WFDC2_RABIT
ID WFDC2_RABIT Reviewed; 123 AA.
AC Q28631;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=WAP four-disulfide core domain protein 2;
DE AltName: Full=Epididymal protein BE-20;
DE AltName: Full=Major epididymis-specific protein E4;
DE Flags: Precursor;
GN Name=WFDC2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SEQUENCE REVISION TO 29.
RC TISSUE=Epididymis;
RX PubMed=10101572; DOI=10.1080/014850199262896;
RA Fan H.-Y., Miao S.-Y., Wang L.-F., Koide S.S.;
RT "Expression and characterization of an epididymis-specific gene.";
RL Arch. Androl. 42:63-69(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-123, AND PROTEIN SEQUENCE OF 29-58.
RC TISSUE=Epididymis;
RX PubMed=8886263; DOI=10.3109/01485019608988514;
RA Xu W.D., Wang L.-F., Miao S.-Y., Zhao M., Fan H.-Y., Zong S.D., Wu Y.W.,
RA Shi X.Q., Koide S.S.;
RT "Identification of a rabbit epididymal protein gene.";
RL Arch. Androl. 37:135-141(1996).
CC -!- FUNCTION: Broad range protease inhibitor. {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Epididymis.
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DR EMBL; U26725; AAA66525.2; -; mRNA.
DR RefSeq; NP_001075823.1; NM_001082354.1.
DR AlphaFoldDB; Q28631; -.
DR SMR; Q28631; -.
DR STRING; 9986.ENSOCUP00000008219; -.
DR MEROPS; I17.004; -.
DR GeneID; 100009206; -.
DR KEGG; ocu:100009206; -.
DR CTD; 10406; -.
DR eggNOG; ENOG502SA8J; Eukaryota.
DR InParanoid; Q28631; -.
DR OrthoDB; 1409658at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
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; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Protease inhibitor; Reference proteome; Repeat; Secreted;
KW Serine protease inhibitor; Signal; Thiol protease inhibitor.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:8886263"
FT CHAIN 29..123
FT /note="WAP four-disulfide core domain protein 2"
FT /id="PRO_0000041373"
FT DOMAIN 30..71
FT /note="WAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DOMAIN 74..122
FT /note="WAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 46..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 50..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 56..71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 81..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 92..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 96..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 102..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
SQ SEQUENCE 123 AA; 12803 MW; 99F9A649CCBB5B32 CRC64;
MPASRLVPLG AVLLLGLLLL LELPPVTGTG ADKPGVCPQL SADLNCTQDC RADQDCAENL
KCCRAGCSAI CSIPNEKEGS CPSIDFPQLG ICQDLCQVDS QCPGKMKCCL NGCGKVSCVT
PNF
