ID A0A3B4CHY9_PYGNA Unreviewed; 380 AA.
AC A0A3B4CHY9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Zona pellucida sperm-binding protein 3 {ECO:0000256|RuleBase:RU367066};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000010441.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000010441.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 {ECO:0000256|RuleBase:RU367066}.
CC -!- SUBCELLULAR LOCATION: Zona pellucida {ECO:0000256|RuleBase:RU367066}.
CC Cell membrane {ECO:0000256|RuleBase:RU367066}; Single-pass type I
CC membrane protein {ECO:0000256|RuleBase:RU367066}.
CC -!- DOMAIN: The ZP domain is involved in the polymerization of the ZP
CC proteins to form the zona pellucida. {ECO:0000256|RuleBase:RU367066}.
CC -!- PTM: Proteolytically cleaved before the transmembrane segment to yield
CC the secreted ectodomain incorporated in the zona pellucida.
CC {ECO:0000256|RuleBase:RU367066}.
CC -!- SIMILARITY: Belongs to the ZP domain family. ZPC subfamily.
CC {ECO:0000256|RuleBase:RU367066}.
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 AlphaFoldDB; A0A3B4CHY9; -.
DR STRING; 42514.ENSPNAP00000010441; -.
DR Ensembl; ENSPNAT00000017105.1; ENSPNAP00000010441.1; ENSPNAG00000016007.1.
DR GeneTree; ENSGT01030000234567; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0035805; C:egg coat; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035804; F:structural constituent of egg coat; IEA:UniProtKB-UniRule.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:UniProtKB-UniRule.
DR GO; GO:0035803; P:egg coat formation; IEA:UniProtKB-UniRule.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; IEA:UniProtKB-UniRule.
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; IPR042235; ZP-C.
DR InterPro; IPR001507; ZP_dom.
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 SMART; SM00241; ZP; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|RuleBase:RU367066};
KW Cleavage on pair of basic residues {ECO:0000256|RuleBase:RU367066};
KW Disulfide bond {ECO:0000256|RuleBase:RU367066};
KW Extracellular matrix {ECO:0000256|RuleBase:RU367066};
KW Membrane {ECO:0000256|RuleBase:RU367066};
KW Secreted {ECO:0000256|RuleBase:RU367066};
KW Signal {ECO:0000256|RuleBase:RU367066};
KW Transmembrane {ECO:0000256|RuleBase:RU367066};
KW Transmembrane helix {ECO:0000256|RuleBase:RU367066}.
FT TRANSMEM 357..379
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367066"
FT DOMAIN 110..377
FT /note="ZP"
FT /evidence="ECO:0000259|PROSITE:PS51034"
SQ SEQUENCE 380 AA; 42168 MW; 67E87E35B7C15CC2 CRC64;
GLYRAQTSTL LNTFGMNQNI DCKPDLSSSI SFKEPSSSNQ WEICISPAWA SVSDSCPGKP
KLSQLLKPII YSLNIQPHQQ LQGLVKKVIW RFPDVPQPPK QPPVQFQLRE PVPQNAVVEV
KQDSFGAGQL LTPSAFMLGG GGPSGQDGAA NVLVLESELQ ACNSALRVTP WLTNDVLIYS
FMLTFTPVAI QGTSIIRTNW HSGDVACTNL VVHLSDIFVN CSVKRISTSH YSCKYIQYID
MWLLADDWTY EWPSIQCLLG DLFNIQASVM KFNHVPLFVF ADSCVVTPVK DANAVPQYSI
IDNHGCLVDA KITGSSSCLH SKIRVTSCSF SWRLSASSFQ QDTVAMYIMV YYGFRNPVFM
CIMTLLALLC DYLCCISCIR
//
