ZP4_BOVIN
ID ZP4_BOVIN Reviewed; 534 AA.
AC Q9BH11;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Zona pellucida sperm-binding protein 4;
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=ZPB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 326-339; 341-352;
RP 399-406 AND 435-446.
RC TISSUE=Ovary;
RX PubMed=11422390; DOI=10.1046/j.1432-1327.2001.02269.x;
RA Yonezawa N., Fukui N., Kuno M., Shinoda M., Goko S., Mitsui S., Nakano M.;
RT "Molecular cloning of bovine zona pellucida glycoproteins ZPA and ZPB and
RT analysis for sperm-binding component of the zona.";
RL Eur. J. Biochem. 268:3587-3594(2001).
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 -!- PTM: The N-terminus is blocked. {ECO:0000305}.
CC -!- PTM: Contains disulfide bond(s).
CC -!- SIMILARITY: Belongs to the ZP domain family. ZPB subfamily.
CC {ECO:0000305}.
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DR EMBL; AB042652; BAB21481.2; -; mRNA.
DR RefSeq; NP_776400.1; NM_173975.2.
DR AlphaFoldDB; Q9BH11; -.
DR SMR; Q9BH11; -.
DR STRING; 9913.ENSBTAP00000036829; -.
DR PaxDb; Q9BH11; -.
DR PRIDE; Q9BH11; -.
DR Ensembl; ENSBTAT00000036982; ENSBTAP00000036829; ENSBTAG00000026085.
DR GeneID; 280965; -.
DR KEGG; bta:280965; -.
DR CTD; 57829; -.
DR VEuPathDB; HostDB:ENSBTAG00000026085; -.
DR VGNC; VGNC:37367; ZP4.
DR eggNOG; ENOG502QU54; Eukaryota.
DR GeneTree; ENSGT00940000161324; -.
DR HOGENOM; CLU_034433_0_0_1; -.
DR InParanoid; Q9BH11; -.
DR OrthoDB; 586615at2759; -.
DR TreeFam; TF332794; -.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000026085; Expressed in oocyte and 2 other tissues.
DR ExpressionAtlas; Q9BH11; baseline.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0032190; F:acrosin binding; IBA:GO_Central.
DR GO; GO:0035804; F:structural constituent of egg coat; ISS:UniProtKB.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IPI:UniProtKB.
DR GO; GO:0060468; P:prevention of polyspermy; IBA:GO_Central.
DR CDD; cd00111; Trefoil; 1.
DR Gene3D; 2.60.40.4100; -; 1.
DR Gene3D; 4.10.110.10; -; 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 Pfam; PF00088; Trefoil; 1.
DR Pfam; PF00100; Zona_pellucida; 1.
DR SMART; SM00018; PD; 1.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF57492; SSF57492; 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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..461
FT /note="Zona pellucida sperm-binding protein 4"
FT /id="PRO_0000041723"
FT CHAIN 18..?
FT /note="Processed zona pellucida sperm-binding protein 4"
FT /id="PRO_0000304576"
FT PROPEP 462..534
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041724"
FT TOPO_DOM 18..509
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 531..534
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 141..183
FT /note="P-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DOMAIN 188..465
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 292
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 302
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 367..441
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
SQ SEQUENCE 534 AA; 59200 MW; F5B127166738C8CC CRC64;
MWLLLQLVWL CFLLSLGLNS WHQSKVPEYP DELRCGLRSF QFTINPLSQE TETPPVLVAW
DNHGLPHSLQ NDSDCGTWVS EGPGSSLVGE ASYSGCYVTE WESYYIMTVG IERAGVSGSG
AFIETKLFKC PVNLPDVPNA GLCDSVPVWD RLPCAPSPIT QGDCKQLGCC YNSEEVISCY
YGNTVTSHCT QDGHFSIAVS RNVTSPPLLL NSVHLAFRND SECKPVMATH TFVLFRFPFT
TCGTTKQITG KQAVYENELV AARDVRTWSR GSITRDSTFR LQVSCSYSAS SSALPVNVQV
LTLPPPLPET QPGNLTLELK IAKDKRYRSY YTASDYPVVK LLRDPIYVEV SIHQRTDPSL
ELRLDQCWAT PGADALLQPQ WPLLVNGCPY TGDNYQTKLI PVWEASDLPF PSHYQRFSIS
TFSFVDSVAK RALKGPVYLH CSASVCQPAG TPSCVTLCPA RRRRSSDIHF QNNTASISSK
GPLILLQAIQ DSSEKLHKYS RSPVDSQALW VAGLSGILIV GALFMSYLAI RKWR
