ID   ZP3_FELCA               Reviewed;         424 AA.
AC   P48832;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   27-MAR-2024, entry version 142.
DE   RecName: Full=Zona pellucida sperm-binding protein 3;
DE   AltName: Full=Sperm receptor;
DE   AltName: Full=Zona pellucida glycoprotein 3;
DE            Short=Zp-3;
DE   AltName: Full=Zona pellucida protein C;
DE   Contains:
DE     RecName: Full=Processed zona pellucida sperm-binding protein 3;
DE   Flags: Precursor;
GN   Name=ZP3; Synonyms=ZPC;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RA   Okazaki Y., Sugimoto M.;
RL   Submitted (JAN-1995) 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       ZP3 is essential for sperm binding and zona matrix formation.
CC   -!- SUBUNIT: Polymers of ZP2 and ZP3 organized into long filaments cross-
CC       linked by ZP1 homodimers. Interacts with ZP1 and ZP2.
CC       {ECO:0000250|UniProtKB:P20239, ECO:0000250|UniProtKB:P21754}.
CC   -!- SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein
CC       3]: Zona pellucida {ECO:0000250|UniProtKB:P21754}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P48833};
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: N-glycosylated. {ECO:0000250}.
CC   -!- PTM: O-glycosylated; removal of O-linked glycans may play an important
CC       role in the post-fertilization block to polyspermy. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ZP domain family. ZPC subfamily.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Molecular chastity - Issue
CC       93 of April 2008;
CC       URL="https://web.expasy.org/spotlight/back_issues/093";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U05778; AAA74390.1; -; mRNA.
DR   EMBL; D45068; BAA08096.1; -; mRNA.
DR   PIR; S70399; S70399.
DR   RefSeq; NP_001009330.1; NM_001009330.2.
DR   AlphaFoldDB; P48832; -.
DR   SMR; P48832; -.
DR   STRING; 9685.ENSFCAP00000012496; -.
DR   GlyCosmos; P48832; 6 sites, No reported glycans.
DR   PaxDb; 9685-ENSFCAP00000012496; -.
DR   GeneID; 493925; -.
DR   KEGG; fca:493925; -.
DR   eggNOG; ENOG502QSZF; Eukaryota.
DR   HOGENOM; CLU_047091_1_1_1; -.
DR   InParanoid; P48832; -.
DR   OrthoDB; 5355932at2759; -.
DR   Proteomes; UP000011712; Unplaced.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0035805; C:egg coat; ISS:UniProtKB.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0032190; F:acrosin binding; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; ISS:UniProtKB.
DR   GO; GO:0048018; F:receptor ligand activity; ISS:UniProtKB.
DR   GO; GO:0035804; F:structural constituent of egg coat; ISS:UniProtKB.
DR   GO; GO:0007339; P:binding of sperm to zona pellucida; ISS:UniProtKB.
DR   GO; GO:0001825; P:blastocyst formation; ISS:UniProtKB.
DR   GO; GO:0035803; P:egg coat formation; ISS:UniProtKB.
DR   GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; ISS:UniProtKB.
DR   GO; GO:2000360; P:negative regulation of binding of sperm to zona pellucida; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0048599; P:oocyte development; ISS:UniProtKB.
DR   GO; GO:2000368; P:positive regulation of acrosomal vesicle exocytosis; ISS:UniProtKB.
DR   GO; GO:2000344; P:positive regulation of acrosome reaction; ISS:UniProtKB.
DR   GO; GO:2000388; P:positive regulation of antral ovarian follicle growth; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0002922; P:positive regulation of humoral immune response; ISS:UniProtKB.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR   GO; GO:0032753; P:positive regulation of interleukin-4 production; ISS:UniProtKB.
DR   GO; GO:0002687; P:positive regulation of leukocyte migration; ISS:UniProtKB.
DR   GO; GO:2000386; P:positive regulation of ovarian follicle development; ISS:UniProtKB.
DR   GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB.
DR   GO; GO:0032729; P:positive regulation of type II interferon production; ISS:UniProtKB.
DR   GO; GO:0001809; P:positive regulation of type IV hypersensitivity; ISS:UniProtKB.
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; IPR042235; ZP-C.
DR   InterPro; IPR048290; ZP_chr.
DR   InterPro; IPR001507; ZP_dom.
DR   InterPro; IPR017977; ZP_dom_CS.
DR   PANTHER; PTHR11576; ZONA PELLUCIDA SPERM-BINDING PROTEIN 3; 1.
DR   PANTHER; PTHR11576:SF2; ZONA PELLUCIDA SPERM-BINDING PROTEIN 3; 1.
DR   Pfam; PF00100; Zona_pellucida; 1.
DR   PRINTS; PR00023; ZPELLUCIDA.
DR   SMART; SM00241; ZP; 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..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..348
FT                   /note="Zona pellucida sperm-binding protein 3"
FT                   /id="PRO_0000041707"
FT   CHAIN           23..?
FT                   /note="Processed zona pellucida sperm-binding protein 3"
FT                   /id="PRO_0000304568"
FT   PROPEP          349..424
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000041708"
FT   TOPO_DOM        23..383
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        384..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        405..424
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          43..305
FT                   /note="ZP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        123
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        154
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        160
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        161
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..138
FT                   /evidence="ECO:0000250"
FT   DISULFID        76..97
FT                   /evidence="ECO:0000250"
FT   DISULFID        215..280
FT                   /evidence="ECO:0000250"
FT   DISULFID        237..298
FT                   /evidence="ECO:0000250"
FT   CONFLICT        72
FT                   /note="G -> W (in Ref. 2; BAA08096)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        264
FT                   /note="D -> Y (in Ref. 2; BAA08096)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   424 AA;  46854 MW;  CFC62F35F9AAFC0D CRC64;
     MGLSYGLFIC FLLWAGTGLC YPPTTTEDKT HPSLPSSPSV VVECRHAWLV VNVSKNLFGT
     GRLVRPADLT LGPENCEPLI SGDSDDTVRF EVELHKCGNS VQVTEDALVY STFLLHNPRP
     MGNLSILRTN RAEVPIECRY PRHSNVSSEA ILPTWVPFRT TMLSEEKLAF SLRLMEEDWG
     SEKQSPTFQL GDLAHLQAEV HTGRHIPLRL FVDYCVATLT PDQNASPHHT IVDFHGCLVD
     GLSDASSAFK APRPRPETLQ FTVDTFHFAN DPRNMIYITC HLKVTPASRV PDQLNKACSF
     IKSSNRWFPV EGPADICNCC NKGSCGLQGR SWRLSHLDRP WHKMASRNRR HVTEEADITV
     GPLIFLGKAA DRGVEGSTSP HTSVMVGIGL ATVLSLTLAT IVLGLARRHH TASRPMICPV
     SASQ
//