ID ZP4_PIG Reviewed; 536 AA.
AC Q07287;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 24-JAN-2024, entry version 148.
DE RecName: Full=Zona pellucida sperm-binding protein 4;
DE AltName: Full=Zona pellucida glycoprotein 3-alpha;
DE Short=Zp-3-alpha;
DE Short=Zp3-alpha;
DE AltName: Full=Zona pellucida glycoprotein 4;
DE Short=Zp-4;
DE AltName: Full=Zona pellucida protein B;
DE Contains:
DE RecName: Full=Processed zona pellucida sperm-binding protein 4;
DE Flags: Precursor;
GN Name=ZP4; Synonyms=ZP3A, ZPB;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=8357839; DOI=10.1016/0167-4781(93)90119-x;
RA Yurewicz E.C., Hibler D., Fontenot G.K., Sacco A.G., Harris J.;
RT "Nucleotide sequence of cDNA encoding ZP3 alpha, a sperm-binding
RT glycoprotein from zona pellucida of pig oocyte.";
RL Biochim. Biophys. Acta 1174:211-214(1993).
RN [2]
RP PROTEIN SEQUENCE OF 137-158.
RX PubMed=3643212; DOI=10.1016/s0021-9258(19)75834-7;
RA Yurewicz E.C., Sacco A.G., Subramanian M.G.;
RT "Biochemical research on oogenesis. Binding of tRNA to the nucleoprotein
RT particles of Xenopus laevis previtellogenic oocytes.";
RL J. Biol. Chem. 262:654-659(1987).
RN [3]
RP PROTEIN SEQUENCE OF 284-318, AND GLYCOSYLATION.
RX PubMed=1418987; DOI=10.1002/mrd.1080330210;
RA Yurewicz E.C., Pack B.A., Sacco A.G.;
RT "Porcine oocyte zona pellucida M(r) 55,000 glycoproteins: identification of
RT O-glycosylated domains.";
RL Mol. Reprod. Dev. 33:182-188(1992).
RN [4]
RP GLYCOSYLATION AT ASN-203; ASN-220 AND ASN-333.
RX PubMed=9546665; DOI=10.1046/j.1432-1327.1998.2520492.x;
RA Kudo K., Yonezawa N., Katsumata T., Aoki H., Nakano M.;
RT "Localization of carbohydrate chains of pig sperm ligand in the
RT glycoprotein ZPB of egg zona pellucida.";
RL Eur. J. Biochem. 252:492-499(1998).
RN [5]
RP PROTEOLYTIC PROCESSING.
RX PubMed=12878193; DOI=10.1016/s0006-291x(03)01297-x;
RA Yonezawa N., Nakano M.;
RT "Identification of the carboxyl termini of porcine zona pellucida
RT glycoproteins ZPB and ZPC.";
RL Biochem. Biophys. Res. Commun. 307:877-882(2003).
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.
CC -!- SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein
CC 4]: Zona pellucida {ECO:0000250|UniProtKB:Q00193}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q00193};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in oocytes.
CC -!- DOMAIN: The ZP domain is involved in the polymerization of the ZP
CC proteins to form the zona pellucida.
CC -!- PTM: Proteolytically cleaved before the transmembrane segment to yield
CC the secreted ectodomain incorporated in the zona pellucida.
CC {ECO:0000269|PubMed:12878193}.
CC -!- PTM: Disulfide bonds are formed between the cysteines of three
CC consecutive regions: Cys-368 and Cys-389, Cys-442 and Cys-447, Cys-455
CC and Cys-459.
CC -!- PTM: N-glycosylated; contains bi-, tri- and tetra-antennary glycans
CC with N-acetyllactosamine repeats.
CC -!- PTM: O-glycosylated; contains sulfate-substituted glycans.
CC -!- SIMILARITY: Belongs to the ZP domain family. ZPB subfamily.
CC {ECO:0000305}.
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DR EMBL; L11000; AAA50164.1; -; mRNA.
DR PIR; S35712; S35712.
DR RefSeq; NP_999210.1; NM_214045.1.
DR AlphaFoldDB; Q07287; -.
DR SMR; Q07287; -.
DR BioGRID; 1149246; 1.
DR STRING; 9823.ENSSSCP00000010814; -.
DR GlyConnect; 636; 6 N-Linked glycans.
DR GlyCosmos; Q07287; 7 sites, 10 glycans.
DR iPTMnet; Q07287; -.
DR PaxDb; 9823-ENSSSCP00000010814; -.
DR Ensembl; ENSSSCT00000011102.4; ENSSSCP00000010814.2; ENSSSCG00000010141.4.
DR Ensembl; ENSSSCT00035038683.1; ENSSSCP00035015446.1; ENSSSCG00035029218.1.
DR Ensembl; ENSSSCT00055028754.1; ENSSSCP00055022915.1; ENSSSCG00055014571.1.
DR Ensembl; ENSSSCT00070036553.1; ENSSSCP00070030564.1; ENSSSCG00070018498.1.
DR GeneID; 397111; -.
DR KEGG; ssc:397111; -.
DR CTD; 57829; -.
DR VGNC; VGNC:95319; ZP4.
DR eggNOG; ENOG502QU54; Eukaryota.
DR GeneTree; ENSGT00940000161324; -.
DR HOGENOM; CLU_034433_0_0_1; -.
DR InParanoid; Q07287; -.
DR OMA; LNCPDQT; -.
DR OrthoDB; 5354962at2759; -.
DR TreeFam; TF332794; -.
DR Reactome; R-SSC-2534343; Interaction With Cumulus Cells And The Zona Pellucida.
DR Proteomes; UP000008227; Chromosome 14.
DR Proteomes; UP000314985; Chromosome 14.
DR Proteomes; UP000694570; Unplaced.
DR Proteomes; UP000694571; Unplaced.
DR Proteomes; UP000694720; Unplaced.
DR Proteomes; UP000694722; Unplaced.
DR Proteomes; UP000694723; Unplaced.
DR Proteomes; UP000694724; Unplaced.
DR Proteomes; UP000694725; Unplaced.
DR Proteomes; UP000694726; Unplaced.
DR Proteomes; UP000694727; Unplaced.
DR Proteomes; UP000694728; Unplaced.
DR Bgee; ENSSSCG00000010141; Expressed in oocyte and 3 other cell types or tissues.
DR Genevisible; Q07287; SS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0035805; C:egg coat; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0035804; F:structural constituent of egg coat; ISS:UniProtKB.
DR GO; GO:0060478; P:acrosomal vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IBA:GO_Central.
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 GO; GO:0060468; P:prevention of polyspermy; IBA:GO_Central.
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; 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; PF00088; Trefoil; 1.
DR Pfam; PF00100; Zona_pellucida; 1.
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; PS00682; ZP_1; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Fertilization; Glycoprotein; Membrane; Receptor; Reference proteome;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..462
FT /note="Zona pellucida sperm-binding protein 4"
FT /id="PRO_0000041729"
FT CHAIN 22..?
FT /note="Processed zona pellucida sperm-binding protein 4"
FT /id="PRO_0000304579"
FT PROPEP 463..536
FT /note="Removed in mature form"
FT /id="PRO_0000041730"
FT TOPO_DOM 22..511
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 533..536
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 142..184
FT /note="P-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DOMAIN 189..462
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:9546665"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:9546665"
FT CARBOHYD 293
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:1418987"
FT CARBOHYD 303
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1418987"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:9546665"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 368..442
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
SQ SEQUENCE 536 AA; 59334 MW; 1EA38E587A7F6CB0 CRC64;
MWLRPSIWLC FPLCLALPGQ SQPKAADDLG GLYCGPSSFH FSINLLSQDT ATPPALVVWD
RRGRLHKLQN DSGCGTWVHK GPGSSMGVEA SYRGCYVTEW DSHYLMPIGL EEADAGGHRT
VTETKLFKCP VDFLALDVPT IGLCDAVPVW DRLPCAPPPI TQGECKQLGC CYNSEEVPSC
YYGNTVTSRC TQDGHFSIAV SRNVTSPPLL WDSVHLAFRN DSECKPVMET HTFVLFRFPF
SSCGTAKRVT GNQAVYENEL VAARDVRTWS HGSITRDSIF RLRVSCIYSV SSSALPVNIQ
VFTLPPPLPE THPGPLTLEL QIAKDERYGS YYNASDYPVV KLLREPIYVE VSIRHRTDPS
LGLHLHQCWA TPGMSPLLQP QWPMLVNGCP YTGDNYQTKL IPVQKASNLL FPSHYQRFSV
STFSFVDSVA KQALKGPVYL HCTASVCKPA GAPICVTTCP AARRRRSSDI HFQNGTASIS
SKGPMILLQA TRDSSERLHK YSRPPVDSHA LWVAGLLGSL IIGALLVSYL VFRKWR
//
