ID A0A3L8RA93_CHLGU Unreviewed; 430 AA.
AC A0A3L8RA93;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Zona pellucida sperm-binding protein 3 {ECO:0000256|RuleBase:RU367066};
GN ORFNames=DV515_00016792 {ECO:0000313|EMBL:RLV76619.1}, DV515_00016795
GN {ECO:0000313|EMBL:RLV76620.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV76619.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLV76619.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLV76619.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLV76619.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
RN [2] {ECO:0000313|EMBL:RLV76619.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Red01 {ECO:0000313|EMBL:RLV76619.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLV76619.1};
RA Sabatino S.J.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLV76619.1}.
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DR EMBL; QUSF01000486; RLV76619.1; -; Genomic_DNA.
DR EMBL; QUSF01000485; RLV76620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8RA93; -.
DR STRING; 44316.ENSEGOP00005019362; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
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:UP000276834};
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 SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU367066"
FT CHAIN 20..430
FT /note="Zona pellucida sperm-binding protein 3"
FT /evidence="ECO:0000256|RuleBase:RU367066"
FT /id="PRO_5034121878"
FT TRANSMEM 400..424
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367066"
FT DOMAIN 64..327
FT /note="ZP"
FT /evidence="ECO:0000259|PROSITE:PS51034"
SQ SEQUENCE 430 AA; 46806 MW; 81BCF510A1329F56 CRC64;
MRSQIRLLLA LLCAAPAAAA PPPWDREWSD PNPWEWGEER WNSRPNSRSN SHWNSRPRAP
VEVQCREARL EVTVHRDLFG NGRLVSAAEL SLGPAACKHS RLDPSQKTVT FSAGLHECGS
TVQVTPDSLI YRTLLSYAPS PGSNPAIVRS DPAVIPIECH YPRRENVSSG SIRPTWAPFN
SALASQERLL FSLRLMNEDW SSERDLSAFR LGDVLNLQAE VGSHSHVPLR LFVDSCVATL
GPGAGSEPHY AIIDFNGCLV DGRSDATSSA FVTPRPRQDV LRFQIDAFRF AGDPRSLIYI
TCHLKVTPAE QSPDTLNKAC SFNKARNAWA PVEGTRDICS CCERGNCGQR PLEPWDGHRH
RRDDGHGATS EADIVIGPVL LSSAQQGQRP EGHQGAVTPL AVGTALACAV ATVAAAGAAL
AIGLRRRNSR
//