ID   WAP_RAT                 Reviewed;         137 AA.
AC   P01174;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 2.
DT   28-FEB-2018, entry version 120.
DE   RecName: Full=Whey acidic protein;
DE            Short=WAP;
DE   AltName: Full=Whey phosphoprotein;
DE   Flags: Precursor;
GN   Name=Wap;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
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.,
RA   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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6896749; DOI=10.1093/nar/10.12.3733;
RA   Hennighausen L.G., Sippel A.E.;
RT   "Comparative sequence analysis of the mRNAs coding for mouse and rat
RT   whey protein.";
RL   Nucleic Acids Res. 10:3733-3744(1982).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-41, AND DISULFIDE
RP   BONDS.
RX   PubMed=6955785; DOI=10.1073/pnas.79.13.3987;
RA   Dandekar A.M., Robinson E.A., Appella E., Qasba P.K.;
RT   "Complete sequence analysis of cDNA clones encoding rat whey
RT   phosphoprotein: homology to a protease inhibitor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 79:3987-3991(1982).
CC   -!- FUNCTION: Could be a protease inhibitor.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Milk-specific; major protein component of milk
CC       whey.
CC   -!- PTM: Contains 8 disulfide bonds.
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DR   EMBL; X01153; CAA25600.2; -; Genomic_DNA.
DR   EMBL; X01154; CAA25600.2; JOINED; Genomic_DNA.
DR   EMBL; X01155; CAA25600.2; JOINED; Genomic_DNA.
DR   EMBL; X01156; CAA25600.2; JOINED; Genomic_DNA.
DR   EMBL; J00802; AAA42347.1; -; mRNA.
DR   EMBL; J00801; AAA42346.1; -; mRNA.
DR   PIR; A93920; WYRT.
DR   RefSeq; NP_446203.1; NM_053751.4.
DR   UniGene; Rn.9978; -.
DR   ProteinModelPortal; P01174; -.
DR   SMR; P01174; -.
DR   STRING; 10116.ENSRNOP00000010744; -.
DR   PaxDb; P01174; -.
DR   PRIDE; P01174; -.
DR   GeneID; 114596; -.
DR   KEGG; rno:114596; -.
DR   UCSC; RGD:621851; rat.
DR   CTD; 22373; -.
DR   RGD; 621851; Wap.
DR   eggNOG; ENOG410JG7V; Eukaryota.
DR   eggNOG; ENOG411160P; LUCA.
DR   HOGENOM; HOG000133035; -.
DR   HOVERGEN; HBG098607; -.
DR   InParanoid; P01174; -.
DR   KO; K17106; -.
DR   PhylomeDB; P01174; -.
DR   PRO; PR:P01174; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030414; F:peptidase inhibitor activity; NAS:RGD.
DR   Gene3D; 4.10.75.10; -; 1.
DR   InterPro; IPR036645; Elafin-like_sf.
DR   InterPro; IPR008197; WAP_dom.
DR   Pfam; PF00095; WAP; 1.
DR   PRINTS; PR00003; 4DISULPHCORE.
DR   SMART; SM00217; WAP; 1.
DR   SUPFAM; SSF57256; SSF57256; 1.
DR   PROSITE; PS51390; WAP; 2.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   Milk protein; Protease inhibitor; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL        1     19       {ECO:0000269|PubMed:6955785}.
FT   CHAIN        20    137       Whey acidic protein.
FT                                /FTId=PRO_0000041353.
FT   DOMAIN       27     73       WAP 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00722}.
FT   DOMAIN       76    127       WAP 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00722}.
FT   DISULFID     34     61       {ECO:0000305|PubMed:6955785}.
FT   DISULFID     45     65       {ECO:0000305|PubMed:6955785}.
FT   DISULFID     48     60       {ECO:0000305|PubMed:6955785}.
FT   DISULFID     54     69       {ECO:0000305|PubMed:6955785}.
FT   DISULFID     83    115       {ECO:0000305|PubMed:6955785}.
FT   DISULFID     96    119       {ECO:0000305|PubMed:6955785}.
FT   DISULFID    102    114       {ECO:0000305|PubMed:6955785}.
FT   DISULFID    108    123       {ECO:0000305|PubMed:6955785}.
FT   CONFLICT      4      4       S -> F (in Ref. 3; AAA42347).
FT                                {ECO:0000305}.
FT   CONFLICT     35     35       S -> P (in Ref. 2 and 3). {ECO:0000305}.
FT   CONFLICT     39     39       F -> S (in Ref. 2 and 3). {ECO:0000305}.
FT   CONFLICT     47     47       N -> K (in Ref. 2; AAA42346).
FT                                {ECO:0000305}.
FT   CONFLICT     68     68       S -> P (in Ref. 2 and 3). {ECO:0000305}.
FT   CONFLICT     99     99       D -> G (in Ref. 2; AAA42346).
FT                                {ECO:0000305}.
FT   CONFLICT    116    116       K -> N (in Ref. 2 and 3). {ECO:0000305}.
FT   CONFLICT    127    127       E -> K (in Ref. 2). {ECO:0000305}.
FT   CONFLICT    129    129       K -> D (in Ref. 2). {ECO:0000305}.
FT   CONFLICT    129    129       K -> E (in Ref. 3; AAA42347).
FT                                {ECO:0000305}.
FT   CONFLICT    134    134       I -> V (in Ref. 3; AAA42347).
FT                                {ECO:0000305}.
SQ   SEQUENCE   137 AA;  14827 MW;  1C2E8ADA9FD97949 CRC64;