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P48833

- ZP3_RABIT

UniProt

P48833 - ZP3_RABIT

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Protein

Zona pellucida sperm-binding protein 3

Gene

ZP3

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - 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

  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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

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.
Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 378360ExtracellularSequence AnalysisAdd
BLAST
Transmembranei379 – 39921HelicalSequence AnalysisAdd
BLAST
Topological domaini400 – 41516CytoplasmicSequence 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 peptidei‹1 – 18›18By similarityAdd
BLAST
Chaini19 – 341323Zona pellucida sperm-binding protein 3PRO_0000041719Add
BLAST
Chaini19 – ?Processed zona pellucida sperm-binding protein 3PRO_0000304574
Propeptidei342 – 41574Removed in mature formBy similarityPRO_0000041720Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Pyrrolidone carboxylic acidBy similarity
Glycosylationi28 – 281O-linked (GalNAc...)By similarity
Disulfide bondi42 ↔ 134By similarity
Disulfide bondi74 ↔ 93By similarity
Glycosylationi119 – 1191N-linked (GlcNAc...)By similarity
Glycosylationi141 – 1411N-linked (GlcNAc...)By similarity
Glycosylationi150 – 1501O-linked (GalNAc...)By similarity
Glycosylationi156 – 1561O-linked (GalNAc...)By similarity
Glycosylationi157 – 1571O-linked (GalNAc...)By similarity
Glycosylationi174 – 1741N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi211 ↔ 276By similarity
Disulfide bondi233 ↔ 294By similarity
Glycosylationi266 – 2661N-linked (GlcNAc...)By similarity
Glycosylationi297 – 2971N-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 (at protein level).1 Publication

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000013539.

Structurei

3D structure databases

ProteinModelPortaliP48833.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 301261ZPPROSITE-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

eggNOGiNOG43042.
HOGENOMiHOG000220813.
HOVERGENiHBG007985.
InParanoidiP48833.

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: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

P48833-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
YGLFVCLLLW GGSELCCPQP LWFWQGGTRQ PAPSVTPVVV ECLEARLVVT
60 70 80 90 100
VSRDLFGTGK LIQEADLSLG PEGCEPQAST DAVVRFEVGL HECGNSVQVT
110 120 130 140 150
DDSLVYSSFL LHDPRPAGNL SILRTNRAEV PIECRYPRQG NVSSRAILPT
160 170 180 190 200
WVPFWTTVLS EERLVFSLRL MEENWSREKM SPTFHLGDTA HLQAEVRTGS
210 220 230 240 250
HPPLLLFVDR CVATPTRDQS GSPYHTIVDL HGCLVDGLSD GASKFKAPRP
260 270 280 290 300
KPDVLQFMVA VFHFANDSRH TVYITCHLRV IPAQQAPDRL NKACSFNQSS
310 320 330 340 350
SSWAPVEGSA DICECCGNGD CDLIAGSPMN QNHAARSSLR SRRHVTEEAD
360 370 380 390 400
VTVGPLIFLG KAGDPAGTEG LASAAQATLV LGLRMATIVF LAVAAVVLGL
410
TRGRHAASHP RSASQ
Length:415
Mass (Da):44,987
Last modified:February 1, 1996 - v1
Checksum:i77396CF1BAA3F5CB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U05782 mRNA. Translation: AAA74392.1.
PIRiS70401.
UniGeneiOcu.2033.

Cross-referencesi

Web resourcesi

Protein Spotlight

Molecular chastity - Issue 93 of April 2008

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U05782 mRNA. Translation: AAA74392.1 .
PIRi S70401.
UniGenei Ocu.2033.

3D structure databases

ProteinModelPortali P48833.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9986.ENSOCUP00000013539.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG43042.
HOGENOMi HOG000220813.
HOVERGENi HBG007985.
InParanoidi P48833.

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. "Cloning and characterization of zona pellucida genes and cDNAs from a variety of mammalian species: the ZPA, ZPB and ZPC gene families."
    Harris J.D., Hibler D.W., Fontenot G.K., Hsu K.T., Yurewicz E.C., Sacco A.G.
    DNA Seq. 4:361-393(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Ovary.
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Ovary.

Entry informationi

Entry nameiZP3_RABIT
AccessioniPrimary (citable) accession number: P48833
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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