ID A0A3Q4GFV1_NEOBR Unreviewed; 435 AA.
AC A0A3Q4GFV1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Zona pellucida sperm-binding protein 3 {ECO:0000256|RuleBase:RU367066};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000001872.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000001872.1}
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}.
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DR RefSeq; XP_006789538.1; XM_006789475.1.
DR AlphaFoldDB; A0A3Q4GFV1; -.
DR STRING; 32507.ENSNBRP00000001872; -.
DR Ensembl; ENSNBRT00000001949.1; ENSNBRP00000001872.1; ENSNBRG00000001316.1.
DR GeneID; 102800271; -.
DR GeneTree; ENSGT01030000234567; -.
DR OMA; CSYINGW; -.
DR OrthoDB; 4263824at2759; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000001316; Expressed in blood and 1 other cell type or tissue.
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; IPR048290; ZP_chr.
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 PRINTS; PR00023; ZPELLUCIDA.
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 Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW Secreted {ECO:0000256|RuleBase:RU367066};
KW Signal {ECO:0000256|RuleBase:RU367066}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU367066"
FT CHAIN 22..435
FT /note="Zona pellucida sperm-binding protein 3"
FT /evidence="ECO:0000256|RuleBase:RU367066"
FT /id="PRO_5025712719"
FT DOMAIN 77..336
FT /note="ZP"
FT /evidence="ECO:0000259|PROSITE:PS51034"
SQ SEQUENCE 435 AA; 47374 MW; E7219AC991D702C5 CRC64;
MLLKCATVCL VALALLGLCD AQGGFVPGVW APESQQQKQI FEKPLTWKYP EDPKPKPKPD
VPFQLRYPVS ASSVAVDCRE DIVHVEVKKD FFGVGQLINS ADLTLGSCAV VGEDIPAQVL
IYQAQLQNCG STLKMTGDSF IYTFTLNYNP QPVGDSAVIR TNKAAVVVEC HYQRKHNVSS
LALDPLWVPY SVAKMAQEFL YFTLTLMTED WKNERPSNQY FLGDEINFEV SVMQYHHVPL
RVYVDKCVAT VSADATSSPR YAFIEQGCMI DGRLTGSISR FLDRTAENKL QFQLESFKFQ
NDNVGKLYIT CHLRATSVAQ VIDSNHRACS YIRGWKEAAG YDGACGSCES LTGGQTGIGI
ISGTTGGGHG NIGTGSTGTG TTGTGTGNIG GGTPVNPIKQ VSWLRGTRDV SQQEVLEWEG
EVTLGPISIE EKNIA
//
