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Protein

Zona pellucida sperm-binding protein 3

Gene

Zp3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The mammalian zona pellucida, which mediates species-specific sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy, is composed of three to four glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP3 is essential for sperm binding and zona matrix formation.

GO - Molecular functioni

  • acrosin binding Source: MGI
  • carbohydrate binding Source: UniProtKB
  • identical protein binding Source: MGI
  • receptor ligand activity Source: UniProtKB
  • structural constituent of egg coat Source: UniProtKB

GO - Biological processi

  • binding of sperm to zona pellucida Source: MGI
  • blastocyst formation Source: UniProtKB
  • egg coat formation Source: UniProtKB
  • humoral immune response mediated by circulating immunoglobulin Source: UniProtKB
  • negative regulation of binding of sperm to zona pellucida Source: MGI
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • oocyte development Source: UniProtKB
  • phosphatidylinositol-mediated signaling Source: UniProtKB
  • positive regulation of acrosomal vesicle exocytosis Source: UniProtKB
  • positive regulation of acrosome reaction Source: UniProtKB
  • positive regulation of antral ovarian follicle growth Source: UniProtKB
  • positive regulation of calcium ion import Source: UniProtKB
  • positive regulation of humoral immune response Source: UniProtKB
  • positive regulation of inflammatory response Source: UniProtKB
  • positive regulation of interferon-gamma production Source: UniProtKB
  • positive regulation of interleukin-4 production Source: UniProtKB
  • positive regulation of leukocyte migration Source: UniProtKB
  • positive regulation of ovarian follicle development Source: UniProtKB
  • positive regulation of phosphatidylinositol biosynthetic process Source: UniProtKB
  • positive regulation of T cell proliferation Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of type IV hypersensitivity Source: UniProtKB

Keywordsi

Molecular functionReceptor

Enzyme and pathway databases

ReactomeiR-MMU-1300644. Interaction With The Zona Pellucida.

Names & Taxonomyi

Protein namesi
Recommended name:
Zona pellucida sperm-binding protein 3
Alternative name(s):
Sperm receptor
Zona pellucida glycoprotein 3
Short name:
Zp-3
Zona pellucida protein C
Cleaved into the following chain:
Gene namesi
Name:Zp3
Synonyms:Zp-3, Zpc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:99215. Zp3.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini23 – 387ExtracellularAdd BLAST365
Transmembranei388 – 408HelicalSequence analysisAdd BLAST21
Topological domaini409 – 424CytoplasmicAdd BLAST16

Keywords - Cellular componenti

Cell membrane, Extracellular matrix, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi111Y → C: Reduces protein solubility and causes formation of an abnormal disulfide bond between C-111 and C-139 in approximately half of the molecules. 1 Publication1
Mutagenesisi111Y → F: Causes a mild reduction of protein solubility. 1 Publication1
Mutagenesisi111Y → L or V: Strongly reduces protein solubility. 1 Publication1
Mutagenesisi111Y → S: Reduces protein solubility. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 221 PublicationAdd BLAST22
ChainiPRO_000004171523 – 351Zona pellucida sperm-binding protein 3Add BLAST329
ChainiPRO_000030457223 – ?Processed zona pellucida sperm-binding protein 3
PropeptideiPRO_0000041716352 – 424Removed in mature form1 PublicationAdd BLAST73

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei23Pyrrolidone carboxylic acid1 Publication1
Glycosylationi32O-linked (GalNAc...) threonineCurated1
Glycosylationi34O-linked (GalNAc...) threonineCurated1
Glycosylationi39O-linked (GalNAc...) serineCurated1
Disulfide bondi46 ↔ 1391 Publication
Disulfide bondi78 ↔ 981 Publication
Glycosylationi146N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi155O-linked (GalNAc...) threonineCurated1
Glycosylationi162O-linked (GalNAc...) threonineCurated1
Disulfide bondi216 ↔ 2831 Publication
Disulfide bondi240 ↔ 3011 Publication
Glycosylationi273N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi304N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi327N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi330N-linked (GlcNAc...) asparagine1 Publication1

Post-translational modificationi

Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.
O-glycosylated; removal of O-linked glycans may play an important role in the post-fertilization block to polyspermy.1 Publication
Cys-320, Cys-322, Cys-323 and Cys-328 are involved in two additional disulfide bonds.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP10761.
PRIDEiP10761.

PTM databases

iPTMnetiP10761.
PhosphoSitePlusiP10761.
UniCarbKBiP10761.

Expressioni

Tissue specificityi

Oocytes.

Developmental stagei

Expressed during the 2-week growth phase of oogenesis, prior to ovulation.

Gene expression databases

BgeeiENSMUSG00000004948.
CleanExiMM_ZP3.
ExpressionAtlasiP10761. baseline and differential.
GenevisibleiP10761. MM.

Interactioni

Subunit structurei

Polymers of ZP2 and ZP3 organized into long filaments cross-linked by ZP1 homodimers.

GO - Molecular functioni

  • acrosin binding Source: MGI
  • identical protein binding Source: MGI
  • receptor ligand activity Source: UniProtKB

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000005073.

Structurei

Secondary structure

1424
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi42 – 46Combined sources5
Beta strandi48 – 58Combined sources11
Beta strandi60 – 63Combined sources4
Helixi68 – 70Combined sources3
Beta strandi71 – 75Combined sources5
Beta strandi81 – 84Combined sources4
Beta strandi86 – 94Combined sources9
Helixi95 – 98Combined sources4
Beta strandi100 – 104Combined sources5
Beta strandi106 – 117Combined sources12
Beta strandi133 – 142Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3D4CX-ray2.90A42-143[»]
3D4GX-ray2.30A/B/C/D/E/F/G/H42-143[»]
3EF7X-ray3.10A/B42-143[»]
5OSQX-ray2.05A/B42-143[»]
ProteinModelPortaliP10761.
SMRiP10761.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10761.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini45 – 308ZPPROSITE-ProRule annotationAdd BLAST264

Domaini

The ZP domain is involved in the polymerization of the ZP proteins to form the zona pellucida.

Sequence similaritiesi

Belongs to the ZP domain family. ZPC subfamily.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410II9V. Eukaryota.
ENOG410YXE1. LUCA.
GeneTreeiENSGT00530000063482.
HOGENOMiHOG000220813.
HOVERGENiHBG007985.
InParanoidiP10761.
KOiK19928.
OMAiNRRHVTE.
OrthoDBiEOG091G0AQ6.
PhylomeDBiP10761.
TreeFamiTF331369.

Family and domain databases

InterProiView protein in InterPro
IPR001507. ZP_dom.
IPR017977. ZP_dom_CS.
PfamiView protein in Pfam
PF00100. Zona_pellucida. 1 hit.
PRINTSiPR00023. ZPELLUCIDA.
SMARTiView protein in SMART
SM00241. ZP. 1 hit.
PROSITEiView protein in PROSITE
PS00682. ZP_1. 1 hit.
PS51034. ZP_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P10761-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSYFLFLC LLLCGGPELC NSQTLWLLPG GTPTPVGSSS PVKVECLEAE
60 70 80 90 100
LVVTVSRDLF GTGKLVQPGD LTLGSEGCQP RVSVDTDVVR FNAQLHECSS
110 120 130 140 150
RVQMTKDALV YSTFLLHDPR PVSGLSILRT NRVEVPIECR YPRQGNVSSH
160 170 180 190 200
PIQPTWVPFR ATVSSEEKLA FSLRLMEENW NTEKSAPTFH LGEVAHLQAE
210 220 230 240 250
VQTGSHLPLQ LFVDHCVATP SPLPDPNSSP YHFIVDFHGC LVDGLSESFS
260 270 280 290 300
AFQVPRPRPE TLQFTVDVFH FANSSRNTLY ITCHLKVAPA NQIPDKLNKA
310 320 330 340 350
CSFNKTSQSW LPVEGDADIC DCCSHGNCSN SSSSQFQIHG PRQWSKLVSR
360 370 380 390 400
NRRHVTDEAD VTVGPLIFLG KANDQTVEGW TASAQTSVAL GLGLATVAFL
410 420
TLAAIVLAVT RKCHSSSYLV SLPQ
Length:424
Mass (Da):46,304
Last modified:November 1, 1997 - v4
Checksum:i9089903FBD268365
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20026 mRNA. Translation: AAB18629.1.
X14376 Genomic DNA. Translation: CAA32550.1.
BC099465 mRNA. Translation: AAH99465.1.
BC100745 mRNA. Translation: AAI00746.1.
BC103583 mRNA. Translation: AAI03584.1.
BC103584 mRNA. Translation: AAI03585.1.
BC103585 mRNA. Translation: AAI03586.1.
CCDSiCCDS19749.1.
PIRiA30334.
RefSeqiNP_035906.1. NM_011776.1.
UniGeneiMm.1381.

Genome annotation databases

EnsembliENSMUST00000005073; ENSMUSP00000005073; ENSMUSG00000004948.
GeneIDi22788.
KEGGimmu:22788.
UCSCiuc008zzl.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiZP3_MOUSE
AccessioniPrimary (citable) accession number: P10761
Secondary accession number(s): Q4FZI2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1997
Last modified: November 22, 2017
This is version 147 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  4. SIMILARITY comments
    Index of protein domains and families