ZP3_MOUSE
ID ZP3_MOUSE Reviewed; 424 AA.
AC P10761; Q4FZI2;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 4.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Zona pellucida sperm-binding protein 3;
DE AltName: Full=Sperm receptor;
DE AltName: Full=Zona pellucida glycoprotein 3;
DE Short=Zp-3;
DE AltName: Full=Zona pellucida protein C;
DE Contains:
DE RecName: Full=Processed zona pellucida sperm-binding protein 3;
DE Flags: Precursor;
GN Name=Zp3; Synonyms=Zp-3, Zpc;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX 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 the
RT 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 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 ZP3
RT -- the mouse sperm receptor.";
RL Nucleic Acids Res. 17:2861-2863(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2842770; DOI=10.1073/pnas.85.17.6409;
RA Kinloch R.A., Roller R.J., Fimiani C.M., Wassarman D.A., Wassarman P.M.;
RT "Primary structure of the mouse sperm receptor polypeptide determined by
RT genomic cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:6409-6413(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 49-63; 197-204; 219-233 AND 261-275.
RC STRAIN=CD-1;
RX 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 that
RT possesses sperm receptor activity.";
RL Dev. Biol. 154:309-317(1992).
RN [7]
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 AND
RP ASN-330, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX 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 using
RT mass spectrometry.";
RL J. Biol. Chem. 278:34189-34202(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 42-143, IDENTIFICATION BY MASS
RP SPECTROMETRY, MUTAGENESIS OF TYR-111, SUBCELLULAR LOCATION, AND DISULFIDE
RP BONDS.
RX PubMed=19052627; DOI=10.1038/nature07599;
RA Monne M., Han L., Schwend T., Burendahl S., Jovine L.;
RT "Crystal structure of the ZP-N domain of ZP3 reveals the core fold of
RT animal egg coats.";
RL Nature 456:653-657(2008).
CC -!- FUNCTION: Component of the zona pellucida, an extracellular matrix
CC surrounding oocytes which mediates sperm binding, induction of the
CC acrosome reaction and prevents post-fertilization polyspermy. The zona
CC pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4.
CC ZP3 is essential for sperm binding and zona matrix formation.
CC -!- SUBUNIT: Polymers of ZP2 and ZP3 organized into long filaments cross-
CC linked by ZP1 homodimers. Interacts with ZP1 and ZP2.
CC {ECO:0000250|UniProtKB:P20239, ECO:0000250|UniProtKB:P21754}.
CC -!- SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein
CC 3]: Zona pellucida {ECO:0000269|PubMed:19052627}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19052627};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in 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 yield
CC the secreted ectodomain incorporated in the zona pellucida.
CC -!- PTM: O-glycosylated; removal of O-linked glycans may play an important
CC role in the post-fertilization block to polyspermy.
CC {ECO:0000269|PubMed:12799386}.
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 {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Molecular chastity - Issue
CC 93 of April 2008;
CC URL="https://web.expasy.org/spotlight/back_issues/093";
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DR EMBL; M20026; AAB18629.1; -; mRNA.
DR EMBL; X14376; CAA32550.1; -; Genomic_DNA.
DR EMBL; BC099465; AAH99465.1; -; mRNA.
DR EMBL; BC100745; AAI00746.1; -; mRNA.
DR EMBL; BC103583; AAI03584.1; -; mRNA.
DR EMBL; BC103584; AAI03585.1; -; mRNA.
DR EMBL; BC103585; AAI03586.1; -; mRNA.
DR CCDS; CCDS19749.1; -.
DR PIR; A30334; A30334.
DR RefSeq; NP_035906.1; NM_011776.1.
DR PDB; 3D4C; X-ray; 2.90 A; A=42-143.
DR PDB; 3D4G; X-ray; 2.30 A; A/B/C/D/E/F/G/H=42-143.
DR PDB; 3EF7; X-ray; 3.10 A; A/B=42-143.
DR PDB; 5OSQ; X-ray; 2.05 A; A/B=42-143.
DR PDBsum; 3D4C; -.
DR PDBsum; 3D4G; -.
DR PDBsum; 3EF7; -.
DR PDBsum; 5OSQ; -.
DR AlphaFoldDB; P10761; -.
DR SMR; P10761; -.
DR STRING; 10090.ENSMUSP00000005073; -.
DR GlyConnect; 633; 15 O-Linked glycans.
DR GlyConnect; 635; 24 N-Linked glycans, 10 O-Linked glycans.
DR GlyGen; P10761; 11 sites, 48 N-linked glycans (1 site), 34 O-linked glycans (1 site).
DR iPTMnet; P10761; -.
DR PhosphoSitePlus; P10761; -.
DR PaxDb; P10761; -.
DR PRIDE; P10761; -.
DR ProteomicsDB; 275314; -.
DR ABCD; P10761; 22 sequenced antibodies.
DR Antibodypedia; 29359; 106 antibodies from 17 providers.
DR DNASU; 22788; -.
DR Ensembl; ENSMUST00000005073; ENSMUSP00000005073; ENSMUSG00000004948.
DR GeneID; 22788; -.
DR KEGG; mmu:22788; -.
DR UCSC; uc008zzl.1; mouse.
DR CTD; 7784; -.
DR MGI; MGI:99215; Zp3.
DR VEuPathDB; HostDB:ENSMUSG00000004948; -.
DR eggNOG; ENOG502QSZF; Eukaryota.
DR GeneTree; ENSGT01030000234567; -.
DR HOGENOM; CLU_047091_1_1_1; -.
DR InParanoid; P10761; -.
DR OMA; ECHYPRH; -.
DR OrthoDB; 495227at2759; -.
DR PhylomeDB; P10761; -.
DR TreeFam; TF331369; -.
DR Reactome; R-MMU-2534343; Interaction With Cumulus Cells And The Zona Pellucida.
DR BioGRID-ORCS; 22788; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Zp3; mouse.
DR EvolutionaryTrace; P10761; -.
DR PRO; PR:P10761; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P10761; protein.
DR Bgee; ENSMUSG00000004948; Expressed in primary oocyte and 18 other tissues.
DR ExpressionAtlas; P10761; baseline and differential.
DR Genevisible; P10761; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB.
DR GO; GO:0035805; C:egg coat; ISS:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032190; F:acrosin binding; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0048018; F:receptor ligand activity; IDA:UniProtKB.
DR GO; GO:0035804; F:structural constituent of egg coat; IMP:UniProtKB.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IDA:MGI.
DR GO; GO:0001825; P:blastocyst formation; IMP:UniProtKB.
DR GO; GO:0035803; P:egg coat formation; IMP:UniProtKB.
DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0048599; P:oocyte development; IMP:UniProtKB.
DR GO; GO:2000368; P:positive regulation of acrosomal vesicle exocytosis; ISS:UniProtKB.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; IDA:UniProtKB.
DR GO; GO:2000388; P:positive regulation of antral ovarian follicle growth; IMP:UniProtKB.
DR GO; GO:0002922; P:positive regulation of humoral immune response; ISS:UniProtKB.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IDA:UniProtKB.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:UniProtKB.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; IDA:UniProtKB.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; IDA:UniProtKB.
DR GO; GO:2000386; P:positive regulation of ovarian follicle development; IDA:UniProtKB.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0001809; P:positive regulation of type IV hypersensitivity; IDA:UniProtKB.
DR GO; GO:0010469; P:regulation of signaling receptor activity; IDA:UniProtKB.
DR DisProt; DP02586; -.
DR Gene3D; 2.60.40.4100; -; 1.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR040196; ZP3.
DR InterPro; IPR001507; ZP_dom.
DR InterPro; IPR017977; ZP_dom_CS.
DR PANTHER; PTHR11576:SF2; PTHR11576:SF2; 1.
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 3D-structure; Cell membrane; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Membrane; Pyrrolidone carboxylic acid; Receptor;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:12799386"
FT CHAIN 23..351
FT /note="Zona pellucida sperm-binding protein 3"
FT /id="PRO_0000041715"
FT CHAIN 23..?
FT /note="Processed zona pellucida sperm-binding protein 3"
FT /id="PRO_0000304572"
FT PROPEP 352..424
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:12799386"
FT /id="PRO_0000041716"
FT TOPO_DOM 23..387
FT /note="Extracellular"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..424
FT /note="Cytoplasmic"
FT DOMAIN 45..308
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT MOD_RES 23
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:12799386"
FT CARBOHYD 32
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 34
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 39
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000305"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12799386"
FT CARBOHYD 155
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 162
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12799386"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12799386"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12799386"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12799386"
FT DISULFID 46..139
FT /evidence="ECO:0000269|PubMed:19052627"
FT DISULFID 78..98
FT /evidence="ECO:0000269|PubMed:12799386"
FT DISULFID 216..283
FT /evidence="ECO:0000269|PubMed:12799386"
FT DISULFID 240..301
FT /evidence="ECO:0000269|PubMed:12799386"
FT MUTAGEN 111
FT /note="Y->C: Reduces protein solubility and causes
FT formation of an abnormal disulfide bond between C-111 and
FT C-139 in approximately half of the molecules."
FT /evidence="ECO:0000269|PubMed:19052627"
FT MUTAGEN 111
FT /note="Y->F: Causes a mild reduction of protein
FT solubility."
FT /evidence="ECO:0000269|PubMed:19052627"
FT MUTAGEN 111
FT /note="Y->L,V: Strongly reduces protein solubility."
FT /evidence="ECO:0000269|PubMed:19052627"
FT MUTAGEN 111
FT /note="Y->S: Reduces protein solubility."
FT /evidence="ECO:0000269|PubMed:19052627"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:5OSQ"
FT STRAND 48..58
FT /evidence="ECO:0007829|PDB:5OSQ"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:5OSQ"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:5OSQ"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:5OSQ"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:5OSQ"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:5OSQ"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:5OSQ"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:5OSQ"
FT STRAND 106..117
FT /evidence="ECO:0007829|PDB:5OSQ"
FT STRAND 133..142
FT /evidence="ECO:0007829|PDB:5OSQ"
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
