ID   ZP3_RAT                 Reviewed;         424 AA.
AC   P97708; O55084;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 2.
DT   02-SEP-2026, entry version 143.
DE   RecName: Full=Zona pellucida sperm-binding protein 3;
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=Zp-3, Zpc;
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=Wistar; TISSUE=Ovary;
RA   MacDuff P.E., Kerr L.E., Aitken R.J.;
RT   "Molecular characterisation of zona pellucida protein 3 (ZP3) in the rat.";
RL   J. Reprod. Fertil. Abstr. Ser. 18:86-86(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 57-63, AND GLYCOSYLATION.
RC   STRAIN=Sprague-Dawley; TISSUE=Ovary;
RX   PubMed=9820205;
RX   DOI=10.1002/(sici)1098-2795(199812)51:4<454::aid-mrd13>3.0.co;2-g;
RA   Akatsuka K., Yoshida-Komiya H., Tulsiani D.R.P., Orgebin-Crist M.-C.,
RA   Hiroi M., Araki Y.;
RT   "Rat zona pellucida glycoproteins: molecular cloning and characterization
RT   of the three major components.";
RL   Mol. Reprod. Dev. 51:454-467(1998).
RN   [3]
RP   PROTEIN SEQUENCE OF C-TERMINUS, PYROGLUTAMATE FORMATION AT GLN-23,
RP   DISULFIDE BOND FORMATION AT 78-CYS--CYS-98; 216-CYS--CYS-283 AND
RP   240-CYS--CYS-301, GLYCOSYLATION AT ASN-146; ASN-273; ASN-304 AND ASN-330,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16342937; DOI=10.1021/bi051883f;
RA   Boja E.S., Hoodbhoy T., Garfield M., Fales H.M.;
RT   "Structural conservation of mouse and rat zona pellucida glycoproteins.
RT   Probing the native rat zona pellucida proteome by mass spectrometry.";
RL   Biochemistry 44:16445-16460(2005).
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; N-linked glycans are of high mannose/hybrid type,
CC       as well as bi-, tri- and tetra-antennary complex types.
CC   -!- PTM: O-glycosylated; removal of O-linked glycans may play an important
CC       role in the post-fertilization block to polyspermy.
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://www.proteinspotlight.org/back_issues/093";
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DR   EMBL; Y10823; CAA71787.1; -; mRNA.
DR   EMBL; D78482; BAA24456.1; -; mRNA.
DR   RefSeq; NP_446214.1; NM_053762.1.
DR   AlphaFoldDB; P97708; -.
DR   SMR; P97708; -.
DR   FunCoup; P97708; 34.
DR   STRING; 10116.ENSRNOP00000001952; -.
DR   GlyCosmos; P97708; 10 sites, No reported glycans.
DR   GlyGen; P97708; 10 sites.
DR   iPTMnet; P97708; -.
DR   PhosphoSitePlus; P97708; -.
DR   PaxDb; 10116-ENSRNOP00000001952; -.
DR   GeneID; 114639; -.
DR   KEGG; rno:114639; -.
DR   UCSC; RGD:620606; rat.
DR   AGR; RGD:620606; -.
DR   CTD; 7784; -.
DR   RGD; 620606; Zp3.
DR   eggNOG; ENOG502QSZF; Eukaryota.
DR   InParanoid; P97708; -.
DR   OrthoDB; 53041at9989; -.
DR   PhylomeDB; P97708; -.
DR   PRO; PR:P97708; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0035805; C:egg coat; ISS:UniProtKB.
DR   GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0032190; F:acrosin binding; ISO:RGD.
DR   GO; GO:0030246; F:carbohydrate binding; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
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   GO; GO:0010469; P:regulation of signaling receptor activity; ISO:RGD.
DR   FunFam; 2.60.40.3210:FF:000001; Zona pellucida sperm-binding protein 3; 1.
DR   FunFam; 2.60.40.4100:FF:000002; Zona pellucida sperm-binding protein 3; 1.
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; IPR055355; ZP-C.
DR   InterPro; IPR042235; ZP-C_dom.
DR   InterPro; IPR055356; ZP-N.
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   Pfam; PF23344; ZP-N; 1.
DR   PRINTS; PR00023; ZPELLUCIDA.
DR   SMART; SM00241; ZP; 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; Pyrrolidone carboxylic acid;
KW   Receptor; Reference proteome; Secreted; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..351
FT                   /note="Zona pellucida sperm-binding protein 3"
FT                   /id="PRO_0000041721"
FT   CHAIN           23..?
FT                   /note="Processed zona pellucida sperm-binding protein 3"
FT                   /id="PRO_0000304575"
FT   PROPEP          352..424
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000269|PubMed:16342937"
FT                   /id="PRO_0000041722"
FT   TOPO_DOM        23..387
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        388..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        409..424
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          45..308
FT                   /note="ZP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT   MOD_RES         23
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:16342937"
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        39
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16342937"
FT   CARBOHYD        155
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        273
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16342937"
FT   CARBOHYD        304
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16342937"
FT   CARBOHYD        327
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16342937"
FT   DISULFID        46..139
FT                   /evidence="ECO:0000250"
FT   DISULFID        78..98
FT                   /evidence="ECO:0000269|PubMed:16342937"
FT   DISULFID        216..283
FT                   /evidence="ECO:0000269|PubMed:16342937"
FT   DISULFID        240..301
FT                   /evidence="ECO:0000269|PubMed:16342937"
FT   CONFLICT        55
FT                   /note="V -> A (in Ref. 2; BAA24456)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        112
FT                   /note="N -> S (in Ref. 2; BAA24456)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        412
FT                   /note="K -> M (in Ref. 2; BAA24456)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   424 AA;  45901 MW;  2AB42CBB14DE8701 CRC64;
     MGPSCLLFLC LLLCGGPELC YPQTQWLLPG GTPTPAGSSS PVEVECKEAE LVVTVRRDLF
     GTGKLVQPGD LTLGSEGCQP LVAVDTDVVR LNAQLHECSS GVQVTEDALV YNTFLLHDPR
     PVNGLSILRT NRVEVPIECR YPRQGNVSSH PIQPTWVPFS ATVSSEEKLA FSLRLMEEDW
     NTEKSSPTFH LGEVAHLQAE VQTGSHLPLQ LFVDHCVATP SPLPGQNSSP HHFIVDSHGC
     LVDGLSESFS AFQVPRPRPE TLQFTVDVFH FANSSRNTVY ITCHLKVAPA NQIPDKLNKA
     CSFNKTSQSW LPVEGDADIC DCCSNGNCSN SSSSEFETHE PAQWSTLVSR NRRHVTDEAD
     VTVGPLIFLG KANDQAVEGW TSSAQTSVAL GLGLATVAFL TLAAIVLGVT RKCHTSSYLV
     SLPQ
//