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Protein

Zona pellucida sperm-binding protein 3

Gene

ZP3

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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):
Sperm receptor
Zona pellucida glycoprotein 3
Short name:
Zp-3
Zona pellucida protein C
Cleaved into the following chain:
Gene namesi
Name:ZP3
Synonyms:ZPC
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Subcellular locationi

Processed zona pellucida sperm-binding protein 3 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 386364ExtracellularSequence AnalysisAdd
BLAST
Transmembranei387 – 40721HelicalSequence AnalysisAdd
BLAST
Topological domaini408 – 42215CytoplasmicSequence AnalysisAdd
BLAST

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 – 2222By similarityAdd
BLAST
Chaini23 – 349327Zona pellucida sperm-binding protein 3PRO_0000041713Add
BLAST
Chaini23 – ?Processed zona pellucida sperm-binding protein 3PRO_0000304571
Propeptidei350 – 42273Removed in mature formBy similarityPRO_0000041714Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231Pyrrolidone carboxylic acidBy similarity
Glycosylationi32 – 321O-linked (GalNAc...)By similarity
Glycosylationi34 – 341O-linked (GalNAc...)By similarity
Disulfide bondi46 ↔ 139By similarity
Disulfide bondi78 ↔ 98By similarity
Glycosylationi146 – 1461N-linked (GlcNAc...)By similarity
Glycosylationi155 – 1551O-linked (GalNAc...)By similarity
Glycosylationi161 – 1611O-linked (GalNAc...)By similarity
Glycosylationi162 – 1621O-linked (GalNAc...)By similarity
Disulfide bondi216 ↔ 281By similarity
Disulfide bondi238 ↔ 299By similarity
Glycosylationi271 – 2711N-linked (GlcNAc...)By similarity
Glycosylationi302 – 3021N-linked (GlcNAc...)By similarity

Post-translational modificationi

Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.
N-glycosylated.By similarity
O-glycosylated; removal of O-linked glycans may play an important role in the post-fertilization block to polyspermy.By similarity

Keywords - PTMi

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

Expressioni

Tissue specificityi

Oocytes.

Developmental stagei

Growing oocytes.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP23491.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 306262ZPPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi119 – 15840Pro-richAdd
BLAST
Compositional biasi208 – 25750Pro-richAdd
BLAST

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

HOVERGENiHBG007985.

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.

P23491-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLSYQLLLC LLLCGGAKQC CSQPLWLLPG GTPTPGKLTS SVEVECLEAE
60 70 80 90 100
LVVTVSRDLF GTGKLIQPED LTLGSENCRP LVSVATDVVR FKAQLHECSN
110 120 130 140 150
RVQVTEDALV YSTVLLHQPR PVPGLSILRT NRADVPIECR YPRQGNVSSH
160 170 180 190 200
AIRPTWVPFS TTVSSEEKLV FSLRLMEENW NTEKLSPTSH LGEVAYLQAE
210 220 230 240 250
VQTGSHLPLL LFVDRCVPTP SPDQTASPYH VIVDFHGCLV DGLSESFSAF
260 270 280 290 300
QVPRPRPETL QFTVDVFHFA NSSRNTIYIT CHLKVTPANQ TPDELNKACS
310 320 330 340 350
FNRSSKSWSP VEGDAEVCGC CSSGDCGSSS RSRYQAHGVS QWPKSASRRR
360 370 380 390 400
RHVRDEADVT VGPLIFLGKA SDQAVEGWAS SAQTSLALGL GLAAVAFLTL
410 420
AAIVLGVTRS CHTPSHVVSL SQ
Length:422
Mass (Da):45,827
Last modified:February 1, 1996 - v2
Checksum:iD0F95BE7FF8E7E01
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63629 mRNA. Translation: AAA37079.1.
PIRiA60503.
RefSeqiNP_001268531.1. NM_001281602.1.

Genome annotation databases

GeneIDi101824371.

Cross-referencesi

Web resourcesi

Protein Spotlight

Molecular chastity - Issue 93 of April 2008

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63629 mRNA. Translation: AAA37079.1.
PIRiA60503.
RefSeqiNP_001268531.1. NM_001281602.1.

3D structure databases

ProteinModelPortaliP23491.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi101824371.

Organism-specific databases

CTDi7784.

Phylogenomic databases

HOVERGENiHBG007985.

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...

Publicationsi

  1. "Genomic organization and polypeptide primary structure of zona pellucida glycoprotein hZP3, the hamster sperm receptor."
    Kinloch R.A., Ruiz-Seller B., Wassarman P.M.
    Dev. Biol. 142:414-421(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Ovary.

Entry informationi

Entry nameiZP3_MESAU
AccessioniPrimary (citable) accession number: P23491
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: February 1, 1996
Last modified: March 4, 2015
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.