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Zona pellucida sperm-binding protein 3 (Sperm receptor) (Zona pellucida glycoprotein 3) (Zp-3) (Zona pellucida protein C) [Cleaved into: Processed zona pellucida sperm-binding protein 3]

 ZP3_MESAU               Reviewed;         422 AA.
P23491;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
22-NOV-2017, entry version 93.
RecName: Full=Zona pellucida sperm-binding protein 3;
AltName: Full=Sperm receptor;
AltName: Full=Zona pellucida glycoprotein 3;
Short=Zp-3;
AltName: Full=Zona pellucida protein C;
Contains:
RecName: Full=Processed zona pellucida sperm-binding protein 3;
Flags: Precursor;
Name=ZP3; Synonyms=ZPC;
Mesocricetus auratus (Golden hamster).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Mesocricetus.
NCBI_TaxID=10036;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovary;
PubMed=2257975; DOI=10.1016/0012-1606(90)90363-N;
Kinloch R.A., Ruiz-Seller B., Wassarman P.M.;
"Genomic organization and polypeptide primary structure of zona
pellucida glycoprotein hZP3, the hamster sperm receptor.";
Dev. Biol. 142:414-421(1990).
-!- 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: Polymers of ZP2 and ZP3 organized into long filaments
cross-linked by ZP1 homodimers. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Processed zona pellucida sperm-binding
protein 3: Secreted, extracellular space, extracellular matrix
{ECO:0000250|UniProtKB:P48833}. Note=The glycoproteinaceous
translucent extracellular matrix that surrounds the mammalian
oocyte is called zona pellucida. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P48833}; Single-pass type I membrane
protein {ECO:0000255}.
-!- TISSUE SPECIFICITY: Oocytes.
-!- DEVELOPMENTAL STAGE: Growing oocytes.
-!- DOMAIN: The ZP domain is involved in the polymerization of the ZP
proteins to form the zona pellucida.
-!- PTM: Proteolytically cleaved before the transmembrane segment to
yield the secreted ectodomain incorporated in the zona pellucida.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- PTM: O-glycosylated; removal of O-linked glycans may play an
important role in the post-fertilization block to polyspermy.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the ZP domain family. ZPC subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Molecular chastity
- Issue 93 of April 2008;
URL="https://web.expasy.org/spotlight/back_issues/093";
-----------------------------------------------------------------------
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EMBL; M63629; AAA37079.1; -; mRNA.
PIR; A60503; A60503.
RefSeq; NP_001268531.1; NM_001281602.1.
ProteinModelPortal; P23491; -.
SMR; P23491; -.
PRIDE; P23491; -.
GeneID; 101824371; -.
CTD; 7784; -.
HOVERGEN; HBG007985; -.
OrthoDB; EOG091G0AQ6; -.
Proteomes; UP000189706; Genome assembly.
GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
GO; GO:0030246; F:carbohydrate binding; ISS:UniProtKB.
GO; GO:0048018; F:receptor ligand activity; ISS:UniProtKB.
GO; GO:0007339; P:binding of sperm to zona pellucida; ISS:UniProtKB.
GO; GO:0001825; P:blastocyst formation; ISS:UniProtKB.
GO; GO:0035803; P:egg coat formation; ISS:UniProtKB.
GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; ISS:UniProtKB.
GO; GO:2000360; P:negative regulation of binding of sperm to zona pellucida; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0048599; P:oocyte development; ISS:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISS:UniProtKB.
GO; GO:2000368; P:positive regulation of acrosomal vesicle exocytosis; ISS:UniProtKB.
GO; GO:2000344; P:positive regulation of acrosome reaction; ISS:UniProtKB.
GO; GO:2000388; P:positive regulation of antral ovarian follicle growth; ISS:UniProtKB.
GO; GO:0090280; P:positive regulation of calcium ion import; ISS:UniProtKB.
GO; GO:0002922; P:positive regulation of humoral immune response; ISS:UniProtKB.
GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
GO; GO:0032753; P:positive regulation of interleukin-4 production; ISS:UniProtKB.
GO; GO:0002687; P:positive regulation of leukocyte migration; ISS:UniProtKB.
GO; GO:2000386; P:positive regulation of ovarian follicle development; ISS:UniProtKB.
GO; GO:0010513; P:positive regulation of phosphatidylinositol biosynthetic process; ISS:UniProtKB.
GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0001809; P:positive regulation of type IV hypersensitivity; ISS:UniProtKB.
InterPro; IPR001507; ZP_dom.
InterPro; IPR017977; ZP_dom_CS.
Pfam; PF00100; Zona_pellucida; 1.
PRINTS; PR00023; ZPELLUCIDA.
SMART; SM00241; ZP; 1.
PROSITE; PS00682; ZP_1; 1.
PROSITE; PS51034; ZP_2; 1.
2: Evidence at transcript level;
Cell membrane; Cleavage on pair of basic residues; Complete proteome;
Disulfide bond; Extracellular matrix; Fertilization; Glycoprotein;
Membrane; Pyrrolidone carboxylic acid; Receptor; Reference proteome;
Secreted; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 22 {ECO:0000250}.
CHAIN 23 349 Zona pellucida sperm-binding protein 3.
/FTId=PRO_0000041713.
CHAIN 23 ? Processed zona pellucida sperm-binding
protein 3.
/FTId=PRO_0000304571.
PROPEP 350 422 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000041714.
TOPO_DOM 23 386 Extracellular. {ECO:0000255}.
TRANSMEM 387 407 Helical. {ECO:0000255}.
TOPO_DOM 408 422 Cytoplasmic. {ECO:0000255}.
DOMAIN 45 306 ZP. {ECO:0000255|PROSITE-
ProRule:PRU00375}.
COMPBIAS 119 158 Pro-rich.
COMPBIAS 208 257 Pro-rich.
MOD_RES 23 23 Pyrrolidone carboxylic acid.
{ECO:0000250|UniProtKB:P21754}.
CARBOHYD 32 32 O-linked (GalNAc...) threonine.
{ECO:0000250}.
CARBOHYD 34 34 O-linked (GalNAc...) threonine.
{ECO:0000250}.
CARBOHYD 146 146 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 155 155 O-linked (GalNAc...) threonine.
{ECO:0000250}.
CARBOHYD 161 161 O-linked (GalNAc...) threonine.
{ECO:0000250}.
CARBOHYD 162 162 O-linked (GalNAc...) threonine.
{ECO:0000250}.
CARBOHYD 271 271 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 302 302 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
DISULFID 46 139 {ECO:0000250}.
DISULFID 78 98 {ECO:0000250}.
DISULFID 216 281 {ECO:0000250}.
DISULFID 238 299 {ECO:0000250}.
SEQUENCE 422 AA; 45827 MW; D0F95BE7FF8E7E01 CRC64;
MGLSYQLLLC LLLCGGAKQC CSQPLWLLPG GTPTPGKLTS SVEVECLEAE LVVTVSRDLF
GTGKLIQPED LTLGSENCRP LVSVATDVVR FKAQLHECSN RVQVTEDALV YSTVLLHQPR
PVPGLSILRT NRADVPIECR YPRQGNVSSH AIRPTWVPFS TTVSSEEKLV FSLRLMEENW
NTEKLSPTSH LGEVAYLQAE VQTGSHLPLL LFVDRCVPTP SPDQTASPYH VIVDFHGCLV
DGLSESFSAF QVPRPRPETL QFTVDVFHFA NSSRNTIYIT CHLKVTPANQ TPDELNKACS
FNRSSKSWSP VEGDAEVCGC CSSGDCGSSS RSRYQAHGVS QWPKSASRRR RHVRDEADVT
VGPLIFLGKA SDQAVEGWAS SAQTSLALGL GLAAVAFLTL AAIVLGVTRS CHTPSHVVSL
SQ


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