P53785 (ZP3_MACRA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

1. Processed zona pellucida sperm-binding protein 3

Gene names

Name:	ZP3
Synonyms:	ZPC

Organism

Macaca radiata (Bonnet macaque)

Taxonomic identifier

9548 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Cercopithecoidea › Cercopithecidae › Cercopithecinae › Macaca

Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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.
Subunit structure	Polymers of ZP2 and ZP3 organized into long filaments cross-linked by ZP1 homodimers By similarity.
Subcellular location	Processed zona pellucida sperm-binding protein 3: Secreted › extracellular space › extracellular matrix. Cell membrane; Single-pass type I membrane protein.
Tissue specificity	Oocytes.
Domain	The ZP domain is involved in the polymerization of the ZP proteins to form the zona pellucida.
Post-translational modification	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.
Sequence similarities	Belongs to the ZP domain family. ZPC subfamily. Contains 1 ZP domain.

Ontologies

Keywords
Biological process	Fertilization
Cellular component	Cell membrane Extracellular matrix Membrane Secreted
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Gene Ontology (GO)
Biological_process	binding of sperm to zona pellucida Inferred from sequence or structural similarity. Source: UniProtKB blastocyst formation Inferred from sequence or structural similarity. Source: UniProtKB egg coat formation Inferred from sequence or structural similarity. Source: UniProtKB humoral immune response mediated by circulating immunoglobulin Inferred from sequence or structural similarity. Source: UniProtKB intracellular protein transport Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of binding of sperm to zona pellucida Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB oocyte development Inferred from sequence or structural similarity. Source: UniProtKB phosphatidylinositol-mediated signaling Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of T cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of acrosomal vesicle exocytosis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of acrosome reaction Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of antral ovarian follicle growth Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of calcium ion import Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of humoral immune response Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of interferon-gamma production Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of interleukin-4 production Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of leukocyte migration Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of ovarian follicle development Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of phosphatidylinositol biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of protein kinase B signaling cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of protein kinase activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of type IV hypersensitivity Inferred from sequence or structural similarity. Source: UniProtKB protein kinase C signaling cascade Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	Golgi apparatus Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum Inferred from sequence or structural similarity. Source: UniProtKB extracellular matrix Inferred from sequence or structural similarity. Source: UniProtKB extracellular space Inferred from sequence or structural similarity. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW multivesicular body Inferred from sequence or structural similarity. Source: UniProtKB outer acrosomal membrane Inferred from sequence or structural similarity. Source: UniProtKB perinuclear region of cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	carbohydrate binding Inferred from sequence or structural similarity. Source: UniProtKB manganese ion transmembrane transporter activity Inferred from sequence or structural similarity. Source: UniProtKB signal transducer activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	By similarity
	Chain	23 – 350	328	Zona pellucida sperm-binding protein 3		PRO_0000041711
	Chain	23 – ?		Processed zona pellucida sperm-binding protein 3		PRO_0000304570
	Propeptide	351 – 424	74	Removed in mature form By similarity		PRO_0000041712
Regions
	Topological domain	23 – 387	365	Extracellular Potential
	Transmembrane	388 – 408	21	Helical; Potential
	Topological domain	409 – 424	16	Cytoplasmic Potential
	Domain	45 – 307	263	ZP
Amino acid modifications
	Modified residue	23	1	Pyrrolidone carboxylic acid By similarity
	Glycosylation	125	1	N-linked (GlcNAc...) By similarity
	Glycosylation	147	1	N-linked (GlcNAc...) By similarity
	Glycosylation	156	1	O-linked (GalNAc...) By similarity
	Glycosylation	162	1	O-linked (GalNAc...) By similarity
	Glycosylation	163	1	O-linked (GalNAc...) By similarity
	Glycosylation	272	1	N-linked (GlcNAc...) By similarity
	Disulfide bond	46 ↔ 140		By similarity
	Disulfide bond	78 ↔ 99		By similarity
	Disulfide bond	217 ↔ 282		By similarity
	Disulfide bond	239 ↔ 300		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P53785 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 3B41C4CFA3792331	FASTA	424	47,040
	10 20 30 40 50 60 MELSYRLFIC LLLWGSTELC YPQPFWLLQG GASRAETSVQ PVLVECREAT LLVTVSKDLF 70 80 90 100 110 120 GTGKLIRAAD LTLGPEACEP LVSMDTEDVV RFEVGLHECG SSMQVTDDAL VYSTFLLHDP 130 140 150 160 170 180 RPVGNLSIVR TNRAEIPIEC RYPRQGNVSS QAILPTWLPF RTTVFSEEKL TFSLRLMEEN 190 200 210 220 230 240 WNAEKRSPTF HLGDAAHLQA EIHTGSHVPL RLFVDHCVAT PTPDQNASPY HTIVDFHGCL 250 260 270 280 290 300 VDGLTDASSA FKVPRPGPDT LQFTVDVFHF ANDSRNMIYI TCHLKAIPAE QEPDELNKAC 310 320 330 340 350 360 SFSKSSNSWF PVEGPADICQ CCSKGDCGTP SHSRRQPHVV SQWSRSASRN RRHVTEEADI 370 380 390 400 410 420 TVGPLIFLDR SADYEVEQWA LPADTSVLLL GIGLAVVASL TLTAVILIFT RRWRTASRPV SASE

References

[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.

Web resources

Protein Spotlight

Molecular chastity - Issue 93 of April 2008

Cross-references

Sequence databases
EMBL GenBank DDBJ	X82639 mRNA. Translation: CAA57961.1.
3D structure databases
ProteinModelPortal	P53785.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG007985.
Family and domain databases
InterPro	IPR001507. ZP_dom. IPR017977. ZP_dom_CS. [Graphical view]
Pfam	PF00100. Zona_pellucida. 1 hit. [Graphical view]
PRINTS	PR00023. ZPELLUCIDA.
SMART	SM00241. ZP. 1 hit. [Graphical view]
PROSITE	PS00682. ZP_1. 1 hit. PS51034. ZP_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ZP3_MACRA

Accession

Primary (citable) accession number: P53785

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program