ID   EPPI_MACMU              Reviewed;         133 AA.
AC   Q9BDL1;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Eppin;
DE   AltName: Full=Epididymal protease inhibitor;
DE   AltName: Full=Serine protease inhibitor-like with Kunitz and WAP domains 1;
DE   Flags: Precursor;
GN   Name=EPPIN; Synonyms=SPINLW1;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Epididymis, and Testis;
RA   Sivashanmugam P., Hall S.H., Hamil K.G., French F.S., O'Rand M.G.,
RA   Richardson R.T.;
RT   "Characterization of monkey and mouse Eppin, a protease inhibitor from
RT   epididymis and testis.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serine protease inhibitor that plays an essential role in
CC       male reproduction and fertility. Modulates the hydrolysis of SEMG1 by
CC       KLK3/PSA (a serine protease), provides antimicrobial protection for
CC       spermatozoa in the ejaculate coagulum, and binds SEMG1 thereby
CC       inhibiting sperm motility (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. Homodimer. Homomultimers. Interacts with SEMG1 (via
CC       164-283 AA). Interacts with LTF. Found in a complex with LTF, CLU,
CC       EPPIN and SEMG1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Note=Bound to the surface
CC       of testicular and on the head and tail of ejaculate spermatozoa.
CC       {ECO:0000250}.
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DR   EMBL; AF346414; AAK31336.1; -; mRNA.
DR   RefSeq; NP_001028013.1; NM_001032841.1.
DR   AlphaFoldDB; Q9BDL1; -.
DR   STRING; 9544.ENSMMUP00000005074; -.
DR   MEROPS; I02.058; -.
DR   MEROPS; I17.953; -.
DR   GeneID; 574162; -.
DR   KEGG; mcc:574162; -.
DR   CTD; 574162; -.
DR   eggNOG; KOG4295; Eukaryota.
DR   InParanoid; Q9BDL1; -.
DR   OrthoDB; 1474897at2759; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR   GO; GO:0010466; P:negative regulation of peptidase activity; ISS:UniProtKB.
DR   CDD; cd00109; KU; 1.
DR   Gene3D; 4.10.410.10; -; 1.
DR   Gene3D; 4.10.75.10; -; 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   Pfam; PF00014; Kunitz_BPTI; 1.
DR   Pfam; PF00095; WAP; 1.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00131; KU; 1.
DR   SUPFAM; SSF57256; SSF57256; 1.
DR   SUPFAM; SSF57362; SSF57362; 1.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR   PROSITE; PS51390; WAP; 1.
PE   2: Evidence at transcript level;
KW   Antimicrobial; Disulfide bond; Protease inhibitor; Reference proteome;
KW   Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..133
FT                   /note="Eppin"
FT                   /id="PRO_0000041379"
FT   DOMAIN          26..73
FT                   /note="WAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DOMAIN          77..127
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   REGION          102..133
FT                   /note="Interaction with SEMG1"
FT                   /evidence="ECO:0000250"
FT   REGION          117..133
FT                   /note="Interaction with LTF"
FT                   /evidence="ECO:0000250"
FT   DISULFID        33..61
FT                   /evidence="ECO:0000250"
FT   DISULFID        40..65
FT                   /evidence="ECO:0000250"
FT   DISULFID        48..60
FT                   /evidence="ECO:0000250"
FT   DISULFID        54..69
FT                   /evidence="ECO:0000250"
FT   DISULFID        77..127
FT                   /evidence="ECO:0000250"
FT   DISULFID        86..110
FT                   /evidence="ECO:0000250"
FT   DISULFID        102..123
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   133 AA;  15279 MW;  433AE946E39A35E9 CRC64;
     MGSSGLLSLL VLFILLVNVQ GPGLTDWLFP RRCPTIREEC EFRERDVCTR HRQCPDNKKC
     CVFSCGKKCL DLKQDVCEMP NETGPCLAFF IRWWYDKKNN TCSTFVHGGC QGNNNNFQSE
     ANCLNTCKNK RFP