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Protein

Zona pellucida sperm-binding protein 2

Gene

Zp2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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. ZP2 may act as a secondary sperm receptor.1 Publication

GO - Molecular functioni

GO - Biological processi

  • binding of sperm to zona pellucida Source: UniProtKB
  • prevention of polyspermy Source: UniProtKB

Keywordsi

Molecular functionReceptor
Biological processFertilization

Enzyme and pathway databases

ReactomeiR-MMU-1300644 Interaction With The Zona Pellucida

Names & Taxonomyi

Protein namesi
Recommended name:
Zona pellucida sperm-binding protein 2
Alternative name(s):
Zona pellucida glycoprotein 2
Short name:
Zp-2
Zona pellucida protein A
Cleaved into the following chain:
Gene namesi
Name:Zp2
Synonyms:Zp-2, Zpa
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:99214 Zp2

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 domaini35 – 683ExtracellularAdd BLAST649
Transmembranei684 – 703HelicalSequence analysisAdd BLAST20
Topological domaini704 – 713Cytoplasmic10

Keywords - Cellular componenti

Cell membrane, Extracellular matrix, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi634 – 635KR → NA: Abolishes proteolytic cleavage of the propeptide. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 342 PublicationsAdd BLAST34
ChainiPRO_000004169335 – 633Zona pellucida sperm-binding protein 2Add BLAST599
ChainiPRO_000030456135 – ?Processed zona pellucida sperm-binding protein 2
PropeptideiPRO_0000041694634 – 713Removed in mature form1 Publication1 PublicationAdd BLAST80

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi51 ↔ 134Combined sources1 Publication
Glycosylationi83N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi84 ↔ 102Combined sources2 Publications
Glycosylationi172N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi184N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi217N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi264N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi365 ↔ 4581 Publication
Glycosylationi393N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi396 ↔ 4171 Publication
Glycosylationi455O-linked (GalNAc...) threonineCurated1
Disulfide bondi538 ↔ 608Combined sources1 Publication
Disulfide bondi559 ↔ 627Combined sources1 Publication
Disulfide bondi613 ↔ 623Combined sources1 Publication

Post-translational modificationi

Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.2 Publications
Proteolytically cleaved in the N-terminal part by the metalloendopeptidase ASTL exocytosed from cortical granules after fertilization, yielding a N-terminal peptide of about 30 kDa which remains covalently attached to the C-terminal peptide via disulfide bond(s). This cleavage may play an important role in the post-fertilization block to polyspermy. Additional proteolytically cleavage of the N-terminal peptide of 30 kDa occurs in one-cell and two-cell embryos.1 Publication
N-glycosylated.1 Publication
O-glycosylated; contains sulfate-substituted glycans.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei167 – 168Cleavage; by ASTL1 Publication2
Sitei633 – 634Cleavage1 Publication1 Publication2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP20239
PaxDbiP20239
PRIDEiP20239

PTM databases

GlyConnecti630
635
iPTMnetiP20239
PhosphoSitePlusiP20239
UniCarbKBiP20239

Miscellaneous databases

PMAP-CutDBiP20239

Expressioni

Tissue specificityi

Detected in the zona pellucida that surrounds the oocyte (at protein level) (PubMed:12799386, PubMed:3845123, PubMed:17559063). Oocyte.1 Publication

Developmental stagei

Expressed during the 2-week growth phase of oogenesis, prior to ovulation.1 Publication

Gene expression databases

BgeeiENSMUSG00000030911 Expressed in 22 organ(s), highest expression level in primary oocyte
CleanExiMM_ZP2
ExpressionAtlasiP20239 baseline and differential
GenevisibleiP20239 MM

Interactioni

Subunit structurei

Can form homopolymers that assemble into long fibers (in vitro) (PubMed:17559063). Polymers of ZP2 and ZP3 organized into long filaments cross-linked by ZP1 homodimers (PubMed:3845123). Interacts with ZP3 (By similarity).By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204708, 1 interactor
STRINGi10090.ENSMUSP00000033207

Structurei

Secondary structure

1713
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP20239
SMRiP20239
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini364 – 630ZPPROSITE-ProRule annotationAdd BLAST267

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni462 – 484Disordered1 PublicationAdd BLAST23

Domaini

The ZP domain is involved in the polymerization of the ZP proteins to form the zona pellucida.1 Publication

Sequence similaritiesi

Belongs to the ZP domain family. ZPA subfamily.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IHBM Eukaryota
ENOG4110GZY LUCA
GeneTreeiENSGT00530000063096
HOGENOMiHOG000059563
HOVERGENiHBG004379
InParanoidiP20239
KOiK19927
OrthoDBiEOG091G02TE
PhylomeDBiP20239
TreeFamiTF332794

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

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P20239-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MARWQRKASV SSPCGRSIYR FLSLLFTLVT SVNSVSLPQS ENPAFPGTLI
60 70 80 90 100
CDKDEVRIEF SSRFDMEKWN PSVVDTLGSE ILNCTYALDL ERFVLKFPYE
110 120 130 140 150
TCTIKVVGGY QVNIRVGDTT TDVRYKDDMY HFFCPAIQAE THEISEIVVC
160 170 180 190 200
RRDLISFSFP QLFSRLADEN QNVSEMGWIV KIGNGTRAHI LPLKDAIVQG
210 220 230 240 250
FNLLIDSQKV TLHVPANATG IVHYVQESSY LYTVQLELLF STTGQKIVFS
260 270 280 290 300
SHAICAPDLS VACNATHMTL TIPEFPGKLE SVDFGQWSIP EDQWHANGID
310 320 330 340 350
KEATNGLRLN FRKSLLKTKP SEKCPFYQFY LSSLKLTFYF QGNMLSTVID
360 370 380 390 400
PECHCESPVS IDELCAQDGF MDFEVYSHQT KPALNLDTLL VGNSSCQPIF
410 420 430 440 450
KVQSVGLARF HIPLNGCGTR QKFEGDKVIY ENEIHALWEN PPSNIVFRNS
460 470 480 490 500
EFRMTVRCYY IRDSMLLNAH VKGHPSPEAF VKPGPLVLVL QTYPDQSYQR
510 520 530 540 550
PYRKDEYPLV RYLRQPIYME VKVLSRNDPN IKLVLDDCWA TSSEDPASAP
560 570 580 590 600
QWQIVMDGCE YELDNYRTTF HPAGSSAAHS GHYQRFDVKT FAFVSEARGL
610 620 630 640 650
SSLIYFHCSA LICNQVSLDS PLCSVTCPAS LRSKREANKE DTMTVSLPGP
660 670 680 690 700
ILLLSDVSSS KGVDPSSSEI TKDIIAKDIA SKTLGAVAAL VGSAVILGFI
710
CYLYKKRTIR FNH
Length:713
Mass (Da):80,210
Last modified:February 1, 1991 - v1
Checksum:iDCF9AE6CCD3461EF
GO

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q3UX44Q3UX44_MOUSE
Zona pellucida sperm-binding protei...
Zp2
676Annotation score:
A0A140LIR5A0A140LIR5_MOUSE
Zona pellucida sperm-binding protei...
Zp2
428Annotation score:

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34148 mRNA Translation: AAA40586.1
CCDSiCCDS21792.1
PIRiA34782
RefSeqiNP_035905.1, NM_011775.7
UniGeneiMm.6510

Genome annotation databases

EnsembliENSMUST00000033207; ENSMUSP00000033207; ENSMUSG00000030911
GeneIDi22787
KEGGimmu:22787
UCSCiuc009jmi.1 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34148 mRNA Translation: AAA40586.1
CCDSiCCDS21792.1
PIRiA34782
RefSeqiNP_035905.1, NM_011775.7
UniGeneiMm.6510

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5BUPX-ray2.25A463-664[»]
5II6X-ray0.95A35-138[»]
ProteinModelPortaliP20239
SMRiP20239
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204708, 1 interactor
STRINGi10090.ENSMUSP00000033207

PTM databases

GlyConnecti630
635
iPTMnetiP20239
PhosphoSitePlusiP20239
UniCarbKBiP20239

Proteomic databases

MaxQBiP20239
PaxDbiP20239
PRIDEiP20239

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033207; ENSMUSP00000033207; ENSMUSG00000030911
GeneIDi22787
KEGGimmu:22787
UCSCiuc009jmi.1 mouse

Organism-specific databases

CTDi7783
MGIiMGI:99214 Zp2

Phylogenomic databases

eggNOGiENOG410IHBM Eukaryota
ENOG4110GZY LUCA
GeneTreeiENSGT00530000063096
HOGENOMiHOG000059563
HOVERGENiHBG004379
InParanoidiP20239
KOiK19927
OrthoDBiEOG091G02TE
PhylomeDBiP20239
TreeFamiTF332794

Enzyme and pathway databases

ReactomeiR-MMU-1300644 Interaction With The Zona Pellucida

Miscellaneous databases

PMAP-CutDBiP20239
PROiPR:P20239
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000030911 Expressed in 22 organ(s), highest expression level in primary oocyte
CleanExiMM_ZP2
ExpressionAtlasiP20239 baseline and differential
GenevisibleiP20239 MM

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
ProtoNetiSearch...

Entry informationi

Entry nameiZP2_MOUSE
AccessioniPrimary (citable) accession number: P20239
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 7, 2018
This is version 138 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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