ID   ZP3_MOUSE               Reviewed;         424 AA.
AC   P10761;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 4.
DT   10-JUN-2008, entry version 72.
DE   Zona pellucida sperm-binding protein 3 precursor (Zona pellucida
DE   glycoprotein ZP3) (Sperm receptor) (Zona pellucida protein C)
DE   [Contains: Processed zona pellucida sperm-binding protein 3].
GN   Name=Zp3; Synonyms=Zp-3, Zpc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=88242926; PubMed=3378665; DOI=10.1016/0012-1606(88)90315-6;
RA   Ringuette M.J., Chamberlin M.E., Baur A.W., Sobieski D.A., Dean J.;
RT   "Molecular analysis of cDNA coding for ZP3, a sperm binding protein of
RT   the mouse zona pellucida.";
RL   Dev. Biol. 127:287-295(1988).
RN   [2]
RP   SEQUENCE REVISION TO 387.
RA   Dean J.;
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CD-1; TISSUE=Liver;
RX   MEDLINE=89240048; PubMed=2541416; DOI=10.1093/nar/17.7.2861;
RA   Kinloch R.A., Wassarman P.M.;
RT   "Nucleotide sequence of the gene encoding zona pellucida glycoprotein
RT   ZP3 -- the mouse sperm receptor.";
RL   Nucleic Acids Res. 17:2861-2863(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=88320451; PubMed=2842770;
RA   Kinloch R.A., Roller R.J., Fimiani C.M., Wassarman D.A.,
RA   Wassarman P.M.;
RT   "Primary structure of the mouse sperm receptor polypeptide determined
RT   by genomic cloning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:6409-6413(1988).
RN   [5]
RP   PROTEIN SEQUENCE OF 49-63; 197-204; 219-233 AND 261-275.
RC   STRAIN=CD-1;
RX   MEDLINE=93050795; PubMed=1330788; DOI=10.1016/0012-1606(92)90070-W;
RA   Rosiere T.K., Wassarman P.M.;
RT   "Identification of a region of mouse zona pellucida glycoprotein mZP3
RT   that possesses sperm receptor activity.";
RL   Dev. Biol. 154:309-317(1992).
RN   [6]
RP   PROTEIN SEQUENCE OF C-TERMINUS, PYROGLUTAMATE FORMATION AT GLN-23,
RP   DISULFIDE BOND FORMATION AT 78-CYS--CYS-98; 216-CYS--CYS-283 AND
RP   240-CYS--CYS-301, GLYCOSYLATION AT ASN-146; ASN-273; ASN-304; ASN-327
RP   AND ASN-330, AND MASS SPECTROMETRY.
RX   MEDLINE=22829890; PubMed=12799386; DOI=10.1074/jbc.M304026200;
RA   Boja E.S., Hoodbhoy T., Fales H.M., Dean J.;
RT   "Structural characterization of native mouse zona pellucida proteins
RT   using mass spectrometry.";
RL   J. Biol. Chem. 278:34189-34202(2003).
CC   -!- FUNCTION: The mammalian zona pellucida, which mediates species-
CC       specific sperm binding, induction of the acrosome reaction and
CC       prevents post-fertilization polyspermy, is composed of three to
CC       four glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP3 is essential for
CC       sperm binding and zona matrix formation.
CC   -!- SUBUNIT: Polymers of ZP2 and ZP3 organized into long filaments
CC       cross-linked by ZP1 homodimers.
CC   -!- SUBCELLULAR LOCATION: Processed zona pellucida sperm-binding
CC       protein 3: Secreted, extracellular space, extracellular matrix.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Oocytes.
CC   -!- DEVELOPMENTAL STAGE: Expressed during the 2-week growth phase of
CC       oogenesis, prior to ovulation.
CC   -!- DOMAIN: The ZP domain is involved in the polymerization of the ZP
CC       proteins to form the zona pellucida.
CC   -!- PTM: Proteolytically cleaved before the transmembrane segment to
CC       yield the secreted ectodomain incorporated in the zona pellucida.
CC   -!- PTM: O-glycosylated; removal of O-linked glycans may play an
CC       important role in the post-fertilization block to polyspermy.
CC   -!- PTM: Cys-320, Cys-322, Cys-323 and Cys-328 are involved in two
CC       additional disulfide bonds.
CC   -!- SIMILARITY: Belongs to the ZP domain family. ZPC subfamily.
CC   -!- SIMILARITY: Contains 1 ZP domain.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Molecular chastity -
CC       Issue 93 of April 2008;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt093.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M20026; AAB18629.1; -; mRNA.
DR   EMBL; X14376; CAA32550.1; -; Genomic_DNA.
DR   PIR; A30334; A30334.
DR   RefSeq; NP_035906.1; -.
DR   UniGene; Mm.1381; -.
DR   Ensembl; ENSMUSG00000004948; Mus musculus.
DR   GeneID; 22788; -.
DR   KEGG; mmu:22788; -.
DR   MGI; MGI:99215; Zp3.
DR   HOGENOM; P10761; -.
DR   HOVERGEN; P10761; -.
DR   ArrayExpress; P10761; -.
DR   CleanEx; MM_ZP3; -.
DR   GermOnline; ENSMUSG00000004948; Mus musculus.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007339; P:binding of sperm to zona pellucida; IDA:MGI.
DR   InterPro; IPR001507; Endoglin/CD105.
DR   Pfam; PF00100; Zona_pellucida; 1.
DR   PRINTS; PR00023; ZPELLUCIDA.
DR   SMART; SM00241; ZP; 1.
DR   PROSITE; PS00682; ZP_1; 1.
DR   PROSITE; PS51034; ZP_2; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Extracellular matrix; Glycoprotein; Membrane;
KW   Pyrrolidone carboxylic acid; Receptor; Secreted; Signal;
KW   Transmembrane.
FT   SIGNAL        1     22
FT   CHAIN        23    351       Zona pellucida sperm-binding protein 3.
FT                                /FTId=PRO_0000041715.
FT   CHAIN        23      ?       Processed zona pellucida sperm-binding
FT                                protein 3.
FT                                /FTId=PRO_0000304572.
FT   PROPEP      352    424       Removed in mature form.
FT                                /FTId=PRO_0000041716.
FT   TOPO_DOM     23    387       Extracellular.
FT   TRANSMEM    388    408       Potential.
FT   TOPO_DOM    409    424       Cytoplasmic.
FT   DOMAIN       45    308       ZP.
FT   MOD_RES      23     23       Pyrrolidone carboxylic acid.
FT   CARBOHYD     32     32       O-linked (GalNAc...) (Probable).
FT   CARBOHYD     34     34       O-linked (GalNAc...) (Probable).
FT   CARBOHYD     39     39       O-linked (GalNAc...) (Probable).
FT   CARBOHYD    146    146       N-linked (GlcNAc...).
FT   CARBOHYD    155    155       O-linked (GalNAc...) (Probable).
FT   CARBOHYD    162    162       O-linked (GalNAc...) (Probable).
FT   CARBOHYD    273    273       N-linked (GlcNAc...).
FT   CARBOHYD    304    304       N-linked (GlcNAc...).
FT   CARBOHYD    327    327       N-linked (GlcNAc...).
FT   CARBOHYD    330    330       N-linked (GlcNAc...).
FT   DISULFID     78     98
FT   DISULFID    216    283
FT   DISULFID    240    301
SQ   SEQUENCE   424 AA;  46304 MW;  9089903FBD268365 CRC64;
     MASSYFLFLC LLLCGGPELC NSQTLWLLPG GTPTPVGSSS PVKVECLEAE LVVTVSRDLF
     GTGKLVQPGD LTLGSEGCQP RVSVDTDVVR FNAQLHECSS RVQMTKDALV YSTFLLHDPR
     PVSGLSILRT NRVEVPIECR YPRQGNVSSH PIQPTWVPFR ATVSSEEKLA FSLRLMEENW
     NTEKSAPTFH LGEVAHLQAE VQTGSHLPLQ LFVDHCVATP SPLPDPNSSP YHFIVDFHGC
     LVDGLSESFS AFQVPRPRPE TLQFTVDVFH FANSSRNTLY ITCHLKVAPA NQIPDKLNKA
     CSFNKTSQSW LPVEGDADIC DCCSHGNCSN SSSSQFQIHG PRQWSKLVSR NRRHVTDEAD
     VTVGPLIFLG KANDQTVEGW TASAQTSVAL GLGLATVAFL TLAAIVLAVT RKCHSSSYLV
     SLPQ
//