ID   ZP3_MESAU               Reviewed;         422 AA.
AC   P23491;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   24-JAN-2024, entry version 114.
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   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=2257975; DOI=10.1016/0012-1606(90)90363-n;
RA   Kinloch R.A., Ruiz-Seller B., Wassarman P.M.;
RT   "Genomic organization and polypeptide primary structure of zona pellucida
RT   glycoprotein hZP3, the hamster sperm receptor.";
RL   Dev. Biol. 142:414-421(1990).
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   -!- DEVELOPMENTAL STAGE: Expressed in growing 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";
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DR   EMBL; M63629; AAA37079.1; -; mRNA.
DR   PIR; A60503; A60503.
DR   RefSeq; NP_001268531.1; NM_001281602.1.
DR   AlphaFoldDB; P23491; -.
DR   SMR; P23491; -.
DR   STRING; 10036.ENSMAUP00000023621; -.
DR   GlyCosmos; P23491; 8 sites, No reported glycans.
DR   GeneID; 101824371; -.
DR   KEGG; maua:101824371; -.
DR   CTD; 7784; -.
DR   eggNOG; ENOG502QSZF; Eukaryota.
DR   OrthoDB; 5355932at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0035805; C:egg coat; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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;
KW   Pyrrolidone carboxylic acid; Receptor; Reference proteome; Secreted;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..349
FT                   /note="Zona pellucida sperm-binding protein 3"
FT                   /id="PRO_0000041713"
FT   CHAIN           23..?
FT                   /note="Processed zona pellucida sperm-binding protein 3"
FT                   /id="PRO_0000304571"
FT   PROPEP          350..422
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000041714"
FT   TOPO_DOM        23..386
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        387..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        408..422
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          45..306
FT                   /note="ZP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT   MOD_RES         23
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P21754"
FT   CARBOHYD        32
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        34
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        155
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        161
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        162
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        46..139
FT                   /evidence="ECO:0000250"
FT   DISULFID        78..98
FT                   /evidence="ECO:0000250"
FT   DISULFID        216..281
FT                   /evidence="ECO:0000250"
FT   DISULFID        238..299
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   422 AA;  45827 MW;  D0F95BE7FF8E7E01 CRC64;
     MGLSYQLLLC LLLCGGAKQC CSQPLWLLPG GTPTPGKLTS SVEVECLEAE LVVTVSRDLF
     GTGKLIQPED LTLGSENCRP LVSVATDVVR FKAQLHECSN RVQVTEDALV YSTVLLHQPR
     PVPGLSILRT NRADVPIECR YPRQGNVSSH AIRPTWVPFS TTVSSEEKLV FSLRLMEENW
     NTEKLSPTSH LGEVAYLQAE VQTGSHLPLL LFVDRCVPTP SPDQTASPYH VIVDFHGCLV
     DGLSESFSAF QVPRPRPETL QFTVDVFHFA NSSRNTIYIT CHLKVTPANQ TPDELNKACS
     FNRSSKSWSP VEGDAEVCGC CSSGDCGSSS RSRYQAHGVS QWPKSASRRR RHVRDEADVT
     VGPLIFLGKA SDQAVEGWAS SAQTSLALGL GLAAVAFLTL AAIVLGVTRS CHTPSHVVSL
     SQ
//