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Eppin (Cancer/testis antigen 71) (CT71) (Epididymal protease inhibitor) (Protease inhibitor WAP7) (Serine protease inhibitor-like with Kunitz and WAP domains 1) (WAP four-disulfide core domain protein 7)

 EPPI_HUMAN              Reviewed;         133 AA.
O95925; A6PVD6; Q86TP9; Q96SD7; Q9HD30;
04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
23-MAY-2018, entry version 154.
RecName: Full=Eppin;
AltName: Full=Cancer/testis antigen 71;
Short=CT71;
AltName: Full=Epididymal protease inhibitor;
AltName: Full=Protease inhibitor WAP7;
AltName: Full=Serine protease inhibitor-like with Kunitz and WAP domains 1;
AltName: Full=WAP four-disulfide core domain protein 7;
Flags: Precursor;
Name=EPPIN; Synonyms=SPINLW1, WAP7, WFDC7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBUNIT, AND TISSUE
SPECIFICITY.
TISSUE=Epididymis, and Testis;
PubMed=11404006; DOI=10.1016/S0378-1119(01)00462-0;
Richardson R.T., Sivashanmugam P., Hall S.H., Hamil K.G., Moore P.A.,
Ruben S.M., French F.S., O'Rand M.G.;
"Cloning and sequencing of human eppin: a novel family of protease
inhibitors expressed in the epididymis and testis.";
Gene 270:93-102(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Stavrides G.S., Huckle E.J., Deloukas P.;
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION.
PubMed=15229136; DOI=10.1095/biolreprod.104.031567;
Yenugu S., Richardson R.T., Sivashanmugam P., Wang Z., O'rand M.G.,
French F.S., Hall S.H.;
"Antimicrobial activity of human EPPIN, an androgen-regulated, sperm-
bound protein with a whey acidic protein motif.";
Biol. Reprod. 71:1484-1490(2004).
[7]
INTERACTION WITH SEMG1, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=15590901; DOI=10.1095/biolreprod.104.036483;
Wang Z., Widgren E.E., Sivashanmugam P., O'Rand M.G., Richardson R.T.;
"Association of eppin with semenogelin on human spermatozoa.";
Biol. Reprod. 72:1064-1070(2005).
[8]
IDENTIFICATION IN A COMPLEX WITH LTF AND CLU, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=17567961; DOI=10.1095/biolreprod.107.060194;
Wang Z., Widgren E.E., Richardson R.T., O'Rand M.G.;
"Characterization of an eppin protein complex from human semen and
spermatozoa.";
Biol. Reprod. 77:476-484(2007).
[9]
FUNCTION ON KLK3 ACTIVITY, AND MUTAGENESIS OF LEU-87.
PubMed=17644992;
Wang Z., Widgren E.E., Richardson R.T., Orand M.G.;
"Eppin: a molecular strategy for male contraception.";
Soc. Reprod. Fertil. Suppl. 65:535-542(2007).
[10]
DOMAIN.
PubMed=18331357; DOI=10.1111/j.1742-4658.2008.06333.x;
McCrudden M.T., Dafforn T.R., Houston D.F., Turkington P.T.,
Timson D.J.;
"Functional domains of the human epididymal protease inhibitor,
eppin.";
FEBS J. 275:1742-1750(2008).
[11]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=21461566; DOI=10.3892/mmr.2010.403;
Long Y., Gu A., Yang H., Ji G., Han X., Song L., Wang S., Wang X.;
"Distribution of Eppin in mouse and human testis.";
Mol. Med. Report. 4:71-75(2011).
[12]
INTERACTION WITH LTF AND SEMG1, MUTAGENESIS OF CYS-102; TYR-107;
CYS-110; PHE-117; CYS-123 AND CYS-127, AND PUTATIVE CONTRACEPTIVE
TARGET.
PubMed=22699487; DOI=10.1095/biolreprod.112.101832;
Silva E.J., Hamil K.G., Richardson R.T., O'Rand M.G.;
"Characterization of EPPIN's semenogelin I binding Site: a
contraceptive drug target.";
Biol. Reprod. 87:56-56(2012).
-!- FUNCTION: Serine protease inhibitor that plays an essential role
in male reproduction and fertility. Modulates the hydrolysis of
SEMG1 by KLK3/PSA (a serine protease), provides antimicrobial
protection for spermatozoa in the ejaculate coagulum, and binds
SEMG1 thereby inhibiting sperm motility.
{ECO:0000269|PubMed:15229136, ECO:0000269|PubMed:17644992}.
-!- SUBUNIT: Monomer. Homodimer. Homomultimers. Interacts with SEMG1
(via 164-283 AA). Interacts with LTF. Found in a complex with LTF,
CLU, EPPIN and SEMG1. {ECO:0000269|PubMed:11404006,
ECO:0000269|PubMed:15590901, ECO:0000269|PubMed:17567961,
ECO:0000269|PubMed:22699487}.
-!- SUBCELLULAR LOCATION: Isoform 1: Secreted. Cell surface.
Note=Bound to the surface of testicular and on the head and tail
of ejaculate spermatozoa.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O95925-1; Sequence=Displayed;
Name=2; Synonyms=Eppin-2;
IsoId=O95925-2; Sequence=VSP_006755;
Note=Lacks a cleavable signal sequence.;
Name=3;
IsoId=O95925-3; Sequence=VSP_043679;
Note=Based on a readthrough transcript which may produce a
EPPIN-WFDC6 fusion protein. No experimental confirmation
available.;
-!- TISSUE SPECIFICITY: In testis, expressed and secreted by Sertoli
cells, appearing on the surface of testicular and ejaculate
spermatozoa. Expressed in the spermatogonia and the earliest
preleptotene spermatocytes. In the epididymis, is expressed and
secreted by epithelial cells and covers the surface of epididymal
spermatozoa and ciliated epithelial cells (at protein level).
Expressed specifically in epididymis and testis. Isoform 2 is
expressed only in the epididymis. Weak expression is detected in
myoid cells as well as spermatogenic cells.
{ECO:0000269|PubMed:11404006, ECO:0000269|PubMed:21461566}.
-!- DOMAIN: The BPTI/Kunitz inhibitor domain is required for elastase
inhibitory activity. BPTI/Kunitz inhibitor and WAP domains are
involved in the protein antibacterial activity.
{ECO:0000269|PubMed:18331357}.
-!- MISCELLANEOUS: Might be used as a target for male contraception.
{ECO:0000305|PubMed:22699487}.
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EMBL; AF286368; AAG00546.1; -; mRNA.
EMBL; AF286369; AAG00547.1; -; mRNA.
EMBL; AF286370; AAG00548.1; -; mRNA.
EMBL; AL118493; CAB56343.1; -; mRNA.
EMBL; AK301937; BAG63357.1; -; mRNA.
EMBL; AL031663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC044829; AAH44829.2; -; mRNA.
EMBL; BC053369; AAH53369.1; -; mRNA.
CCDS; CCDS13359.1; -. [O95925-1]
RefSeq; NP_001185915.1; NM_001198986.1. [O95925-3]
RefSeq; NP_001289790.1; NM_001302861.1.
RefSeq; NP_065131.1; NM_020398.3. [O95925-1]
UniGene; Hs.121084; -.
UniGene; Hs.274876; -.
ProteinModelPortal; O95925; -.
SMR; O95925; -.
BioGrid; 121383; 4.
IntAct; O95925; 1.
STRING; 9606.ENSP00000452085; -.
MEROPS; I02.058; -.
BioMuta; EPPIN; -.
PaxDb; O95925; -.
PeptideAtlas; O95925; -.
PRIDE; O95925; -.
DNASU; 57119; -.
Ensembl; ENST00000336443; ENSP00000338114; ENSG00000101448. [O95925-2]
Ensembl; ENST00000354280; ENSP00000361746; ENSG00000101448. [O95925-1]
Ensembl; ENST00000504988; ENSP00000424176; ENSG00000249139. [O95925-3]
GeneID; 100526773; -.
GeneID; 57119; -.
KEGG; hsa:100526773; -.
KEGG; hsa:57119; -.
UCSC; uc002xou.4; human. [O95925-1]
CTD; 100526773; -.
CTD; 57119; -.
DisGeNET; 57119; -.
EuPathDB; HostDB:ENSG00000101448.13; -.
EuPathDB; HostDB:ENSG00000249139.1; -.
GeneCards; EPPIN; -.
GeneCards; EPPIN-WFDC6; -.
HGNC; HGNC:15932; EPPIN.
HGNC; HGNC:38825; EPPIN-WFDC6.
MIM; 609031; gene.
neXtProt; NX_O95925; -.
OpenTargets; ENSG00000101448; -.
OpenTargets; ENSG00000249139; -.
PharmGKB; PA38054; -.
eggNOG; KOG4295; Eukaryota.
eggNOG; ENOG410XQNP; LUCA.
GeneTree; ENSGT00730000110932; -.
HOGENOM; HOG000115819; -.
HOVERGEN; HBG004024; -.
InParanoid; O95925; -.
OMA; ANVQGPG; -.
OrthoDB; EOG091G09P2; -.
PhylomeDB; O95925; -.
TreeFam; TF342459; -.
Reactome; R-HSA-6803157; Antimicrobial peptides.
GeneWiki; SPINLW1; -.
PRO; PR:O95925; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000101448; -.
CleanEx; HS_SPINLW1; -.
ExpressionAtlas; O95925; baseline and differential.
Genevisible; O95925; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0097524; C:sperm plasma membrane; TAS:Reactome.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0019730; P:antimicrobial humoral response; TAS:Reactome.
GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
GO; GO:0090281; P:negative regulation of calcium ion import; IMP:UniProtKB.
GO; GO:1901318; P:negative regulation of flagellated sperm motility; IMP:UniProtKB.
GO; GO:0010466; P:negative regulation of peptidase activity; IDA:UniProtKB.
GO; GO:0051259; P:protein complex oligomerization; IDA:UniProtKB.
CDD; cd00109; KU; 1.
Gene3D; 4.10.410.10; -; 1.
Gene3D; 4.10.75.10; -; 1.
InterPro; IPR036645; Elafin-like_sf.
InterPro; IPR002223; Kunitz_BPTI.
InterPro; IPR036880; Kunitz_BPTI_sf.
InterPro; IPR020901; Prtase_inh_Kunz-CS.
InterPro; IPR008197; WAP_dom.
Pfam; PF00014; Kunitz_BPTI; 1.
Pfam; PF00095; WAP; 1.
PRINTS; PR00759; BASICPTASE.
SMART; SM00131; KU; 1.
SMART; SM00217; WAP; 1.
SUPFAM; SSF57256; SSF57256; 1.
SUPFAM; SSF57362; SSF57362; 1.
PROSITE; PS00280; BPTI_KUNITZ_1; 1.
PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PROSITE; PS51390; WAP; 1.
1: Evidence at protein level;
Alternative splicing; Antimicrobial; Complete proteome;
Disulfide bond; Polymorphism; Protease inhibitor; Reference proteome;
Secreted; Serine protease inhibitor; Signal.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 133 Eppin.
/FTId=PRO_0000041378.
DOMAIN 26 73 WAP. {ECO:0000255|PROSITE-
ProRule:PRU00722}.
DOMAIN 77 127 BPTI/Kunitz inhibitor.
{ECO:0000255|PROSITE-ProRule:PRU00031}.
REGION 102 133 Interaction with SEMG1.
REGION 117 133 Interaction with LTF.
{ECO:0000269|PubMed:22699487}.
DISULFID 33 61 {ECO:0000250}.
DISULFID 40 65 {ECO:0000250}.
DISULFID 48 60 {ECO:0000250}.
DISULFID 54 69 {ECO:0000250}.
DISULFID 77 127 {ECO:0000250}.
DISULFID 86 110 {ECO:0000250}.
DISULFID 102 123 {ECO:0000250}.
VAR_SEQ 1 31 MGSSGLLSLLVLFVLLANVQGPGLTDWLFPR -> MLSKAH
GCKTALSLG (in isoform 2).
{ECO:0000303|PubMed:11404006}.
/FTId=VSP_006755.
VAR_SEQ 131 133 RFP -> QPCPKIKVECEVEEIDQCTKPRDCPENMKCCPFS
RGKKCLDFRKASLST (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043679.
VARIANT 92 92 H -> R (in dbSNP:rs2231838).
/FTId=VAR_024696.
VARIANT 128 128 K -> T (in dbSNP:rs2231839).
/FTId=VAR_052950.
MUTAGEN 87 87 L->G: Loss of effect on KLK3 activity.
{ECO:0000269|PubMed:17644992}.
MUTAGEN 102 102 C->A: Reduces the binding to SEMG1 by
45%. {ECO:0000269|PubMed:22699487}.
MUTAGEN 107 107 Y->A: Reduces the binding to SEMG1 by
68%. {ECO:0000269|PubMed:22699487}.
MUTAGEN 110 110 C->A: Does not affect the binding of
SEMG1 or LTF. Does not affect the binding
of SEMG1; when associated with A-123 and
A-127. {ECO:0000269|PubMed:22699487}.
MUTAGEN 117 117 F->A: Reduces the binding to SEMG1 by 68%
and to LTF by 73%.
{ECO:0000269|PubMed:22699487}.
MUTAGEN 123 123 C->A: Does not affect the binding of
SEMG1 or LTF. Does not affect the binding
of SEMG1; when associated with A-110 and
A-127. {ECO:0000269|PubMed:22699487}.
MUTAGEN 127 127 C->A: Does not affect the binding of
SEMG1 or LTF. Does not affect the binding
of SEMG1; when associated with A-110 and
A-123. {ECO:0000269|PubMed:22699487}.
SEQUENCE 133 AA; 15284 MW; F7831B203366D9DC CRC64;
MGSSGLLSLL VLFVLLANVQ GPGLTDWLFP RRCPKIREEC EFQERDVCTK DRQCQDNKKC
CVFSCGKKCL DLKQDVCEMP KETGPCLAYF LHWWYDKKDN TCSMFVYGGC QGNNNNFQSK
ANCLNTCKNK RFP


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EIAAB46307 C20orf122,Homo sapiens,Human,Putative protease inhibitor WAP12,UNQ544_PRO844,WAP four-disulfide core domain protein 12,WAP2,WFDC12,Whey acidic protein 2
EIAAB46324 C20orf170,Homo sapiens,Human,Putative protease inhibitor WAP8,WAP four-disulfide core domain protein 8,WAP8,WFDC8


 

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