P42098 (ZP3_PIG) 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 glycoprotein 3-beta
Short name=Zp-3-beta
Short name=Zp3-beta
Zona pellucida protein C

Cleaved into the following chain:

1. Processed zona pellucida sperm-binding protein 3

Gene names

Name:	ZP3
Synonyms:	ZP3B, ZPC

Organism

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	421 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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 zona matrix formation. In pig, does not seem to have a sperm-binding activity by itself but may increase sperm-binding activity of ZPB.
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. Ref.4 O-glycosylated; removal of O-linked glycans may play an important role in the post-fertilization block to polyspermy By similarity. Ref.5 All cysteine residues are involved in disulfide bonds.
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
Technical term	Complete proteome Direct protein sequencing Reference proteome
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 direct assay PubMed 15579591. 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	Ref.3
	Chain	23 – 332	310	Zona pellucida sperm-binding protein 3		PRO_0000041717
	Chain	23 – ?		Processed zona pellucida sperm-binding protein 3		PRO_0000304573
	Propeptide	333 – 421	89	Removed in mature form		PRO_0000041718
Regions
	Topological domain	23 – 381	359	Extracellular Potential
	Transmembrane	382 – 402	21	Helical; Potential
	Topological domain	403 – 421	19	Cytoplasmic Potential
	Domain	44 – 306	263	ZP
Amino acid modifications
	Modified residue	23	1	Pyrrolidone carboxylic acid
	Glycosylation	124	1	N-linked (GlcNAc...)		CAR_000151
	Glycosylation	146	1	N-linked (GlcNAc...)		CAR_000152
	Glycosylation	155	1	O-linked (GalNAc...)
	Glycosylation	161	1	O-linked (GalNAc...)
	Glycosylation	162	1	O-linked (GalNAc...)
	Glycosylation	179	1	N-linked (GlcNAc...) Potential
	Glycosylation	271	1	N-linked (GlcNAc...)		CAR_000153
	Disulfide bond	45 ↔ 139		By similarity
	Disulfide bond	77 ↔ 98		By similarity
	Disulfide bond	216 ↔ 281		By similarity
	Disulfide bond	238 ↔ 299		By similarity
Experimental info
	Sequence conflict	101	1	Missing in BAA08093. Ref.2
	Sequence conflict	107	1	D → V in BAA08093. Ref.2
	Sequence conflict	163 – 164	2	VF → GV in BAA08093. Ref.2
	Sequence conflict	404	1	P → A in BAA08093. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P42098 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: DC97D760E985213A	FASTA	421	46,239
	10 20 30 40 50 60 MAPSWRFFVC FLLWGGTELC SPQPVWQDEG QRLRPSKPPT VMVECQEAQL VVIVSKDLFG 70 80 90 100 110 120 TGKLIRPADL SLGPAKCEPL VSQDTDAVVR FEVGLHECGS SLQVTDDALV YSTFLRHDPR 130 140 150 160 170 180 PAGNLSILRT NRAEVPIECH YPRQGNVSSW AILPTWVPFR TTVFSEEKLV FSLRLMEENW 190 200 210 220 230 240 SAEKMTPTFQ LGDRAHLQAQ VHTGSHVPLR LFVDHCVATL TPDWNTSPSH TIVDFHGCLV 250 260 270 280 290 300 DGLTEASSAF KAPRPGPETL QFTVDVFHFA NDSRNTIYIT CHLKVTPADR VPDQLNKACS 310 320 330 340 350 360 FSKSSNRWSP VEGPAVICRC CHKGQCGTPS LSRKLSMPKR QSAPRSRRHV TDEADVTVGP 370 380 390 400 410 420 LIFLGKTSDH GVEGSTSSPT SVMVGLGLAT VVTLTLATIV LGVPRRRRAA AHLVCPVSAS Q

References

[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]	Okazaki Y., Sugimoto M. Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Ovary.
[3]	"Localization of epitopes for monoclonal antibodies at the N-terminus of the porcine zona pellucida glycoprotein pZPC." Gupta S.K., Yurewicz E.C., Afzalpurkar A., Rao K.V., Gage D.A., Wu H., Sacco A.G. Mol. Reprod. Dev. 42:220-225(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF N-TERMINUS, PYROGLUTAMATE FORMATION AT GLN-23, MASS SPECTROMETRY.
[4]	"Identification of the carboxyl termini of porcine zona pellucida glycoproteins ZPB and ZPC." Yonezawa N., Nakano M. Biochem. Biophys. Res. Commun. 307:877-882(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING.
[5]	"Porcine oocyte zona pellucida M(r) 55,000 glycoproteins: identification of O-glycosylated domains." Yurewicz E.C., Pack B.A., Sacco A.G. Mol. Reprod. Dev. 33:182-188(1992) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION.

Web resources

Protein Spotlight

Molecular chastity - Issue 93 of April 2008

Cross-references

Sequence databases
EMBL GenBank DDBJ	L22169 mRNA. Translation: AAA31145.1. D45065 mRNA. Translation: BAA08093.1.
PIR	S70433.
RefSeq	NP_999058.1. NM_213893.1.
UniGene	Ssc.80359.
3D structure databases
ProteinModelPortal	P42098.
ModBase	Search...
Protein-protein interaction databases
STRING	9823.ENSSSCP00000008213.
PTM databases
GlycoSuiteDB	P42098.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	396927.
KEGG	ssc:396927.
Organism-specific databases
CTD	7784.
Phylogenomic databases
eggNOG	NOG43042.
HOGENOM	HOG000220813.
HOVERGEN	HBG007985.
OrthoDB	EOG437RFK.
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_PIG

Accession

Primary (citable) accession number: P42098

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program