WAP_NOTEU
ID WAP_NOTEU Reviewed; 191 AA.
AC Q9N0L8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Whey acidic protein;
DE AltName: Full=tWAP;
DE Flags: Precursor;
GN Name=WAP;
OS Notamacropus eugenii (Tammar wallaby) (Macropus eugenii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Diprotodontia; Macropodidae; Notamacropus.
OX NCBI_TaxID=9315;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], 3D-STRUCTURE MODELING, AND DISULFIDE BONDS.
RC TISSUE=Lactating mammary gland;
RX PubMed=10801834; DOI=10.1074/jbc.m002161200;
RA Simpson K.J., Ranganathan S., Fisher J.A., Janssens P.A., Shaw D.C.,
RA Nicholas K.R.;
RT "The gene for a novel member of the whey acidic protein family encodes
RT three four-disulfide core domains and is asynchronously expressed during
RT lactation.";
RL J. Biol. Chem. 275:23074-23081(2000).
CC -!- FUNCTION: Could be a protease inhibitor.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Milk-specific; major protein component of milk
CC whey.
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DR EMBL; AJ005356; CAB90357.1; -; mRNA.
DR AlphaFoldDB; Q9N0L8; -.
DR SMR; Q9N0L8; -.
DR MEROPS; I17.950; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030414; F:peptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0010466; P:negative regulation of peptidase activity; IEA:UniProtKB-KW.
DR Gene3D; 4.10.75.10; -; 3.
DR InterPro; IPR036645; Elafin-like_sf.
DR InterPro; IPR008197; WAP_dom.
DR Pfam; PF00095; WAP; 3.
DR PRINTS; PR00003; 4DISULPHCORE.
DR SMART; SM00217; WAP; 3.
DR SUPFAM; SSF57256; SSF57256; 3.
DR PROSITE; PS51390; WAP; 3.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Milk protein; Protease inhibitor; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..191
FT /note="Whey acidic protein"
FT /id="PRO_0000041354"
FT DOMAIN 22..71
FT /note="WAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DOMAIN 72..125
FT /note="WAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DOMAIN 126..175
FT /note="WAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:10801834"
FT DISULFID 42..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:10801834"
FT DISULFID 46..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:10801834"
FT DISULFID 52..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:10801834"
FT DISULFID 78..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:10801834"
FT DISULFID 97..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:10801834"
FT DISULFID 101..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:10801834"
FT DISULFID 107..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:10801834"
FT DISULFID 133..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:10801834"
FT DISULFID 140..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:10801834"
FT DISULFID 150..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:10801834"
FT DISULFID 156..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:10801834"
SQ SEQUENCE 191 AA; 21133 MW; BF90B81DADBBE50D CRC64;
MQPVQILTLV LLALGAWAAQ ESTEKAGYCP DFRQVLLDRR DCKQLCNDDA SCPQNMRCCQ
RGCSWLCMNT TQEKDGLCPV ATSHSSSSEE QQRKQLCDKT CKTDLGCEGK AKCCASSCGQ
TCFMPVKAKP GRCPAVTGIC PEKKSWFHTC QRDDQCKENK KCCSSACGRR CTNPFPEEYE
ASQDESTLLA L