ID G1R4U2_NOMLE Unreviewed; 133 AA.
AC G1R4U2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Epididymal peptidase inhibitor {ECO:0000313|Ensembl:ENSNLEP00000008214.2};
GN Name=EPPIN {ECO:0000313|Ensembl:ENSNLEP00000008214.2};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000008214.2, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000008214.2, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000008214.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; ADFV01004494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003253690.1; XM_003253642.2.
DR AlphaFoldDB; G1R4U2; -.
DR STRING; 61853.ENSNLEP00000008214; -.
DR Ensembl; ENSNLET00000008602.2; ENSNLEP00000008214.2; ENSNLEG00000035598.1.
DR GeneID; 100606932; -.
DR KEGG; nle:100606932; -.
DR eggNOG; KOG4295; Eukaryota.
DR GeneTree; ENSGT00940000156753; -.
DR HOGENOM; CLU_127181_0_0_1; -.
DR InParanoid; G1R4U2; -.
DR OMA; CCVFNCG; -.
DR OrthoDB; 3558236at2759; -.
DR TreeFam; TF342459; -.
DR Proteomes; UP000001073; Chromosome 13.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
DR GO; GO:0090281; P:negative regulation of calcium ion import; IEA:Ensembl.
DR GO; GO:1901318; P:negative regulation of flagellated sperm motility; IEA:Ensembl.
DR CDD; cd22611; Kunitz_eppin; 1.
DR Gene3D; 4.10.75.10; Elafin-like; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1.
DR InterPro; IPR036645; Elafin-like_sf.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR008197; WAP_dom.
DR PANTHER; PTHR46751; EPPIN; 1.
DR PANTHER; PTHR46751:SF2; EPPIN; 1.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR Pfam; PF00095; WAP; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 1.
DR SMART; SM00217; WAP; 1.
DR SUPFAM; SSF57362; BPTI-like; 1.
DR SUPFAM; SSF57256; Elafin-like; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR PROSITE; PS51390; WAP; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..133
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014195348"
FT DOMAIN 26..73
FT /note="WAP"
FT /evidence="ECO:0000259|PROSITE:PS51390"
FT DOMAIN 77..127
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
SQ SEQUENCE 133 AA; 15213 MW; 68026707181A6034 CRC64;
MGSSGLLSLL VLFILLANVQ GPGLTDWLFP RRCPKIREEC GFKERDVCTK DRQCQDNKKC
CVFSCGKKCL DLKQDVCEMP KETGPCLAYF LRWWYDKKNN TCSMFVYGGC PGNNNNFQSK
ANCLNTCKNK RFP
//
