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Database: UniProt
Entry: A0A3L8RA93_CHLGU
LinkDB: A0A3L8RA93_CHLGU
Original site: A0A3L8RA93_CHLGU 
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
//
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