WFDC2_CANLF
ID WFDC2_CANLF Reviewed; 124 AA.
AC Q28894;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=WAP four-disulfide core domain protein 2;
DE AltName: Full=Epididymal secretory protein E4;
DE Short=CE4;
DE AltName: Full=Major epididymis-specific protein E4;
DE Flags: Precursor;
GN Name=WFDC2;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Epididymis;
RX PubMed=7744511; DOI=10.1111/j.1365-2605.1994.tb01262.x;
RA Ellerbrock K., Pera I., Hartung S., Ivell R.;
RT "Gene expression in the dog epididymis: a model for human epididymal
RT function.";
RL Int. J. Androl. 17:314-323(1994).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=7744512; DOI=10.1111/j.1365-2605.1994.tb01263.x;
RA Pera I., Ivell R., Kirchhoff C.;
RT "Regional variation of specific gene expression in the dog epididymis as
RT revealed by in-situ transcript hybridization.";
RL Int. J. Androl. 17:324-330(1994).
CC -!- FUNCTION: Broad range protease inhibitor (By similarity). Possible
CC function in sperm maturation. {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Epididymis. Highest levels are found in the caput
CC and proximal cauda regions. Lower levels in the distal cauda. Not
CC detected in the efferent ducts. {ECO:0000269|PubMed:7744512}.
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DR EMBL; S77395; AAB34264.1; -; mRNA.
DR PIR; I54768; I54768.
DR RefSeq; NP_001003241.1; NM_001003241.1.
DR AlphaFoldDB; Q28894; -.
DR SMR; Q28894; -.
DR STRING; 9615.ENSCAFP00000014248; -.
DR MEROPS; I17.004; -.
DR GeneID; 403919; -.
DR KEGG; cfa:403919; -.
DR CTD; 10406; -.
DR eggNOG; ENOG502SA8J; Eukaryota.
DR InParanoid; Q28894; -.
DR OrthoDB; 1409658at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; 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; 2.
DR PROSITE; PS51390; WAP; 2.
PE 2: Evidence at transcript level;
KW Aspartic protease inhibitor; Disulfide bond; Glycoprotein;
KW Protease inhibitor; Reference proteome; Repeat; Secreted;
KW Serine protease inhibitor; Signal; Thiol protease inhibitor.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..124
FT /note="WAP four-disulfide core domain protein 2"
FT /id="PRO_0000041369"
FT DOMAIN 29..73
FT /note="WAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DOMAIN 74..123
FT /note="WAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 45..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 49..61
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 55..70
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 80..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 93..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 97..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 103..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
SQ SEQUENCE 124 AA; 12951 MW; 15AAF315BA13958C CRC64;
MPACRPGPLA GALLLGLLLL GLPRVPGGEV EKTGVCPQLQ ADLNCTQECV SDAQCADNLK
CCQAGCATIC HLPNEKEGSC PQVNTDFPQL GLCQDQCQVD SHCPGLLKCC YNGCGKVSCV
TPIF
