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P97708

- ZP3_RAT

UniProt

P97708 - ZP3_RAT

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Protein

Zona pellucida sperm-binding protein 3

Gene

Zp3

Organism
Rattus norvegicus (Rat)
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):
Zona pellucida glycoprotein 3
Short name:
Zp-3
Zona pellucida protein C
Cleaved into the following chain:
Gene namesi
Name:Zp3
Synonyms:Zp-3, Zpc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi620606. Zp3.

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 – 351329Zona pellucida sperm-binding protein 3PRO_0000041721Add
BLAST
Chaini23 – ?Processed zona pellucida sperm-binding protein 3PRO_0000304575
Propeptidei352 – 42473Removed in mature form1 PublicationPRO_0000041722Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231Pyrrolidone carboxylic acid1 Publication
Glycosylationi32 – 321O-linked (GalNAc...)By similarity
Glycosylationi34 – 341O-linked (GalNAc...)By similarity
Glycosylationi39 – 391O-linked (GalNAc...)By similarity
Disulfide bondi46 ↔ 139By similarity
Disulfide bondi78 ↔ 981 Publication
Glycosylationi146 – 1461N-linked (GlcNAc...)1 Publication
Glycosylationi155 – 1551O-linked (GalNAc...)By similarity
Glycosylationi162 – 1621O-linked (GalNAc...)By similarity
Disulfide bondi216 ↔ 2831 Publication
Disulfide bondi240 ↔ 3011 Publication
Glycosylationi273 – 2731N-linked (GlcNAc...)1 Publication
Glycosylationi304 – 3041N-linked (GlcNAc...)1 Publication
Glycosylationi327 – 3271N-linked (GlcNAc...)By similarity
Glycosylationi330 – 3301N-linked (GlcNAc...)1 Publication

Post-translational modificationi

Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.
N-glycosylated; N-linked glycans are of high mannose/hybrid type, as well as bi-, tri- and tetra-antennary complex types.
O-glycosylated; removal of O-linked glycans may play an important role in the post-fertilization block to polyspermy.

Keywords - PTMi

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

Proteomic databases

PRIDEiP97708.

Expressioni

Tissue specificityi

Oocytes.

Gene expression databases

GenevestigatoriP97708.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP97708.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 308264ZPPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi329 – 3346Poly-Ser

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.
InParanoidiP97708.
PhylomeDBiP97708.

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.

P97708-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGPSCLLFLC LLLCGGPELC YPQTQWLLPG GTPTPAGSSS PVEVECKEAE
60 70 80 90 100
LVVTVRRDLF GTGKLVQPGD LTLGSEGCQP LVAVDTDVVR LNAQLHECSS
110 120 130 140 150
GVQVTEDALV YNTFLLHDPR PVNGLSILRT NRVEVPIECR YPRQGNVSSH
160 170 180 190 200
PIQPTWVPFS ATVSSEEKLA FSLRLMEEDW NTEKSSPTFH LGEVAHLQAE
210 220 230 240 250
VQTGSHLPLQ LFVDHCVATP SPLPGQNSSP HHFIVDSHGC LVDGLSESFS
260 270 280 290 300
AFQVPRPRPE TLQFTVDVFH FANSSRNTVY ITCHLKVAPA NQIPDKLNKA
310 320 330 340 350
CSFNKTSQSW LPVEGDADIC DCCSNGNCSN SSSSEFETHE PAQWSTLVSR
360 370 380 390 400
NRRHVTDEAD VTVGPLIFLG KANDQAVEGW TSSAQTSVAL GLGLATVAFL
410 420
TLAAIVLGVT RKCHTSSYLV SLPQ
Length:424
Mass (Da):45,901
Last modified:June 1, 1998 - v2
Checksum:i2AB42CBB14DE8701
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551V → A in BAA24456. (PubMed:9820205)Curated
Sequence conflicti112 – 1121N → S in BAA24456. (PubMed:9820205)Curated
Sequence conflicti412 – 4121K → M in BAA24456. (PubMed:9820205)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10823 mRNA. Translation: CAA71787.1.
D78482 mRNA. Translation: BAA24456.1.
RefSeqiNP_446214.1. NM_053762.1.
UniGeneiRn.10892.

Genome annotation databases

GeneIDi114639.
KEGGirno:114639.
UCSCiRGD:620606. rat.

Cross-referencesi

Web resourcesi

Protein Spotlight

Molecular chastity - Issue 93 of April 2008

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10823 mRNA. Translation: CAA71787.1 .
D78482 mRNA. Translation: BAA24456.1 .
RefSeqi NP_446214.1. NM_053762.1.
UniGenei Rn.10892.

3D structure databases

ProteinModelPortali P97708.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P97708.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 114639.
KEGGi rno:114639.
UCSCi RGD:620606. rat.

Organism-specific databases

CTDi 7784.
RGDi 620606. Zp3.

Phylogenomic databases

eggNOGi NOG43042.
HOGENOMi HOG000220813.
HOVERGENi HBG007985.
InParanoidi P97708.
PhylomeDBi P97708.

Miscellaneous databases

NextBioi 618829.
PROi P97708.

Gene expression databases

Genevestigatori P97708.

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. "Molecular characterisation of zona pellucida protein 3 (ZP3) in the rat."
    MacDuff P.E., Kerr L.E., Aitken R.J.
    J. Reprod. Fertil. Abstr. Ser. 18:86-86(1996)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Ovary.
  2. "Rat zona pellucida glycoproteins: molecular cloning and characterization of the three major components."
    Akatsuka K., Yoshida-Komiya H., Tulsiani D.R.P., Orgebin-Crist M.-C., Hiroi M., Araki Y.
    Mol. Reprod. Dev. 51:454-467(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 57-63, GLYCOSYLATION.
    Strain: Sprague-Dawley.
    Tissue: Ovary.
  3. "Structural conservation of mouse and rat zona pellucida glycoproteins. Probing the native rat zona pellucida proteome by mass spectrometry."
    Boja E.S., Hoodbhoy T., Garfield M., Fales H.M.
    Biochemistry 44:16445-16460(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF C-TERMINUS, PYROGLUTAMATE FORMATION AT GLN-23, DISULFIDE BOND FORMATION AT 78-CYS--CYS-98; 216-CYS--CYS-283 AND 240-CYS--CYS-301, GLYCOSYLATION AT ASN-146; ASN-273; ASN-304 AND ASN-330, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiZP3_RAT
AccessioniPrimary (citable) accession number: P97708
Secondary accession number(s): O55084
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 1998
Last modified: October 29, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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