WAP_PIG
ID WAP_PIG Reviewed; 132 AA.
AC O46655; O97559;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Whey acidic protein;
DE Short=WAP;
DE Flags: Precursor;
GN Name=WAP;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 20-56 AND 93-132.
RX PubMed=9513079; DOI=10.1677/jme.0.0200027;
RA Simpson K.J., Bird P., Shaw D., Nicholas K.R.;
RT "Molecular characterisation and hormone-dependent expression of the porcine
RT whey acidic protein gene.";
RL J. Mol. Endocrinol. 20:27-35(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11311554; DOI=10.1016/s0378-1119(01)00388-2;
RA Rival S., Attal J., Delville-Giraud C., Yerle M., Laffont P.,
RA Rogel-Gaillard C., Houdebine L.-M.;
RT "Cloning, transcription and chromosomal localization of the porcine whey
RT acidic protein gene and its expression in HC11 cell line.";
RL Gene 267:37-47(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-132.
RC TISSUE=Mammary gland;
RA Masel A.M., Hall A., Bell K.T.;
RT "Cloning and characterisation of the porcine whey acidic protein.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP 3D-STRUCTURE MODELING OF 20-132, AND DISULFIDE BONDS.
RX PubMed=10680116; DOI=10.1016/s1093-3263(99)00023-6;
RA Ranganathan S., Simpson K.J., Shaw D.C., Nicholas K.R.;
RT "The whey acidic protein family: a new signature motif and three-
RT dimensional structure by comparative modeling.";
RL J. Mol. Graph. Model. 17:106-113(1999).
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.
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DR EMBL; AJ000221; CAA03950.1; -; mRNA.
DR EMBL; AF320306; AAK52450.1; -; Genomic_DNA.
DR EMBL; AF034646; AAC72878.1; -; mRNA.
DR RefSeq; NP_999006.1; NM_213841.2.
DR AlphaFoldDB; O46655; -.
DR SMR; O46655; -.
DR STRING; 9823.ENSSSCP00000017721; -.
DR MEROPS; I17.001; -.
DR PaxDb; O46655; -.
DR PeptideAtlas; O46655; -.
DR Ensembl; ENSSSCT00000018212; ENSSSCP00000017721; ENSSSCG00000016731.
DR Ensembl; ENSSSCT00015003203; ENSSSCP00015001061; ENSSSCG00015002600.
DR Ensembl; ENSSSCT00025009917; ENSSSCP00025003957; ENSSSCG00025007450.
DR Ensembl; ENSSSCT00030043698; ENSSSCP00030019754; ENSSSCG00030031546.
DR Ensembl; ENSSSCT00035087512; ENSSSCP00035036539; ENSSSCG00035064989.
DR Ensembl; ENSSSCT00040021168; ENSSSCP00040008877; ENSSSCG00040015722.
DR Ensembl; ENSSSCT00045054069; ENSSSCP00045037630; ENSSSCG00045031688.
DR Ensembl; ENSSSCT00050053853; ENSSSCP00050022665; ENSSSCG00050039885.
DR Ensembl; ENSSSCT00055046999; ENSSSCP00055037489; ENSSSCG00055023873.
DR Ensembl; ENSSSCT00060005564; ENSSSCP00060001890; ENSSSCG00060004478.
DR Ensembl; ENSSSCT00065024780; ENSSSCP00065010118; ENSSSCG00065018652.
DR Ensembl; ENSSSCT00070030198; ENSSSCP00070025188; ENSSSCG00070015373.
DR GeneID; 396835; -.
DR KEGG; ssc:396835; -.
DR CTD; 22373; -.
DR eggNOG; ENOG502RXHY; Eukaryota.
DR GeneTree; ENSGT00730000111762; -.
DR HOGENOM; CLU_156961_0_0_1; -.
DR InParanoid; O46655; -.
DR OMA; PQGTKCC; -.
DR OrthoDB; 1438317at2759; -.
DR TreeFam; TF339378; -.
DR Proteomes; UP000008227; Chromosome 18.
DR Proteomes; UP000314985; Chromosome 18.
DR Bgee; ENSSSCG00000016731; Expressed in epididymis and 15 other tissues.
DR Genevisible; O46655; SS.
DR GO; GO:0005615; C:extracellular space; 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 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; 1.
DR PROSITE; PS51390; WAP; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Milk protein;
KW Protease inhibitor; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:9513079"
FT CHAIN 20..132
FT /note="Whey acidic protein"
FT /id="PRO_0000041351"
FT DOMAIN 23..73
FT /note="WAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DOMAIN 76..126
FT /note="WAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 32..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:10680116"
FT DISULFID 43..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:10680116"
FT DISULFID 47..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:10680116"
FT DISULFID 53..69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:10680116"
FT DISULFID 83..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:10680116"
FT DISULFID 95..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:10680116"
FT DISULFID 101..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:10680116"
FT DISULFID 107..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:10680116"
FT CONFLICT 39..40
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 132 AA; 13956 MW; 7F7796493C0D98E0 CRC64;
MRFLTSLALA LIALEAALAL APALNLPGLA TCPELSSSSE DPCVISCVND ESCPQGTKCC
ARSPCSRSCT VPLLVPVPKA GRCPWVPAPL APELCLEKNE CSRDDQCRGN KKCCFSSCAM
RCLDPDTEAP LQ
