EPPI_RAT
ID EPPI_RAT Reviewed; 134 AA.
AC D4A2Z2;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 73.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) 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}.
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DR EMBL; AABR06027547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474005; EDL96509.1; -; Genomic_DNA.
DR RefSeq; NP_001102927.1; NM_001109457.1.
DR AlphaFoldDB; D4A2Z2; -.
DR SMR; D4A2Z2; -.
DR STRING; 10116.ENSRNOP00000019829; -.
DR MEROPS; I02.956; -.
DR PaxDb; D4A2Z2; -.
DR PRIDE; D4A2Z2; -.
DR Ensembl; ENSRNOT00000019829; ENSRNOP00000019829; ENSRNOG00000028908.
DR GeneID; 685161; -.
DR KEGG; rno:685161; -.
DR UCSC; RGD:1597722; rat.
DR CTD; 57119; -.
DR RGD; 1597722; Eppin.
DR eggNOG; KOG4295; Eukaryota.
DR GeneTree; ENSGT00940000156753; -.
DR HOGENOM; CLU_127181_0_0_1; -.
DR InParanoid; D4A2Z2; -.
DR OMA; CCVFNCG; -.
DR OrthoDB; 1474897at2759; -.
DR PhylomeDB; D4A2Z2; -.
DR TreeFam; TF342459; -.
DR Reactome; R-RNO-6803157; Antimicrobial peptides.
DR PRO; PR:D4A2Z2; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000234681; Chromosome 3.
DR Bgee; ENSRNOG00000028908; Expressed in testis and 7 other tissues.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
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:0090281; P:negative regulation of calcium ion import; ISO:RGD.
DR GO; GO:1901318; P:negative regulation of flagellated sperm motility; ISO:RGD.
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 SMART; SM00217; WAP; 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 3: Inferred from homology;
KW Antimicrobial; Disulfide bond; Protease inhibitor; Reference proteome;
KW Repeat; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..134
FT /note="Eppin"
FT /id="PRO_0000419802"
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 134 AA; 15684 MW; 402CDFB7B7CFA260 CRC64;
MKFSRFVSIL VLFGLLTKVQ GPSLTDFLFP RRCPRFREEC EHRERDLCTR DRDCQKREKC
CIFSCGKKCL NPQQDICSLP KDSGYCMAYF PRWWYNKKNG TCQLFIYGGC QGNNNNFQSQ
SICQNACEKK SNST
