ID   ZP3_PIG                 Reviewed;         421 AA.
AC   P42098;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   24-JAN-2024, entry version 135.
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 glycoprotein 3-beta;
DE            Short=Zp-3-beta;
DE            Short=Zp3-beta;
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=ZP3B, ZPC;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
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.
RN   [3]
RP   PROTEIN SEQUENCE OF N-TERMINUS, PYROGLUTAMATE FORMATION AT GLN-23, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=8562067; DOI=10.1002/mrd.1080420211;
RA   Gupta S.K., Yurewicz E.C., Afzalpurkar A., Rao K.V., Gage D.A., Wu H.,
RA   Sacco A.G.;
RT   "Localization of epitopes for monoclonal antibodies at the N-terminus of
RT   the porcine zona pellucida glycoprotein pZPC.";
RL   Mol. Reprod. Dev. 42:220-225(1995).
RN   [4]
RP   PROTEOLYTIC PROCESSING.
RX   PubMed=12878193; DOI=10.1016/s0006-291x(03)01297-x;
RA   Yonezawa N., Nakano M.;
RT   "Identification of the carboxyl termini of porcine zona pellucida
RT   glycoproteins ZPB and ZPC.";
RL   Biochem. Biophys. Res. Commun. 307:877-882(2003).
RN   [5]
RP   GLYCOSYLATION.
RX   PubMed=1418987; DOI=10.1002/mrd.1080330210;
RA   Yurewicz E.C., Pack B.A., Sacco A.G.;
RT   "Porcine oocyte zona pellucida M(r) 55,000 glycoproteins: identification of
RT   O-glycosylated domains.";
RL   Mol. Reprod. Dev. 33:182-188(1992).
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 zona matrix formation. May not have a sperm-
CC       binding activity by itself but may increase sperm-binding activity of
CC       ZPB.
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       {ECO:0000269|PubMed:12878193}.
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   -!- PTM: All cysteine residues are involved in disulfide bonds.
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; L22169; AAA31145.1; -; mRNA.
DR   EMBL; D45065; BAA08093.1; -; mRNA.
DR   PIR; S70433; S70433.
DR   RefSeq; NP_999058.1; NM_213893.1.
DR   AlphaFoldDB; P42098; -.
DR   SMR; P42098; -.
DR   STRING; 9823.ENSSSCP00000008213; -.
DR   GlyConnect; 632; 5 N-Linked glycans (3 sites).
DR   GlyConnect; 636; 6 N-Linked glycans.
DR   GlyCosmos; P42098; 7 sites, 10 glycans.
DR   iPTMnet; P42098; -.
DR   PaxDb; 9823-ENSSSCP00000008213; -.
DR   GeneID; 396927; -.
DR   KEGG; ssc:396927; -.
DR   CTD; 7784; -.
DR   eggNOG; ENOG502QSZF; Eukaryota.
DR   InParanoid; P42098; -.
DR   OrthoDB; 5355932at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; 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; IDA: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   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:0000269|PubMed:8562067"
FT   CHAIN           23..332
FT                   /note="Zona pellucida sperm-binding protein 3"
FT                   /id="PRO_0000041717"
FT   CHAIN           23..?
FT                   /note="Processed zona pellucida sperm-binding protein 3"
FT                   /id="PRO_0000304573"
FT   PROPEP          333..421
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000269|PubMed:8562067"
FT                   /id="PRO_0000041718"
FT   TOPO_DOM        23..381
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        382..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        403..421
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          44..306
FT                   /note="ZP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT   REGION          331..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         23
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:8562067"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:1418987"
FT                   /id="CAR_000151"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:1418987"
FT                   /id="CAR_000152"
FT   CARBOHYD        155
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:1418987"
FT   CARBOHYD        161
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:1418987"
FT   CARBOHYD        162
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:1418987"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:1418987"
FT                   /id="CAR_000153"
FT   DISULFID        45..139
FT                   /evidence="ECO:0000250"
FT   DISULFID        77..98
FT                   /evidence="ECO:0000250"
FT   DISULFID        216..281
FT                   /evidence="ECO:0000250"
FT   DISULFID        238..299
FT                   /evidence="ECO:0000250"
FT   CONFLICT        101
FT                   /note="Missing (in Ref. 2; BAA08093)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        107
FT                   /note="D -> V (in Ref. 2; BAA08093)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163..164
FT                   /note="VF -> GV (in Ref. 2; BAA08093)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        404
FT                   /note="P -> A (in Ref. 2; BAA08093)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   421 AA;  46239 MW;  DC97D760E985213A CRC64;
     MAPSWRFFVC FLLWGGTELC SPQPVWQDEG QRLRPSKPPT VMVECQEAQL VVIVSKDLFG
     TGKLIRPADL SLGPAKCEPL VSQDTDAVVR FEVGLHECGS SLQVTDDALV YSTFLRHDPR
     PAGNLSILRT NRAEVPIECH YPRQGNVSSW AILPTWVPFR TTVFSEEKLV FSLRLMEENW
     SAEKMTPTFQ LGDRAHLQAQ VHTGSHVPLR LFVDHCVATL TPDWNTSPSH TIVDFHGCLV
     DGLTEASSAF KAPRPGPETL QFTVDVFHFA NDSRNTIYIT CHLKVTPADR VPDQLNKACS
     FSKSSNRWSP VEGPAVICRC CHKGQCGTPS LSRKLSMPKR QSAPRSRRHV TDEADVTVGP
     LIFLGKTSDH GVEGSTSSPT SVMVGLGLAT VVTLTLATIV LGVPRRRRAA AHLVCPVSAS
     Q
//