ZP4_RABIT
ID ZP4_RABIT Reviewed; 540 AA.
AC Q00193;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Zona pellucida sperm-binding protein 4;
DE AltName: Full=RC55;
DE AltName: Full=Zona pellucida glycoprotein 4;
DE Short=Zp-4;
DE AltName: Full=Zona pellucida glycoprotein X;
DE Short=Zp-X;
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, ZPX;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 25-49.
RC TISSUE=Ovary;
RX PubMed=1707882; DOI=10.1016/s0021-9258(20)89632-x;
RA Schwoebel E., Prasad S., Timmons T.M., Cook R., Kimura H., Niu E.-M.,
RA Cheung P., Skinner S., Avery S.E., Wilkins B., Dunbar B.S.;
RT "Isolation and characterization of a full-length cDNA encoding the 55-kDa
RT rabbit zona pellucida protein.";
RL J. Biol. Chem. 266:7214-7219(1991).
RN [2]
RP DOMAINS.
RX PubMed=8518738; DOI=10.1002/pro.5560020417;
RA Bork P.;
RT "A trefoil domain in the major rabbit zona pellucida protein.";
RL Protein Sci. 2:669-670(1993).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Ovary;
RX PubMed=22842159; DOI=10.1016/j.jprot.2012.07.027;
RA Stetson I., Izquierdo-Rico M.J., Moros C., Chevret P., Lorenzo P.L.,
RA Ballesta J., Rebollar P.G., Gutierrez-Gallego R., Aviles M.;
RT "Rabbit zona pellucida composition: a molecular, proteomic and phylogenetic
RT approach.";
RL J. Proteomics 75:5920-5935(2012).
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:0000269|PubMed:22842159}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22842159};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in oocytes (at protein level).
CC {ECO:0000269|PubMed:22842159}.
CC -!- DOMAIN: The ZP domain is involved in the polymerization of the ZP
CC proteins to form the zona pellucida. {ECO:0000269|PubMed:8518738}.
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; M58160; AAA31501.1; -; mRNA.
DR PIR; A39783; A39783.
DR RefSeq; NP_001075764.1; NM_001082295.2.
DR AlphaFoldDB; Q00193; -.
DR SMR; Q00193; -.
DR STRING; 9986.ENSOCUP00000022164; -.
DR Ensembl; ENSOCUT00000032066; ENSOCUP00000022164; ENSOCUG00000002467.
DR GeneID; 100009131; -.
DR KEGG; ocu:100009131; -.
DR CTD; 57829; -.
DR eggNOG; ENOG502QU54; Eukaryota.
DR GeneTree; ENSGT00940000161324; -.
DR HOGENOM; CLU_034433_0_0_1; -.
DR InParanoid; Q00193; -.
DR OMA; RTWSHGS; -.
DR OrthoDB; 586615at2759; -.
DR TreeFam; TF332794; -.
DR Proteomes; UP000001811; Chromosome 16.
DR Bgee; ENSOCUG00000002467; Expressed in ovary and 3 other tissues.
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; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0035804; F:structural constituent of egg coat; IDA:UniProtKB.
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; 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 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..24
FT /evidence="ECO:0000269|PubMed:1707882"
FT CHAIN 25..466
FT /note="Zona pellucida sperm-binding protein 4"
FT /id="PRO_0000041731"
FT CHAIN 25..?
FT /note="Processed zona pellucida sperm-binding protein 4"
FT /id="PRO_0000304580"
FT PROPEP 467..540
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041732"
FT TOPO_DOM 25..515
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 537..540
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 145..187
FT /note="P-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DOMAIN 192..470
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 296
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 306
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 371..446
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
SQ SEQUENCE 540 AA; 59835 MW; 030EE13D057F6D6F CRC64;
MAPGSTMWLL GYIFLCFPVS FALIKQPKPE TPTDPGVLHC RPWNFKFTIN FQNQETGSSP
VLVTWDNQGR LHRLQNDTDC GTRVGEGPGP SVVLEANYSS CYVTESEPYY VMLVGVEEVD
AAGQNLVTKQ QLLKCPMHLP APDAGLCDSV PVQDRLPCAT APISQEDCEE LGCCHSSEEV
NACYYGNTVT SHCTQEGHFS IAVSRNVSSP PLHLDSVHLV FGNDSECQPV VATRAFVLFL
FPFTACGTTR QITGDRAIYE NELLATREVR TWSRGSITRD SIFRLRVSCS YSISSSALPV
DMHVLTLPPP LPETQPGPLT VVLQIAKDKD YHSYYTMDDY PVVKLLRDPI YVDVSILYRT
DPYLGLRLHQ CWATPRTNPL YQPQWPILVK GCPYTGDNYQ TQLIPVQEAF DLPFPSHHQR
FSISTFSFLD SSVAKEALKG PIYLHCSVSV CQPTGTQSCT VTCPIDSRRR NSDINFQNST
ANISSKGPMI LLQATEDPSE KLHKHSGVPV HPGALWVAGL SGIFIIGALL VSYVAIRTRR
