P01173; -.
DR PRIDE; P01173; -.
DR MGI; MGI:98943; Wap.
DR eggNOG; ENOG502RXHY; Eukaryota.
DR InParanoid; P01173; -.
DR ChiTaRS; Wap; mouse.
DR PRO; PR:P01173; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P01173; protein.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0045735; F:nutrient reservoir activity; IMP:MGI.
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 Gene3D; 4.10.75.10; -; 1.
DR InterPro; IPR036645; Elafin-like_sf.
DR InterPro; IPR008197; WAP_dom.
DR Pfam; PF00095; WAP; 1.
DR SMART; SM00217; WAP; 1.
DR SUPFAM; SSF57256; SSF57256; 1.
DR PROSITE; PS51390; WAP; 2.
PE 1: Evidence at protein level;
KW Disulfide bond; Milk protein; Protease inhibitor; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..134
FT /note="Whey acidic protein"
FT /id="PRO_0000041350"
FT DOMAIN 27..73
FT /note="WAP 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DOMAIN 76..128
FT /note="WAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 45..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 48..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 83..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 97..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 103..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 109..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT CONFLICT 2
FT /note="R -> S (in Ref. 2; CAA25604)"
FT /evidence="ECO:0000305"
FT CONFLICT 11
FT /note="L -> R (in Ref. 3; AAA91321)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="Q -> P (in Ref. 1; CAA24224)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="G -> R (in Ref. 1; CAA24224)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="G -> V (in Ref. 2; CAA25604)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="L -> S (in Ref. 2; CAA25604)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="K -> Q (in Ref. 1; CAA24224)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 134 AA; 14423 MW; C12B2544877ECA80 CRC64;
MRCLISLVLG LLALEVALAQ NLEEQVFNSV QSMFQKASPI EGTECIICQT NEECAQNAMC
CPGSCGRTRK TPVNIGVPKA GFCPWNLLQT ISSTGPCPMK IECSSDRECS GNMKCCNVDC
VMTCTPPVPV ITLQ
