ID A0A3B3SJF0_9TELE Unreviewed; 378 AA.
AC A0A3B3SJF0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000030136.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000030136.1}
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 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00779}.
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DR AlphaFoldDB; A0A3B3SJF0; -.
DR Ensembl; ENSPKIT00000010943.1; ENSPKIP00000030136.1; ENSPKIG00000010973.1.
DR GeneTree; ENSGT00940000163253; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0035805; C:egg coat; IEA:UniProtKB-SubCell.
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; 2.60.40.4100; Zona pellucida, ZP-C domain; 1.
DR Gene3D; 2.60.40.3210; Zona pellucida, ZP-N domain; 1.
DR InterPro; IPR000519; P_trefoil_dom.
DR InterPro; IPR044913; P_trefoil_dom_sf.
DR InterPro; IPR042235; ZP-C.
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; PF00100; Zona_pellucida; 1.
DR SMART; SM00018; PD; 1.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF57492; Trefoil; 1.
DR PROSITE; PS51448; P_TREFOIL_2; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 4: Predicted;
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 Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 1..330
FT /note="ZP"
FT /evidence="ECO:0000259|PROSITE:PS51034"
FT DOMAIN 53..91
FT /note="P-type"
FT /evidence="ECO:0000259|PROSITE:PS51448"
FT DISULFID 65..80
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00779"
SQ SEQUENCE 378 AA; 40951 MW; 889B36C9D8D2E8F2 CRC64;
AGTQASLLLI TLLTFIMEKS RCIRQLWVHA SVLLAVLAVS FAQNTAVKGF VSTSAKCQVY
EQVPCGDPAF GKAACEAINC CFDGQQCYYG NAVTVQCTRD GQFVLVVAKD STVPQLDVAS
LSLLGGNAAP CLPVATTNAF AIYTFPVTAC GTVVKLDGDY VVYENRMTSS YEVGVGPLGS
ITRDSLYELL FQSAAYTSYY QDSDYPITKV LRQPVYVEVR ILNRTDPNLV LVLEDCWAAA
GLDPLSLPQW SLLVDGCPYQ GDKYQTTLVP VDGSSGLPFP THYKRFIVKM FTFVDPASHP
AVSLQGFIHC SVAVCRPSAT DSCEQRCFRK VTAATSPSQP LVLLCWGGWC WIVGLIKCHV
WFALVAESVS ASRGFQGG
//
