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Database: UniProt
Entry: I3KC81_ORENI
LinkDB: I3KC81_ORENI
Original site: I3KC81_ORENI 
ID   I3KC81_ORENI            Unreviewed;       389 AA.
AC   I3KC81;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Zona pellucida sperm-binding protein 4 {ECO:0000256|ARBA:ARBA00040238};
DE   AltName: Full=Zona pellucida glycoprotein 4 {ECO:0000256|ARBA:ARBA00042573};
DE   AltName: Full=Zona pellucida protein B {ECO:0000256|ARBA:ARBA00042273};
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000018726.2, ECO:0000313|Proteomes:UP000005207};
RN   [1] {ECO:0000313|Proteomes:UP000005207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Broad Institute Genome Assembly Team;
RG   Broad Institute Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSONIP00000018726.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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       ZP4 may act as a sperm receptor. {ECO:0000256|ARBA:ARBA00037545}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004479}. Zona pellucida
CC       {ECO:0000256|ARBA:ARBA00024183}.
CC   -!- SIMILARITY: Belongs to the ZP domain family. ZPB subfamily.
CC       {ECO:0000256|ARBA:ARBA00010863}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00779}.
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DR   AlphaFoldDB; I3KC81; -.
DR   STRING; 8128.ENSONIP00000040535; -.
DR   Ensembl; ENSONIT00000018743.2; ENSONIP00000018726.2; ENSONIG00000014876.2.
DR   eggNOG; ENOG502QU54; Eukaryota.
DR   GeneTree; ENSGT00940000163253; -.
DR   HOGENOM; CLU_026010_2_0_1; -.
DR   TreeFam; TF332794; -.
DR   Proteomes; UP000005207; Linkage group LG7.
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:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR   CDD; cd00111; Trefoil; 1.
DR   Gene3D; 4.10.110.10; Spasmolytic Protein, domain 1; 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; IPR017957; P_trefoil_CS.
DR   InterPro; IPR000519; P_trefoil_dom.
DR   InterPro; IPR044913; P_trefoil_dom_sf.
DR   InterPro; IPR042235; ZP-C.
DR   InterPro; IPR048290; ZP_chr.
DR   InterPro; IPR001507; ZP_dom.
DR   PANTHER; PTHR23343; ZONA PELLUCIDA SPERM-BINDING PROTEIN; 1.
DR   PANTHER; PTHR23343:SF31; ZONA PELLUCIDA SPERM-BINDING PROTEIN 4; 1.
DR   Pfam; PF00088; Trefoil; 1.
DR   Pfam; PF00100; Zona_pellucida; 1.
DR   PRINTS; PR00023; ZPELLUCIDA.
DR   SMART; SM00018; PD; 1.
DR   SMART; SM00241; ZP; 1.
DR   SUPFAM; SSF57492; Trefoil; 1.
DR   PROSITE; PS00025; P_TREFOIL_1; 1.
DR   PROSITE; PS51448; P_TREFOIL_2; 1.
DR   PROSITE; PS51034; ZP_2; 1.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00779}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Fertilization {ECO:0000256|ARBA:ARBA00023279};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          38..76
FT                   /note="P-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51448"
FT   DOMAIN          81..361
FT                   /note="ZP"
FT                   /evidence="ECO:0000259|PROSITE:PS51034"
FT   DISULFID        40..66
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00779"
FT   DISULFID        50..65
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00779"
SQ   SEQUENCE   389 AA;  43764 MW;  E9598A6829784035 CRC64;
     QHICRILFTE SAVLFCEVMQ PQQPRKPQNP QKPLEPFHTC EVAENYKIPC GTNEISASEC
     DTINCCFDGR MCYYGKSVTL QCTKEGLFIV VVARDATLPN IDLETVSFYE NGHSCNPVGS
     TSAFAIYEFP VTACGTIVKE EPGVLIYENR MSSLYQVITG PHGSITRDTY YELLFQCRYV
     GTTVEALVID IGLVPPPNSV AAAGPVRVEL KLANGQCVAK GCVEEEEVYT SFYTAAKYPV
     RKVLRDPVYV EVYLMERTDP NLVLTLGRCW ATSDSYPHSL PQWDLLIDGC PYRDDRYLTT
     LLLRPSSGFK FPPQPLSKNI FLFISCPFFF FLFFDQLYIH CNVAICQPTL GNNCEPRWRE
     IAGSVKKVTR EETTVVSSPG LIFVERSTE
//
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