ID   ZP3_CALSQ               Reviewed;         424 AA.
AC   P53786;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 110.
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   Callithrix sp. (Marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=8081814; DOI=10.1017/s0967199400001350;
RA   Thillai-Koothan P., van Duin M., Aitken R.J.;
RT   "Cloning, sequencing and oocyte-specific expression of the marmoset sperm
RT   receptor protein, ZP3.";
RL   Zygote 1:93-101(1993).
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://www.proteinspotlight.org/back_issues/093";
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DR   EMBL; S71825; AAB31866.1; -; mRNA.
DR   AlphaFoldDB; P53786; -.
DR   SMR; P53786; -.
DR   GlyCosmos; P53786; 8 sites, No reported glycans.
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; IEA:TreeGrafter.
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   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   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; Secreted; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..350
FT                   /note="Zona pellucida sperm-binding protein 3"
FT                   /id="PRO_0000041703"
FT   CHAIN           23..?
FT                   /note="Processed zona pellucida sperm-binding protein 3"
FT                   /id="PRO_0000304566"
FT   PROPEP          351..424
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000041704"
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..307
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        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        156
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        163
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        46..140
FT                   /evidence="ECO:0000250"
FT   DISULFID        78..99
FT                   /evidence="ECO:0000250"
FT   DISULFID        217..282
FT                   /evidence="ECO:0000250"
FT   DISULFID        239..300
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   424 AA;  46809 MW;  1DACBD03026C2739 CRC64;
     MELSYRLFIC LLLWGSTELC YPQPLRLLQG GTSHPETALQ PVVVECQEAT LVVTVSKDLF
     GTRKLIRAVD LTLGPEGCEP LVSTDTEDVV RFEVGLHECG NSMQVTDDAL VYSTFLLHDP
     RPVGNLSIVR TNRAEIPIEC RYPRRGNVSS QAILPTWLPF RTTVFSEEKL TFSLRLMEEN
     WSTEKRTPTF HLGDVAHLQA EIHTGSHVPL RLFVDHCVAT PTPDQNASPY HTIVDFHGCL
     VDGLTDASSA FQAPRPRPDT LQFTVDVFHF ANDSRNMIYI TCHLKVTLAE QDPDELNKAC
     SFSKASNSWF PVEGPADICQ CCSKGDCGTP SHARRQPHVV SLGSGSPARD RRHVTEEADV
     TVGPLIFLDR TGDHEMEQWA LPADTSLLLL GTGLAVVALL TLTAVILVLT RRCRTASLPV
     SASE
//