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Protein

Zona pellucida sperm-binding protein 3

Gene

Zp3

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. ZP3 is essential for sperm binding and zona matrix formation.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Fertilization

Names & Taxonomyi

Protein namesi
Recommended name:
Zona pellucida sperm-binding protein 3
Alternative name(s):
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620606. Zp3.

Subcellular locationi

Processed zona pellucida sperm-binding protein 3 :
  • Secretedextracellular spaceextracellular matrix By similarity

  • Note: The glycoproteinaceous translucent extracellular matrix that surrounds the mammalian oocyte is called zona pellucida.Curated

Topology

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Extracellular matrix, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22By similarityAdd BLAST22
ChainiPRO_000004172123 – 351Zona pellucida sperm-binding protein 3Add BLAST329
ChainiPRO_000030457523 – ?Processed zona pellucida sperm-binding protein 3
PropeptideiPRO_0000041722352 – 424Removed in mature form1 PublicationAdd BLAST73

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei23Pyrrolidone carboxylic acid1 Publication1
Glycosylationi32O-linked (GalNAc...)By similarity1
Glycosylationi34O-linked (GalNAc...)By similarity1
Glycosylationi39O-linked (GalNAc...)By similarity1
Disulfide bondi46 ↔ 139By similarity
Disulfide bondi78 ↔ 981 Publication
Glycosylationi146N-linked (GlcNAc...)1 Publication1
Glycosylationi155O-linked (GalNAc...)By similarity1
Glycosylationi162O-linked (GalNAc...)By similarity1
Disulfide bondi216 ↔ 2831 Publication
Disulfide bondi240 ↔ 3011 Publication
Glycosylationi273N-linked (GlcNAc...)1 Publication1
Glycosylationi304N-linked (GlcNAc...)1 Publication1
Glycosylationi327N-linked (GlcNAc...)By similarity1
Glycosylationi330N-linked (GlcNAc...)1 Publication1

Post-translational modificationi

Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.
N-glycosylated; N-linked glycans are of high mannose/hybrid type, as well as bi-, tri- and tetra-antennary complex types.
O-glycosylated; removal of O-linked glycans may play an important role in the post-fertilization block to polyspermy.

Keywords - PTMi

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

Proteomic databases

PaxDbiP97708.
PRIDEiP97708.

Expressioni

Tissue specificityi

Oocytes.

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001952.

Structurei

3D structure databases

ProteinModelPortaliP97708.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi329 – 334Poly-Ser6

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
Contains 1 ZP domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410II9V. Eukaryota.
ENOG410YXE1. LUCA.
HOGENOMiHOG000220813.
HOVERGENiHBG007985.
InParanoidiP97708.
KOiK19928.
PhylomeDBiP97708.

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.

P97708-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPSCLLFLC LLLCGGPELC YPQTQWLLPG GTPTPAGSSS PVEVECKEAE
60 70 80 90 100
LVVTVRRDLF GTGKLVQPGD LTLGSEGCQP LVAVDTDVVR LNAQLHECSS
110 120 130 140 150
GVQVTEDALV YNTFLLHDPR PVNGLSILRT NRVEVPIECR YPRQGNVSSH
160 170 180 190 200
PIQPTWVPFS ATVSSEEKLA FSLRLMEEDW NTEKSSPTFH LGEVAHLQAE
210 220 230 240 250
VQTGSHLPLQ LFVDHCVATP SPLPGQNSSP HHFIVDSHGC LVDGLSESFS
260 270 280 290 300
AFQVPRPRPE TLQFTVDVFH FANSSRNTVY ITCHLKVAPA NQIPDKLNKA
310 320 330 340 350
CSFNKTSQSW LPVEGDADIC DCCSNGNCSN SSSSEFETHE PAQWSTLVSR
360 370 380 390 400
NRRHVTDEAD VTVGPLIFLG KANDQAVEGW TSSAQTSVAL GLGLATVAFL
410 420
TLAAIVLGVT RKCHTSSYLV SLPQ
Length:424
Mass (Da):45,901
Last modified:June 1, 1998 - v2
Checksum:i2AB42CBB14DE8701
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti55V → A in BAA24456 (PubMed:9820205).Curated1
Sequence conflicti112N → S in BAA24456 (PubMed:9820205).Curated1
Sequence conflicti412K → M in BAA24456 (PubMed:9820205).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10823 mRNA. Translation: CAA71787.1.
D78482 mRNA. Translation: BAA24456.1.
RefSeqiNP_446214.1. NM_053762.1.
UniGeneiRn.10892.

Genome annotation databases

GeneIDi114639.
KEGGirno:114639.
UCSCiRGD:620606. rat.

Cross-referencesi

Web resourcesi

Protein Spotlight

Molecular chastity - Issue 93 of April 2008

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10823 mRNA. Translation: CAA71787.1.
D78482 mRNA. Translation: BAA24456.1.
RefSeqiNP_446214.1. NM_053762.1.
UniGeneiRn.10892.

3D structure databases

ProteinModelPortaliP97708.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001952.

Proteomic databases

PaxDbiP97708.
PRIDEiP97708.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi114639.
KEGGirno:114639.
UCSCiRGD:620606. rat.

Organism-specific databases

CTDi7784.
RGDi620606. Zp3.

Phylogenomic databases

eggNOGiENOG410II9V. Eukaryota.
ENOG410YXE1. LUCA.
HOGENOMiHOG000220813.
HOVERGENiHBG007985.
InParanoidiP97708.
KOiK19928.
PhylomeDBiP97708.

Miscellaneous databases

PROiP97708.

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 nameiZP3_RAT
AccessioniPrimary (citable) accession number: P97708
Secondary accession number(s): O55084
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 1998
Last modified: July 6, 2016
This is version 102 of the entry and version 2 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  2. 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.