ELAF_PIG
ID ELAF_PIG Reviewed; 167 AA.
AC Q29125;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Elafin;
DE AltName: Full=Protein WAP-1;
DE Flags: Precursor;
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 [GENOMIC DNA].
RX PubMed=8636131; DOI=10.1074/jbc.271.12.7012;
RA Tamechika I., Itakura M., Saruta Y., Furukawa M., Kato A., Tachibana S.,
RA Hirose S.;
RT "Accelerated evolution in inhibitor domains of porcine elafin family
RT members.";
RL J. Biol. Chem. 271:7012-7018(1996).
CC -!- FUNCTION: Neutrophil and pancreatic elastase-specific inhibitor of
CC skin. It may prevent elastase-mediated tissue proteolysis (By
CC similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Trachea and large intestine.
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DR EMBL; D50319; BAA08854.1; -; Genomic_DNA.
DR RefSeq; NP_001116687.1; NM_001123215.1.
DR AlphaFoldDB; Q29125; -.
DR SMR; Q29125; -.
DR MEROPS; I17.002; -.
DR PRIDE; Q29125; -.
DR Ensembl; ENSSSCT00070024379; ENSSSCP00070020177; ENSSSCG00070012460.
DR Ensembl; ENSSSCT00070024381; ENSSSCP00070020179; ENSSSCG00070012460.
DR GeneID; 396757; -.
DR CTD; 5266; -.
DR eggNOG; ENOG502SZ79; Eukaryota.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 17.
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; -; 1.
DR InterPro; IPR036645; Elafin-like_sf.
DR InterPro; IPR019541; Trappin_transglut-bd_rpt.
DR InterPro; IPR008197; WAP_dom.
DR Pfam; PF10511; Cementoin; 1.
DR Pfam; PF00095; WAP; 1.
DR PRINTS; PR00003; 4DISULPHCORE.
DR SMART; SM00217; WAP; 1.
DR SUPFAM; SSF57256; SSF57256; 1.
DR PROSITE; PS51390; WAP; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Protease inhibitor; Reference proteome; Repeat;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..70
FT /evidence="ECO:0000255"
FT /id="PRO_0000041359"
FT CHAIN 71..167
FT /note="Elafin"
FT /id="PRO_0000041360"
FT REPEAT 44..49
FT /note="1"
FT REPEAT 50..55
FT /note="2"
FT REPEAT 56..61
FT /note="3"
FT REPEAT 62..67
FT /note="4"
FT REPEAT 68..73
FT /note="5"
FT REPEAT 74..79
FT /note="6"
FT REPEAT 80..101
FT /note="SVP-1 clotting 1"
FT REPEAT 80..85
FT /note="7"
FT REPEAT 86..91
FT /note="8"
FT REPEAT 92..97
FT /note="9"
FT REPEAT 98..103
FT /note="10"
FT REPEAT 104..126
FT /note="SVP-1 clotting 2"
FT REPEAT 104..109
FT /note="11"
FT REPEAT 110..115
FT /note="12"
FT DOMAIN 119..167
FT /note="WAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT REGION 44..115
FT /note="12 X 6 AA tandem repeats of [GSAL]-[QEK]-[DGLP]-
FT [APSLQ]-[VGDFI]-[KR]"
FT REGION 46..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..126
FT /note="2 X tandem repeats of SVP-1 like motif"
FT DISULFID 126..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 133..159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 142..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 148..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
SQ SEQUENCE 167 AA; 17923 MW; 25932EA1A459D9CA CRC64;
MRSRSFLVLV VVFLICGTLV AQAAGRIRRP KGKGTKKILA LVKGQGPVRG KDQVKGQGPV
KGQDLGKSQD PVKAQLPDKG QDLGKGEDSV KGQDPFKAQL PDKLQDPVKA QPAIKRLILL
TKPGSCPRIL IRCLMVNPPN RCLSDAQCPG LKKCCEGFCG KACMDPK
