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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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 405385ExtracellularCuratedAdd
BLAST
Transmembranei406 – 42621HelicalSequence analysisAdd
BLAST
Topological domaini427 – 43711CytoplasmicSequence analysisAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi58 – 581C → A: Abolishes secretion of processed zona pellucida sperm-binding protein 3; when associated with A-152. 1 Publication
Mutagenesisi90 – 901C → A: Abolishes secretion of processed zona pellucida sperm-binding protein 3; when associated with A-111. 1 Publication
Mutagenesisi111 – 1111C → A: Abolishes secretion of processed zona pellucida sperm-binding protein 3; when associated with A-90.
Mutagenesisi142 – 1421R → A: Impaired homodimerization and abolished secretion of processed zona pellucida sperm-binding protein 3. 1 Publication
Mutagenesisi152 – 1521C → A: Abolishes secretion of processed zona pellucida sperm-binding protein 3; when associated with A-58. 1 Publication
Mutagenesisi159 – 1591N → Q: Loss of N-glycosylation. 1 Publication
Mutagenesisi168 – 1681T → A: Loss of O-glycosylation. No effect on secretion. Reduces binding to the sperm head by about 80%. 1 Publication
Mutagenesisi196 – 1961E → A: No effect on secretion. 1 Publication
Mutagenesisi229 – 2291C → A: Impaired secretion of processed zona pellucida sperm-binding protein 3; when associated with A-295. 1 Publication
Mutagenesisi235 – 2351P → D: Abolishes secretion of processed zona pellucida sperm-binding protein 3. 1 Publication
Mutagenesisi241 – 2411P → A: No effect on dimerization or secretion. 1 Publication
Mutagenesisi251 – 2511C → A: Abolishes secretion of processed zona pellucida sperm-binding protein 3; when associated with A-335. 1 Publication
Mutagenesisi292 – 2921Y → A: Abolishes secretion of processed zona pellucida sperm-binding protein 3. 1 Publication
Mutagenesisi295 – 2951C → A: Impaired secretion of processed zona pellucida sperm-binding protein 3; when associated with A-229.
Mutagenesisi313 – 3131C → A: Abolishes secretion of processed zona pellucida sperm-binding protein 3; when associated with A-332. 1 Publication
Mutagenesisi332 – 3321C → A: Abolishes secretion of processed zona pellucida sperm-binding protein 3; when associated with A-313. 1 Publication
Mutagenesisi334 – 3341C → A: Abolishes secretion of processed zona pellucida sperm-binding protein 3; when associated with A-340. 1 Publication
Mutagenesisi335 – 3351C → A: Abolishes secretion of processed zona pellucida sperm-binding protein 3; when associated with A-251. 1 Publication
Mutagenesisi340 – 3401C → A: Abolishes secretion of processed zona pellucida sperm-binding protein 3; when associated with A-334. 1 Publication
Mutagenesisi359 – 3624RFRR → AFAA: Abolishes cleavage of C-terminal propeptide. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20201 PublicationAdd
BLAST
Chaini21 – 360340Zona pellucida sperm-binding protein 3PRO_0000405431Add
BLAST
Chaini21 – ?Processed zona pellucida sperm-binding protein 3PRO_0000405432
Propeptidei361 – 43777Removed in mature formBy similarityPRO_0000405433Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi58 ↔ 1521 Publication
Disulfide bondi90 ↔ 1111 Publication
Glycosylationi159 – 1591N-linked (GlcNAc...)1 Publication
Glycosylationi168 – 1681O-linked (GalNAc...)1 Publication
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

1
437
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi53 – 586Combined sources
Beta strandi60 – 6910Combined sources
Helixi80 – 823Combined sources
Beta strandi83 – 853Combined sources
Turni86 – 894Combined sources
Beta strandi93 – 964Combined sources
Turni97 – 1004Combined sources
Beta strandi101 – 1077Combined sources
Beta strandi114 – 1174Combined sources
Beta strandi119 – 13012Combined sources
Beta strandi140 – 1434Combined sources
Beta strandi146 – 15510Combined sources
Turni171 – 1733Combined sources
Beta strandi184 – 1896Combined sources
Beta strandi193 – 1964Combined sources
Beta strandi199 – 2024Combined sources
Beta strandi207 – 2148Combined sources
Beta strandi217 – 2193Combined sources
Beta strandi222 – 23514Combined sources
Beta strandi239 – 2479Combined sources
Turni248 – 2503Combined sources
Helixi253 – 2564Combined sources
Beta strandi273 – 2797Combined sources
Beta strandi290 – 30112Combined sources
Beta strandi313 – 3164Combined sources
Turni317 – 3204Combined sources
Beta strandi321 – 3277Combined sources
Helixi329 – 3324Combined sources
Helixi333 – 3375Combined sources
Beta strandi368 – 37912Combined sources

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 320264ZPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni368 – 38013Extracellular hydrophobic patchAdd
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. ZPC subfamily.Curated
Contains 1 ZP domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410II9V. Eukaryota.
ENOG410YXE1. LUCA.
GeneTreeiENSGT00530000063482.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431A → V in AAV35184 (PubMed:16283938).Curated
Sequence conflicti48 – 481V → M in AAV35193 (PubMed:16283938).Curated
Sequence conflicti48 – 481V → M in AAV35180 (PubMed:16283938).Curated
Sequence conflicti48 – 481V → M in AAV35179 (PubMed:16283938).Curated
Sequence conflicti424 – 4241G → C in BAA13760 (PubMed:10103002).Curated
Sequence conflicti424 – 4241G → C in BAA83418 (Ref. 3) Curated
Sequence conflicti435 – 4351A → T in BAA13760 (PubMed:10103002).Curated

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

EnsembliENSGALT00000002370; ENSGALP00000002368; ENSGALG00000001559.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
3NK3X-ray2.60A/B53-347[»]
C/D359-382[»]
3NK4X-ray2.00A/B53-347[»]
C/D359-382[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000002368.

Proteomic databases

PaxDbiP79762.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000002370; ENSGALP00000002368; ENSGALG00000001559.
GeneIDi378906.
KEGGigga:378906.

Organism-specific databases

CTDi7784.

Phylogenomic databases

eggNOGiENOG410II9V. Eukaryota.
ENOG410YXE1. LUCA.
GeneTreeiENSGT00530000063482.
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: September 7, 2016
This is version 92 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.