ID ZP3_MACRA Reviewed; 424 AA. AC P53785; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 02-SEP-2026, entry version 107. DE RecName: Full=Zona pellucida sperm-binding protein 3; DE AltName: Full=Sperm receptor; DE AltName: Full=Zona pellucida glycoprotein 3; DE Short=Zp-3; DE AltName: Full=Zona pellucida protein C; DE Contains: DE RecName: Full=Processed zona pellucida sperm-binding protein 3; DE Flags: Precursor; GN Name=ZP3; Synonyms=ZPC; OS Macaca radiata (Bonnet macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9548; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Ovary; RX PubMed=8848588; DOI=10.1071/rd9951209; RA Kolluri S.K., Kaul R., Banerjee K., Gupta S.K.; RT "Nucleotide sequence of cDNA encoding bonnet monkey (Macaca radiata) zona RT pellucida glycoprotein-ZP3."; RL Reprod. Fertil. Dev. 7:1209-1212(1995). CC -!- FUNCTION: Component of the zona pellucida, an extracellular matrix CC surrounding oocytes which mediates sperm binding, induction of the CC acrosome reaction and prevents post-fertilization polyspermy. The zona CC pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. CC ZP3 is essential for sperm binding and zona matrix formation. CC -!- SUBUNIT: Polymers of ZP2 and ZP3 organized into long filaments cross- CC linked by ZP1 homodimers. Interacts with ZP1 and ZP2. CC {ECO:0000250|UniProtKB:P20239, ECO:0000250|UniProtKB:P21754}. CC -!- SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein CC 3]: Zona pellucida {ECO:0000250|UniProtKB:P21754}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P48833}; CC Single-pass type I membrane protein {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Expressed in oocytes. CC -!- DOMAIN: The ZP domain is involved in the polymerization of the ZP CC proteins to form the zona pellucida. CC -!- PTM: Proteolytically cleaved before the transmembrane segment to yield CC the secreted ectodomain incorporated in the zona pellucida. CC -!- PTM: N-glycosylated. {ECO:0000250}. CC -!- PTM: O-glycosylated; removal of O-linked glycans may play an important CC role in the post-fertilization block to polyspermy. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ZP domain family. ZPC subfamily. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Molecular chastity - Issue CC 93 of April 2008; CC URL="https://www.proteinspotlight.org/back_issues/093"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X82639; CAA57961.1; -; mRNA. DR AlphaFoldDB; P53785; -. DR SMR; P53785; -. DR GlyCosmos; P53785; 6 sites, No reported glycans. DR PRO; PR:P53785; -. DR GO; GO:0035805; C:egg coat; ISS:UniProtKB. DR GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB. DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0032190; F:acrosin binding; IEA:TreeGrafter. DR GO; GO:0030246; F:carbohydrate binding; ISS:UniProtKB. DR GO; GO:0048018; F:receptor ligand activity; ISS:UniProtKB. DR GO; GO:0035804; F:structural constituent of egg coat; ISS:UniProtKB. DR GO; GO:0007339; P:binding of sperm to zona pellucida; ISS:UniProtKB. DR GO; GO:0001825; P:blastocyst formation; ISS:UniProtKB. DR GO; GO:0035803; P:egg coat formation; ISS:UniProtKB. DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; ISS:UniProtKB. DR GO; GO:2000360; P:negative regulation of binding of sperm to zona pellucida; ISS:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0048599; P:oocyte development; ISS:UniProtKB. DR GO; GO:2000368; P:positive regulation of acrosomal vesicle exocytosis; ISS:UniProtKB. DR GO; GO:2000344; P:positive regulation of acrosome reaction; ISS:UniProtKB. DR GO; GO:2000388; P:positive regulation of antral ovarian follicle growth; ISS:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0002922; P:positive regulation of humoral immune response; ISS:UniProtKB. DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB. DR GO; GO:0032753; P:positive regulation of interleukin-4 production; ISS:UniProtKB. DR GO; GO:0002687; P:positive regulation of leukocyte migration; ISS:UniProtKB. DR GO; GO:2000386; P:positive regulation of ovarian follicle development; ISS:UniProtKB. DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB. DR GO; GO:0032729; P:positive regulation of type II interferon production; ISS:UniProtKB. DR GO; GO:0001809; P:positive regulation of type IV hypersensitivity; ISS:UniProtKB. DR FunFam; 2.60.40.3210:FF:000001; Zona pellucida sperm-binding protein 3; 1. DR FunFam; 2.60.40.4100:FF:000002; Zona pellucida sperm-binding protein 3; 1. DR Gene3D; 2.60.40.4100; Zona pellucida, ZP-C domain; 1. DR Gene3D; 2.60.40.3210; Zona pellucida, ZP-N domain; 1. DR InterPro; IPR055355; ZP-C. DR InterPro; IPR042235; ZP-C_dom. DR InterPro; IPR055356; ZP-N. DR InterPro; IPR048290; ZP_chr. DR InterPro; IPR001507; ZP_dom. DR InterPro; IPR017977; ZP_dom_CS. DR PANTHER; PTHR11576; ZONA PELLUCIDA SPERM-BINDING PROTEIN 3; 1. DR PANTHER; PTHR11576:SF2; ZONA PELLUCIDA SPERM-BINDING PROTEIN 3; 1. DR Pfam; PF00100; Zona_pellucida; 1. DR Pfam; PF23344; ZP-N; 1. DR PRINTS; PR00023; ZPELLUCIDA. DR SMART; SM00241; ZP; 1. DR PROSITE; PS00682; ZP_1; 1. DR PROSITE; PS51034; ZP_2; 1. PE 2: Evidence at transcript level; KW Cell membrane; Cleavage on pair of basic residues; Disulfide bond; KW Extracellular matrix; Fertilization; Glycoprotein; Membrane; KW Pyrrolidone carboxylic acid; Receptor; Secreted; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..22 FT /evidence="ECO:0000250" FT CHAIN 23..350 FT /note="Zona pellucida sperm-binding protein 3" FT /id="PRO_0000041711" FT CHAIN 23..? FT /note="Processed zona pellucida sperm-binding protein 3" FT /id="PRO_0000304570" FT PROPEP 351..424 FT /note="Removed in mature form" FT /evidence="ECO:0000250" FT /id="PRO_0000041712" FT TOPO_DOM 23..387 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 388..408 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 409..424 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 45..307 FT /note="ZP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375" FT MOD_RES 23 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000250|UniProtKB:P21754" FT CARBOHYD 125 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000250" FT CARBOHYD 147 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000250" FT CARBOHYD 156 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000250" FT CARBOHYD 162 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000250" FT CARBOHYD 163 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000250" FT CARBOHYD 272 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000250" FT DISULFID 46..140 FT /evidence="ECO:0000250" FT DISULFID 78..99 FT /evidence="ECO:0000250" FT DISULFID 217..282 FT /evidence="ECO:0000250" FT DISULFID 239..300 FT /evidence="ECO:0000250" SQ SEQUENCE 424 AA; 47040 MW; 3B41C4CFA3792331 CRC64; MELSYRLFIC LLLWGSTELC YPQPFWLLQG GASRAETSVQ PVLVECREAT LLVTVSKDLF GTGKLIRAAD LTLGPEACEP LVSMDTEDVV RFEVGLHECG SSMQVTDDAL VYSTFLLHDP RPVGNLSIVR TNRAEIPIEC RYPRQGNVSS QAILPTWLPF RTTVFSEEKL TFSLRLMEEN WNAEKRSPTF HLGDAAHLQA EIHTGSHVPL RLFVDHCVAT PTPDQNASPY HTIVDFHGCL VDGLTDASSA FKVPRPGPDT LQFTVDVFHF ANDSRNMIYI TCHLKAIPAE QEPDELNKAC SFSKSSNSWF PVEGPADICQ CCSKGDCGTP SHSRRQPHVV SQWSRSASRN RRHVTEEADI TVGPLIFLDR SADYEVEQWA LPADTSVLLL GIGLAVVASL TLTAVILIFT RRWRTASRPV SASE //