Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P53785

- ZP3_MACRA

UniProt

P53785 - ZP3_MACRA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Zona pellucida sperm-binding protein 3

Gene

ZP3

Organism
Macaca radiata (Bonnet macaque)
Status
Reviewed - 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

  1. carbohydrate binding Source: UniProtKB
  2. manganese ion transmembrane transporter activity Source: UniProtKB
  3. signal transducer activity Source: UniProtKB

GO - Biological processi

  1. binding of sperm to zona pellucida Source: UniProtKB
  2. blastocyst formation Source: UniProtKB
  3. egg coat formation Source: UniProtKB
  4. humoral immune response mediated by circulating immunoglobulin Source: UniProtKB
  5. intracellular protein transport Source: UniProtKB
  6. intracellular signal transduction Source: UniProtKB
  7. manganese ion transmembrane transport Source: GOC
  8. manganese ion transport Source: UniProtKB
  9. negative regulation of binding of sperm to zona pellucida Source: UniProtKB
  10. negative regulation of transcription, DNA-templated Source: UniProtKB
  11. oocyte development Source: UniProtKB
  12. phosphatidylinositol-mediated signaling Source: UniProtKB
  13. positive regulation of acrosomal vesicle exocytosis Source: UniProtKB
  14. positive regulation of acrosome reaction Source: UniProtKB
  15. positive regulation of antral ovarian follicle growth Source: UniProtKB
  16. positive regulation of calcium ion import Source: UniProtKB
  17. positive regulation of humoral immune response Source: UniProtKB
  18. positive regulation of inflammatory response Source: UniProtKB
  19. positive regulation of interferon-gamma production Source: UniProtKB
  20. positive regulation of interleukin-4 production Source: UniProtKB
  21. positive regulation of leukocyte migration Source: UniProtKB
  22. positive regulation of ovarian follicle development Source: UniProtKB
  23. positive regulation of phosphatidylinositol biosynthetic process Source: UniProtKB
  24. positive regulation of protein kinase activity Source: UniProtKB
  25. positive regulation of protein kinase B signaling Source: UniProtKB
  26. positive regulation of T cell proliferation Source: UniProtKB
  27. positive regulation of transcription, DNA-templated Source: UniProtKB
  28. positive regulation of type IV hypersensitivity Source: UniProtKB
  29. protein kinase C signaling Source: UniProtKB
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
OrganismiMacaca radiata (Bonnet macaque)
Taxonomic identifieri9548 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Subcellular locationi

Chain Processed zona pellucida sperm-binding protein 3 : Secretedextracellular spaceextracellular matrix
Note: The glycoproteinaceous translucent extracellular matrix that surrounds the mammalian oocyte is called zona pellucida.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 387365ExtracellularSequence AnalysisAdd
BLAST
Transmembranei388 – 40821HelicalSequence AnalysisAdd
BLAST
Topological domaini409 – 42416CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. endoplasmic reticulum Source: UniProtKB
  3. extracellular matrix Source: UniProtKB
  4. extracellular space Source: UniProtKB
  5. Golgi apparatus Source: UniProtKB
  6. integral component of membrane Source: UniProtKB-KW
  7. multivesicular body Source: UniProtKB
  8. outer acrosomal membrane Source: UniProtKB
  9. perinuclear region of cytoplasm Source: UniProtKB
  10. plasma membrane Source: UniProtKB
  11. proteinaceous extracellular matrix Source: UniProtKB-KW
  12. secretory granule Source: UniProtKB
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 – 350328Zona pellucida sperm-binding protein 3PRO_0000041711Add
BLAST
Chaini23 – ?Processed zona pellucida sperm-binding protein 3PRO_0000304570
Propeptidei351 – 42474Removed in mature formBy similarityPRO_0000041712Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231Pyrrolidone carboxylic acidBy similarity
Disulfide bondi46 ↔ 140By similarity
Disulfide bondi78 ↔ 99By similarity
Glycosylationi125 – 1251N-linked (GlcNAc...)By similarity
Glycosylationi147 – 1471N-linked (GlcNAc...)By similarity
Glycosylationi156 – 1561O-linked (GalNAc...)By similarity
Glycosylationi162 – 1621O-linked (GalNAc...)By similarity
Glycosylationi163 – 1631O-linked (GalNAc...)By similarity
Disulfide bondi217 ↔ 282By similarity
Disulfide bondi239 ↔ 300By similarity
Glycosylationi272 – 2721N-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.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP53785.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 307263ZPPROSITE-ProRule annotationAdd
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.

P53785-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MELSYRLFIC LLLWGSTELC YPQPFWLLQG GASRAETSVQ PVLVECREAT
60 70 80 90 100
LLVTVSKDLF GTGKLIRAAD LTLGPEACEP LVSMDTEDVV RFEVGLHECG
110 120 130 140 150
SSMQVTDDAL VYSTFLLHDP RPVGNLSIVR TNRAEIPIEC RYPRQGNVSS
160 170 180 190 200
QAILPTWLPF RTTVFSEEKL TFSLRLMEEN WNAEKRSPTF HLGDAAHLQA
210 220 230 240 250
EIHTGSHVPL RLFVDHCVAT PTPDQNASPY HTIVDFHGCL VDGLTDASSA
260 270 280 290 300
FKVPRPGPDT LQFTVDVFHF ANDSRNMIYI TCHLKAIPAE QEPDELNKAC
310 320 330 340 350
SFSKSSNSWF PVEGPADICQ CCSKGDCGTP SHSRRQPHVV SQWSRSASRN
360 370 380 390 400
RRHVTEEADI TVGPLIFLDR SADYEVEQWA LPADTSVLLL GIGLAVVASL
410 420
TLTAVILIFT RRWRTASRPV SASE
Length:424
Mass (Da):47,040
Last modified:October 1, 1996 - v1
Checksum:i3B41C4CFA3792331
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82639 mRNA. Translation: CAA57961.1.

Cross-referencesi

Web resourcesi

Protein Spotlight

Molecular chastity - Issue 93 of April 2008

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82639 mRNA. Translation: CAA57961.1 .

3D structure databases

ProteinModelPortali P53785.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG007985.

Family and domain databases

InterProi IPR001507. ZP_dom.
IPR017977. ZP_dom_CS.
[Graphical view ]
Pfami PF00100. Zona_pellucida. 1 hit.
[Graphical view ]
PRINTSi PR00023. ZPELLUCIDA.
SMARTi SM00241. ZP. 1 hit.
[Graphical view ]
PROSITEi PS00682. ZP_1. 1 hit.
PS51034. ZP_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Nucleotide sequence of cDNA encoding bonnet monkey (Macaca radiata) zona pellucida glycoprotein-ZP3."
    Kolluri S.K., Kaul R., Banerjee K., Gupta S.K.
    Reprod. Fertil. Dev. 7:1209-1212(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Ovary.

Entry informationi

Entry nameiZP3_MACRA
AccessioniPrimary (citable) accession number: P53785
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 71 of the entry and version 1 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