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Protein

Zona pellucida sperm-binding protein 2

Gene

Zp2

Organism
Rattus norvegicus (Rat)
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. ZP2 may act as a secondary sperm receptor.By similarity

GO - Biological processi

  • binding of sperm to zona pellucida Source: UniProtKB
  • intracellular protein transport Source: UniProtKB
  • prevention of polyspermy Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Fertilization

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:Zpa
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620605. Zp2.

Subcellular locationi

Processed zona pellucida sperm-binding protein 2 :
  • Secretedextracellular spaceextracellular matrix By similarity

  • Note: The glycoproteinaceous translucent extracellular matrix that surrounds the mammalian oocyte is called zona pellucida.By similarity
  • Cell membrane By similarity; Single-pass type I membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 664640ExtracellularSequence analysisAdd
BLAST
Transmembranei665 – 68521HelicalSequence analysisAdd
BLAST
Topological domaini686 – 69510CytoplasmicSequence analysis

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Extracellular matrix, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 PublicationAdd
BLAST
Chaini25 – 619595Zona pellucida sperm-binding protein 2PRO_0000041699Add
BLAST
Chaini25 – ?Processed zona pellucida sperm-binding protein 2PRO_0000304564
Propeptidei620 – 69576Removed in mature formBy similarityPRO_0000041700Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi72 – 721N-linked (GlcNAc...); partial1 Publication
Disulfide bondi73 ↔ 911 Publication
Glycosylationi161 – 1611N-linked (GlcNAc...); partial1 Publication
Glycosylationi173 – 1731N-linked (GlcNAc...)1 Publication
Glycosylationi206 – 2061N-linked (GlcNAc...)1 Publication
Glycosylationi253 – 2531N-linked (GlcNAc...)1 Publication
Disulfide bondi354 ↔ 4471 Publication
Glycosylationi382 – 3821N-linked (GlcNAc...)1 Publication
Disulfide bondi385 ↔ 4061 Publication
Glycosylationi444 – 4441O-linked (GalNAc...)By similarity
Disulfide bondi527 ↔ 597By similarity
Disulfide bondi548 ↔ 613By similarity
Glycosylationi563 – 5631N-linked (GlcNAc...)1 Publication
Disulfide bondi602 ↔ 609By similarity

Post-translational modificationi

Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.By similarity
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.By similarity
N-glycosylated.By similarity
O-glycosylated; contains sulfate-substituted glycans.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei156 – 1572Cleavage; by ASTLBy similarity
Sitei619 – 6202CleavageBy similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO54767.
PRIDEiO54767.

Expressioni

Tissue specificityi

Oocytes.1 Publication

Interactioni

Subunit structurei

Can form homopolymers that assemble into long fibers (in vitro). Polymers of ZP2 and ZP3 organized into long filaments cross-linked by ZP1 homodimers.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000064370.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini353 – 616264ZPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni451 – 47323DisorderedBy similarityAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the ZP domain family. ZPA subfamily.Curated
Contains 1 ZP domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IHBM. Eukaryota.
ENOG4110GZY. LUCA.
HOVERGENiHBG004379.
InParanoidiO54767.
KOiK19927.
PhylomeDBiO54767.

Family and domain databases

InterProiIPR001507. ZP_dom.
IPR017977. ZP_dom_CS.
[Graphical view]
PfamiPF00100. Zona_pellucida. 1 hit.
[Graphical view]
PRINTSiPR00023. ZPELLUCIDA.
SMARTiSM00241. ZP. 1 hit.
[Graphical view]
PROSITEiPS00682. ZP_1. 1 hit.
PS51034. ZP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O54767-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARWQRVYWL RSLFFALVTS VNSLSLPQSE NPAFPGTLIC DKDEVRVEFS
60 70 80 90 100
SRFDMEKWNP SLVDTFGNEI SNCTYALDLE KFILKFPYET CTIKVIGGYQ
110 120 130 140 150
VNIRVQDTNA DVSYKDDVHH FFCPAIQAEI HEVSEIVVCM EDLISFSFPQ
160 170 180 190 200
LFSRLADENQ NVSEMGWIIK IGNGTRVHTL PLKDAIVQGF NLLIDSQKIT
210 220 230 240 250
LHVPANATGV AHYVQESSYL YTVQLKLLFS SPGQKITFSS QAICAPDLSV
260 270 280 290 300
ACNVTHMSLT IPEFPGKLKS VGFGQRNIPE DQWHANGIDK EATNGLRLHF
310 320 330 340 350
RKSLLKTKPS EKCPFYQFYF SSLELTFNFQ GDMLSTVIDP ECHCESPVSI
360 370 380 390 400
DELCTRDGFM DFEVYSHQTK PALNLESLLV GNSSCQPIFK VQSLGLARFH
410 420 430 440 450
IPLNGCGTRQ KFEGDKVIYE NEIHALWENP PSNIIFRNSE FRMTVRCHYI
460 470 480 490 500
RDSMLLRAHI KSHSSPVASV KPGPLALVLQ TYPDISYQRP YRKNEYPLVR
510 520 530 540 550
YLRQPIYMEV TVLNRNDPNI KLVLDDCWAT TFEDPASVPQ WQIIMDGCEY
560 570 580 590 600
ELDNYRTTFH AANSSAAHSG HYQRFDVKTF AFVSESRGLS SLIYFHCSAL
610 620 630 640 650
ICNQASPLCS VTCPAPLRNK REASKEGTMT VSLPGPIILL SDDSSSKGVM
660 670 680 690
NPDSYEITKD IASKTLGAVA ALVGSAVIIG FICYLHKKRI VRFNS
Length:695
Mass (Da):78,444
Last modified:June 1, 1998 - v1
Checksum:iB1660D35C01D1635
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB000929 mRNA. Translation: BAA24487.1.
RefSeqiNP_112412.1. NM_031150.1.
UniGeneiRn.10891.

Genome annotation databases

GeneIDi81828.
KEGGirno:81828.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB000929 mRNA. Translation: BAA24487.1.
RefSeqiNP_112412.1. NM_031150.1.
UniGeneiRn.10891.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000064370.

Proteomic databases

PaxDbiO54767.
PRIDEiO54767.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi81828.
KEGGirno:81828.

Organism-specific databases

CTDi7783.
RGDi620605. Zp2.

Phylogenomic databases

eggNOGiENOG410IHBM. Eukaryota.
ENOG4110GZY. LUCA.
HOVERGENiHBG004379.
InParanoidiO54767.
KOiK19927.
PhylomeDBiO54767.

Miscellaneous databases

PROiO54767.

Family and domain databases

InterProiIPR001507. ZP_dom.
IPR017977. ZP_dom_CS.
[Graphical view]
PfamiPF00100. Zona_pellucida. 1 hit.
[Graphical view]
PRINTSiPR00023. ZPELLUCIDA.
SMARTiSM00241. ZP. 1 hit.
[Graphical view]
PROSITEiPS00682. ZP_1. 1 hit.
PS51034. ZP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiZP2_RAT
AccessioniPrimary (citable) accession number: O54767
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 1998
Last modified: June 8, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.