ZP4_RAT
ID ZP4_RAT Reviewed; 545 AA.
AC Q8CH34;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 99.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Kuwahara A., Hennebold J.D., King G., Adashi E.Y.;
RT "Genetic determinants of the transition from the afollicular ovary to one
RT dominated by fully-formed primordial follicles: marked increments in the
RT ovarian expression of the rat zona pellucida 4 gene.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the ZP domain family. ZPB subfamily.
CC {ECO:0000305}.
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DR EMBL; AF456325; AAN76981.1; -; mRNA.
DR AlphaFoldDB; Q8CH34; -.
DR SMR; Q8CH34; -.
DR STRING; 10116.ENSRNOP00000031597; -.
DR GlyGen; Q8CH34; 6 sites.
DR PaxDb; Q8CH34; -.
DR PRIDE; Q8CH34; -.
DR UCSC; RGD:628708; rat.
DR RGD; 628708; Zp4.
DR eggNOG; ENOG502QU54; Eukaryota.
DR InParanoid; Q8CH34; -.
DR PhylomeDB; Q8CH34; -.
DR PRO; PR:Q8CH34; -.
DR Proteomes; UP000002494; Unplaced.
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:0032190; F:acrosin binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0035804; F:structural constituent of egg coat; ISS:UniProtKB.
DR GO; GO:0060478; P:acrosomal vesicle exocytosis; ISO:RGD.
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; ISO:RGD.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; ISO:RGD.
DR GO; GO:0002922; P:positive regulation of humoral immune response; ISO:RGD.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:RGD.
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 PRINTS; PR00023; ZPELLUCIDA.
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 2: Evidence at transcript level;
KW Cell membrane; Cleavage on pair of basic residues; Disulfide bond;
KW Extracellular matrix; Fertilization; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..471
FT /note="Zona pellucida sperm-binding protein 4"
FT /id="PRO_0000041733"
FT CHAIN 29..?
FT /note="Processed zona pellucida sperm-binding protein 4"
FT /id="PRO_0000304581"
FT PROPEP 472..545
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041734"
FT TOPO_DOM 29..518
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..545
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 148..192
FT /note="P-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DOMAIN 197..471
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 312
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 377..451
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
SQ SEQUENCE 545 AA; 59874 MW; 159F29E68D2884FB CRC64;
MARQALRSTL WLLPSILLCF PFCLPLSGQH VTELPGVLHC GLQSFQFAVN LSLEAESPVL
TTWDSQGLPH RLKNDSDCGT WVMDSPDGFL VLEASYSGCY VTLEGSHYIM TVGVQEADVA
GHVAGTRQRL LTCPLALQGK APDTPNAKVC SPVPVKERLP CASSTISRGD CEELGCCYSS
EEEGADSCYY GNTVTSHCTK EGHFSIAVSR DVTSPPLRLD SLRLGFRNIT TGCDPVMKTS
TFVLFQFPLT SCGTTQRITG DQAMYENELV AIRDVQAWGR SSITRDSNFR LRVSCTYSIH
SIMSPVNMQV WTLPPPLPKT QPGPLSLELQ IAQDKNYSSY YGTDAYPLVK FLQDPIYVEV
SILHRTDPSL SLLLEQCWAT PGSNPFHQPQ WPILVKGCPY AGDNYQTKRI PVQKASDVFP
SHHQRFSIST FSFMSAGREK QVLGGQVYLH CSASVCQPAG MPSCTVICPA SRRRRKSELY
FDNSTSISSK GPVILLQATK DPAVMLHKHS GTHADSPTLW VMGLSASMVI TGVLVVSYLA
TRKQR
