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Protein

Zona pellucida sperm-binding protein 3

Gene

ZP3

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the zona pellucida, which mediates species-specific sperm binding. Directly binds to sperm. Important for egg fertilization.2 Publications

GO - Molecular functioni

  • acrosin binding Source: GO_Central
  • identical protein binding Source: IntAct

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Fertilization

Enzyme and pathway databases

ReactomeiR-GGA-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 C protein
Zona pellucida glycoprotein 3
Short name:
Zp-3
Cleaved into the following chain:
Gene namesi
Name:ZP3
Synonyms:ZPC
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 10

Subcellular locationi

Processed zona pellucida sperm-binding protein 3 :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini21 – 405ExtracellularCuratedAdd BLAST385
Transmembranei406 – 426HelicalSequence analysisAdd BLAST21
Topological domaini427 – 437CytoplasmicSequence analysisAdd BLAST11

GO - Cellular componenti

  • apical part of cell Source: AgBase
  • cell Source: AgBase
  • extracellular matrix Source: GO_Central
  • extracellular space Source: AgBase
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: UniProtKB-SubCell
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Extracellular matrix, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi58C → A: Abolishes secretion of processed zona pellucida sperm-binding protein 3; when associated with A-152. 1 Publication1
Mutagenesisi90C → A: Abolishes secretion of processed zona pellucida sperm-binding protein 3; when associated with A-111. 1 Publication1
Mutagenesisi111C → A: Abolishes secretion of processed zona pellucida sperm-binding protein 3; when associated with A-90. 1
Mutagenesisi142R → A: Impaired homodimerization and abolished secretion of processed zona pellucida sperm-binding protein 3. 1 Publication1
Mutagenesisi152C → A: Abolishes secretion of processed zona pellucida sperm-binding protein 3; when associated with A-58. 1 Publication1
Mutagenesisi159N → Q: Loss of N-glycosylation. 1 Publication1
Mutagenesisi168T → A: Loss of O-glycosylation. No effect on secretion. Reduces binding to the sperm head by about 80%. 1 Publication1
Mutagenesisi196E → A: No effect on secretion. 1 Publication1
Mutagenesisi229C → A: Impaired secretion of processed zona pellucida sperm-binding protein 3; when associated with A-295. 1 Publication1
Mutagenesisi235P → D: Abolishes secretion of processed zona pellucida sperm-binding protein 3. 1 Publication1
Mutagenesisi241P → A: No effect on dimerization or secretion. 1 Publication1
Mutagenesisi251C → A: Abolishes secretion of processed zona pellucida sperm-binding protein 3; when associated with A-335. 1 Publication1
Mutagenesisi292Y → A: Abolishes secretion of processed zona pellucida sperm-binding protein 3. 1 Publication1
Mutagenesisi295C → A: Impaired secretion of processed zona pellucida sperm-binding protein 3; when associated with A-229. 1
Mutagenesisi313C → A: Abolishes secretion of processed zona pellucida sperm-binding protein 3; when associated with A-332. 1 Publication1
Mutagenesisi332C → A: Abolishes secretion of processed zona pellucida sperm-binding protein 3; when associated with A-313. 1 Publication1
Mutagenesisi334C → A: Abolishes secretion of processed zona pellucida sperm-binding protein 3; when associated with A-340. 1 Publication1
Mutagenesisi335C → A: Abolishes secretion of processed zona pellucida sperm-binding protein 3; when associated with A-251. 1 Publication1
Mutagenesisi340C → A: Abolishes secretion of processed zona pellucida sperm-binding protein 3; when associated with A-334. 1 Publication1
Mutagenesisi359 – 362RFRR → AFAA: Abolishes cleavage of C-terminal propeptide. 1 Publication4

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 201 PublicationAdd BLAST20
ChainiPRO_000040543121 – 360Zona pellucida sperm-binding protein 3Add BLAST340
ChainiPRO_000040543221 – ?Processed zona pellucida sperm-binding protein 3
PropeptideiPRO_0000405433361 – 437Removed in mature formBy similarityAdd BLAST77

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi58 ↔ 1521 Publication
Disulfide bondi90 ↔ 1111 Publication
Glycosylationi159N-linked (GlcNAc...)1 Publication1
Glycosylationi168O-linked (GalNAc...)1 Publication1
Disulfide bondi229 ↔ 2951 Publication
Disulfide bondi251 ↔ 3351 Publication
Disulfide bondi313 ↔ 3321 Publication
Disulfide bondi334 ↔ 3401 Publication

Post-translational modificationi

Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.
N-glycosylated.
O-glycosylated. O-glycosylation at Thr-168 is important for efficient interaction with the sperm head.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP79762.

Expressioni

Tissue specificityi

Detected in the ovarian perivitteline layer. Detected in granulosa cells in ovarian follicle (at protein level). Detected in granulosa cells in ovarian follicle.2 Publications

Gene expression databases

BgeeiENSGALG00000001559.

Interactioni

Subunit structurei

Homodimer. Forms higher oligomers, once its C-terminus has been proteolytically removed. Forms heterooligomers with other zona pellucida glycoproteins (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-2942236,EBI-2942236

GO - Molecular functioni

  • acrosin binding Source: GO_Central
  • identical protein binding Source: IntAct

Protein-protein interaction databases

STRINGi9031.ENSGALP00000002368.

Structurei

Secondary structure

1437
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi53 – 58Combined sources6
Beta strandi60 – 69Combined sources10
Helixi80 – 82Combined sources3
Beta strandi83 – 85Combined sources3
Turni86 – 89Combined sources4
Beta strandi93 – 96Combined sources4
Turni97 – 100Combined sources4
Beta strandi101 – 107Combined sources7
Beta strandi114 – 117Combined sources4
Beta strandi119 – 130Combined sources12
Beta strandi140 – 143Combined sources4
Beta strandi146 – 155Combined sources10
Turni171 – 173Combined sources3
Beta strandi184 – 189Combined sources6
Beta strandi193 – 196Combined sources4
Beta strandi199 – 202Combined sources4
Beta strandi207 – 214Combined sources8
Beta strandi217 – 219Combined sources3
Beta strandi222 – 235Combined sources14
Beta strandi239 – 247Combined sources9
Turni248 – 250Combined sources3
Helixi253 – 256Combined sources4
Beta strandi273 – 279Combined sources7
Beta strandi290 – 301Combined sources12
Beta strandi313 – 316Combined sources4
Turni317 – 320Combined sources4
Beta strandi321 – 327Combined sources7
Helixi329 – 332Combined sources4
Helixi333 – 337Combined sources5
Beta strandi368 – 379Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NK3X-ray2.60A/B53-347[»]
C/D359-382[»]
3NK4X-ray2.00A/B53-347[»]
C/D359-382[»]
ProteinModelPortaliP79762.
SMRiP79762.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini57 – 320ZPPROSITE-ProRule annotationAdd BLAST264

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni368 – 380Extracellular hydrophobic patchAdd BLAST13

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. ZPC subfamily.Curated
Contains 1 ZP domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410II9V. Eukaryota.
ENOG410YXE1. LUCA.
HOVERGENiHBG007985.
InParanoidiP79762.
KOiK19928.
OMAiGPAACKH.
OrthoDBiEOG091G0E1O.
PhylomeDBiP79762.
TreeFamiTF331369.

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.

P79762-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQGGRVVLGL LCCLVAGVGS YTPWDISWAA RGDPSAWSWG AEAHSRAVAG
60 70 80 90 100
SHPVAVQCQE AQLVVTVHRD LFGTGRLINA ADLTLGPAAC KHSSLNAAHN
110 120 130 140 150
TVTFAAGLHE CGSVVQVTPD TLIYRTLINY DPSPASNPVI IRTNPAVIPI
160 170 180 190 200
ECHYPRRENV SSNAIRPTWS PFNSALSAEE RLVFSLRLMS DDWSTERPFT
210 220 230 240 250
GFQLGDILNI QAEVSTENHV PLRLFVDSCV AALSPDGDSS PHYAIIDFNG
260 270 280 290 300
CLVDGRVDDT SSAFITPRPR EDVLRFRIDV FRFAGDNRNL IYITCHLKVT
310 320 330 340 350
PADQGPDPQN KACSFNKARN TWVPVEGSRD VCNCCETGNC EPPALSRRLN
360 370 380 390 400
PMERWQSRRF RRDAGKEVAA DVVIGPVLLS ADPGAVGQQE EGGDGAAVMV
410 420 430
PSVGTGLVCV AVAVALAAVG VAVGIARKGC TRTSAAV
Length:437
Mass (Da):46,766
Last modified:March 8, 2011 - v4
Checksum:iA9B59E9DE71819B3
GO

Sequence cautioni

The sequence AAV35179 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAV35180 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAV35181 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAV35182 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAV35183 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAV35184 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAV35185 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAV35186 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAV35187 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAV35188 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAV35189 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAV35190 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAV35191 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAV35192 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAV35193 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAV35194 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAV35195 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAV35196 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAV35197 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAV35198 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAV35199 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAV35200 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAV35201 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA83418 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti43A → V in AAV35184 (PubMed:16283938).Curated1
Sequence conflicti48V → M in AAV35193 (PubMed:16283938).Curated1
Sequence conflicti48V → M in AAV35180 (PubMed:16283938).Curated1
Sequence conflicti48V → M in AAV35179 (PubMed:16283938).Curated1
Sequence conflicti424G → C in BAA13760 (PubMed:10103002).Curated1
Sequence conflicti424G → C in BAA83418 (Ref. 3) Curated1
Sequence conflicti435A → T in BAA13760 (PubMed:10103002).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89097 mRNA. Translation: BAA13760.3.
AY628608 Genomic DNA. Translation: AAV35179.1. Different initiation.
AY628609 Genomic DNA. Translation: AAV35180.1. Different initiation.
AY628610 Genomic DNA. Translation: AAV35181.1. Different initiation.
AY628611 Genomic DNA. Translation: AAV35182.1. Different initiation.
AY628612 Genomic DNA. Translation: AAV35183.1. Different initiation.
AY628613 Genomic DNA. Translation: AAV35184.1. Different initiation.
AY628614 Genomic DNA. Translation: AAV35185.1. Different initiation.
AY628615 Genomic DNA. Translation: AAV35186.1. Different initiation.
AY628616 Genomic DNA. Translation: AAV35187.1. Different initiation.
AY628617 Genomic DNA. Translation: AAV35188.1. Different initiation.
AY628618 Genomic DNA. Translation: AAV35189.1. Different initiation.
AY628619 Genomic DNA. Translation: AAV35190.1. Different initiation.
AY628620 Genomic DNA. Translation: AAV35191.1. Different initiation.
AY628621 Genomic DNA. Translation: AAV35192.1. Different initiation.
AY628622 Genomic DNA. Translation: AAV35193.1. Different initiation.
AY628623 Genomic DNA. Translation: AAV35194.1. Different initiation.
AY628624 Genomic DNA. Translation: AAV35195.1. Different initiation.
AY628625 Genomic DNA. Translation: AAV35196.1. Different initiation.
AY628626 Genomic DNA. Translation: AAV35197.1. Different initiation.
AY628627 Genomic DNA. Translation: AAV35198.1. Different initiation.
AY628628 Genomic DNA. Translation: AAV35199.1. Different initiation.
AY628629 Genomic DNA. Translation: AAV35200.1. Different initiation.
AY628630 Genomic DNA. Translation: AAV35201.1. Different initiation.
AB031033 Genomic DNA. Translation: BAA83418.1. Different initiation.
RefSeqiNP_989720.3. NM_204389.2.
UniGeneiGga.7210.

Genome annotation databases

GeneIDi378906.
KEGGigga:378906.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89097 mRNA. Translation: BAA13760.3.
AY628608 Genomic DNA. Translation: AAV35179.1. Different initiation.
AY628609 Genomic DNA. Translation: AAV35180.1. Different initiation.
AY628610 Genomic DNA. Translation: AAV35181.1. Different initiation.
AY628611 Genomic DNA. Translation: AAV35182.1. Different initiation.
AY628612 Genomic DNA. Translation: AAV35183.1. Different initiation.
AY628613 Genomic DNA. Translation: AAV35184.1. Different initiation.
AY628614 Genomic DNA. Translation: AAV35185.1. Different initiation.
AY628615 Genomic DNA. Translation: AAV35186.1. Different initiation.
AY628616 Genomic DNA. Translation: AAV35187.1. Different initiation.
AY628617 Genomic DNA. Translation: AAV35188.1. Different initiation.
AY628618 Genomic DNA. Translation: AAV35189.1. Different initiation.
AY628619 Genomic DNA. Translation: AAV35190.1. Different initiation.
AY628620 Genomic DNA. Translation: AAV35191.1. Different initiation.
AY628621 Genomic DNA. Translation: AAV35192.1. Different initiation.
AY628622 Genomic DNA. Translation: AAV35193.1. Different initiation.
AY628623 Genomic DNA. Translation: AAV35194.1. Different initiation.
AY628624 Genomic DNA. Translation: AAV35195.1. Different initiation.
AY628625 Genomic DNA. Translation: AAV35196.1. Different initiation.
AY628626 Genomic DNA. Translation: AAV35197.1. Different initiation.
AY628627 Genomic DNA. Translation: AAV35198.1. Different initiation.
AY628628 Genomic DNA. Translation: AAV35199.1. Different initiation.
AY628629 Genomic DNA. Translation: AAV35200.1. Different initiation.
AY628630 Genomic DNA. Translation: AAV35201.1. Different initiation.
AB031033 Genomic DNA. Translation: BAA83418.1. Different initiation.
RefSeqiNP_989720.3. NM_204389.2.
UniGeneiGga.7210.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NK3X-ray2.60A/B53-347[»]
C/D359-382[»]
3NK4X-ray2.00A/B53-347[»]
C/D359-382[»]
ProteinModelPortaliP79762.
SMRiP79762.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000002368.

Proteomic databases

PaxDbiP79762.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi378906.
KEGGigga:378906.

Organism-specific databases

CTDi7784.

Phylogenomic databases

eggNOGiENOG410II9V. Eukaryota.
ENOG410YXE1. LUCA.
HOVERGENiHBG007985.
InParanoidiP79762.
KOiK19928.
OMAiGPAACKH.
OrthoDBiEOG091G0E1O.
PhylomeDBiP79762.
TreeFamiTF331369.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP79762.

Gene expression databases

BgeeiENSGALG00000001559.

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_CHICK
AccessioniPrimary (citable) accession number: P79762
Secondary accession number(s): Q4VU46
, Q4VU49, Q4VU50, Q4VU53, Q4VU54, Q4VU57, Q4VU62, Q4VU63, Q4VU66, Q9PWF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 8, 2011
Last sequence update: March 8, 2011
Last modified: November 30, 2016
This is version 94 of the entry and version 4 of the sequence. [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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.