ID U3I3Z2_ANAPP Unreviewed; 551 AA.
AC U3I3Z2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 2.
DT 27-MAR-2024, entry version 49.
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};
GN Name=ZP4 {ECO:0000313|Ensembl:ENSAPLP00000001963.2};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000001963.2, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000001963.2, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000001963.2}
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 -!- 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; U3I3Z2; -.
DR STRING; 8840.ENSAPLP00000001963; -.
DR Ensembl; ENSAPLT00000002543.2; ENSAPLP00000001963.2; ENSAPLG00000002531.2.
DR GeneTree; ENSGT00940000161324; -.
DR HOGENOM; CLU_026010_1_0_1; -.
DR OMA; LNCPDQT; -.
DR Proteomes; UP000016666; Chromosome 6.
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:0032190; F:acrosin binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0060478; P:acrosomal vesicle exocytosis; IEA:Ensembl.
DR GO; GO:2000360; P:negative regulation of binding of sperm to zona pellucida; IEA:Ensembl.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; IEA:Ensembl.
DR GO; GO:0002922; P:positive regulation of humoral immune response; IEA:Ensembl.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
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|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..551
FT /note="Zona pellucida sperm-binding protein 4"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019838730"
FT TRANSMEM 515..536
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 149..192
FT /note="P-type"
FT /evidence="ECO:0000259|PROSITE:PS51448"
FT DOMAIN 197..470
FT /note="ZP"
FT /evidence="ECO:0000259|PROSITE:PS51034"
FT REGION 467..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 162..177
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00779"
SQ SEQUENCE 551 AA; 59193 MW; 947CF093AFB66540 CRC64;
MGVVGQARPV CGALFFWGLL GPFALVVGSQ GSFLDEPGLL ACGQDSLQLT LPVGWEGNVS
FVLTAWDTEG KAHALHNDSG CGLWVSGAPD GSRKVSVSYT SCYVFEWDGN YLMIVGLEGT
DATGQRVLQE EKLLRCPVDL PALDAPSSSV CSAVRSQDRL PCASSPVSQG DCEARGCCYN
PRDRVKTCYY GNTVTAHCTP DGQFSIAVSR DVTLPPVILD SVHLASGPSA GCTPVVKNSA
FVVYQFPLSA CGTTFQVTGG HAVYENELVA SRDVRTGSLG SVTRDSTFRL HVRCSYLITG
SFIPLSVQVF TLPPLPAVSQ PGPLSLELRV ASDKSYSSYY TDSDYPVVKA LRDPVYVEVR
ILQRTDPELV LVLHHCWATP SINPHQQMQW PVLVDGCPYA GDNYQTQLVP LSIASGLQFP
LHYQRFTLYT FTFVDSISQE MLSGLVYLHC SASVCHRSAQ ESCTTTCPAG ARGKRSADHN
IQDGASHVSS KGPVIFLQNE LRQGAAVDRA AVLAAAPWAL GFAAVATVVV VVASVLRWRK
VPVAHEVNAL Q
//
