ZP4_FELCA
ID ZP4_FELCA Reviewed; 570 AA.
AC P48834;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 107.
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 Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=7841460; DOI=10.3109/10425179409010186;
RA Harris J.D., Hibler D.W., Fontenot G.K., Hsu K.T., Yurewicz E.C.,
RA Sacco A.G.;
RT "Cloning and characterization of zona pellucida genes and cDNAs from a
RT variety of mammalian species: the ZPA, ZPB and ZPC gene families.";
RL DNA Seq. 4:361-393(1994).
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; U05777; AAA74389.1; -; mRNA.
DR PIR; S70400; S70400.
DR RefSeq; NP_001009260.1; NM_001009260.1.
DR AlphaFoldDB; P48834; -.
DR SMR; P48834; -.
DR STRING; 9685.ENSFCAP00000010184; -.
DR GeneID; 493791; -.
DR KEGG; fca:493791; -.
DR CTD; 57829; -.
DR eggNOG; ENOG502QU54; Eukaryota.
DR InParanoid; P48834; -.
DR OrthoDB; 586615at2759; -.
DR Proteomes; UP000011712; Unplaced.
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:0035804; F:structural constituent of egg coat; ISS:UniProtKB.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..496
FT /note="Zona pellucida sperm-binding protein 4"
FT /id="PRO_0000041725"
FT CHAIN 20..?
FT /note="Processed zona pellucida sperm-binding protein 4"
FT /id="PRO_0000304577"
FT PROPEP 497..570
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041726"
FT TOPO_DOM 20..545
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 546..566
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 567..570
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 177..218
FT /note="P-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DOMAIN 223..496
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 337
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 402..476
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
SQ SEQUENCE 570 AA; 62867 MW; 93CDCAA5B949B96D CRC64;
MWLLQPLLLC VPLSLAVHGQ QKPQVPDYPG ELHCGLQSLQ FAINPSPGKA TPALIVWDNR
GLPHKLQNNS GCGTWVRESP GGSVLLDASY SSCYVNEWVS TTQSPGTSRP PTPASRVTPQ
DSHYVMIVGV EGTDAAGRRV TNTKVLRCPR NPPDQALVSS LSPSPLQNVA LEAPNADLCD
SVPKWDRLPC ASSPITQGDC NKLGCCYKSE ANSCYYGNTV TSRCTQDGHF SIAVSRNVTS
PPLLLNSLRL AFGKDRECNP VKATRAFALF FFPFNSCGTT RWVTGDQAVY ENELVAARDV
RTWSHGSITR DSIFRLRVSC SYSVRSNAFP LSVQVFTIPP PHLKTQHGPL TLELKIAKDK
HYGSYYTIGD YPVVKLLRDP IYVEVSIRHR TDPSLGLLLH NCWATPGKNS QSLSQWPILV
KGCPYVGDNY QTQLIPVQKA LDTPFPSYYK RFSIFTFSFV DTMAKWALRG PVYLHCNVSI
CQPAGTSSCR ITCPVARRRR HSDLHHHSST ASISSKGPMI LLQATMDSAE KLHKNSSSPI
DSQALWMAGL SGTLIFGFLL VSYLAIRKRR
