ID A0A3B3TCM6_9TELE Unreviewed; 472 AA.
AC A0A3B3TCM6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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:ENSPKIP00000041032.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000041032.1}
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; A0A3B3TCM6; -.
DR STRING; 1676925.ENSPKIP00000041032; -.
DR Ensembl; ENSPKIT00000022062.1; ENSPKIP00000041032.1; ENSPKIG00000017712.1.
DR GeneTree; ENSGT00940000163253; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0005576; C:extracellular region; 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; IPR048290; ZP_chr.
DR InterPro; IPR001507; ZP_dom.
DR InterPro; IPR017977; ZP_dom_CS.
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 PRINTS; PR00023; ZPELLUCIDA.
DR SMART; SM00018; PD; 1.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF57492; Trefoil; 1.
DR PROSITE; PS51448; P_TREFOIL_2; 1.
DR PROSITE; PS00682; ZP_1; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 105..144
FT /note="P-type"
FT /evidence="ECO:0000259|PROSITE:PS51448"
FT DOMAIN 149..430
FT /note="ZP"
FT /evidence="ECO:0000259|PROSITE:PS51034"
FT DISULFID 118..133
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00779"
SQ SEQUENCE 472 AA; 51577 MW; C4F6088885F702F8 CRC64;
MLACFQSEGT TPADNDFWNI KVKGRQIISL ISFNTIGKMP SGPCDLFILS LARLCKTSDS
VIYILVIDDA SFLQICLSLD NVKQDHSSLY EYPTCQSSIF CHPYTETEIQ SICDKVPCGG
PAISKDACAA INCCFDGQQC YYGNAVTMQC TSDGQFVVVV AKDSTVPQLD VTSISMLGGK
AAPCSPVATT DAFAIFTFPV TACGTVVKVG LYENRMSSSY EVGVGPLGSI TRDSLYELLF
QCRYWGTEVV SLVAEYQPIA ADMPFPLVVP GPLRVELRLA NGQCYTKGCD EGAAAYTSYY
QDSDYPVTKW LRQPVYVEVR LLSRTDPNLV LLLDSCWATP TPDPLSLPQW SLLETGCPNP
GDKYLTTLVP VDGSSGLPFP TYYKRFIVQM FAFVDPASKH HLQGQVFFHC STAVCAPSAT
DSCEQRCFRK VEGGVKTISP RGSIKYLFAC GEVENETANW SKEVLSGSFS HS
//