ZP3_MESAU
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 25-MAY-2022, 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 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";
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; 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.XP_005080436.1; -.
DR GeneID; 101824371; -.
DR CTD; 7784; -.
DR eggNOG; ENOG502QSZF; Eukaryota.
DR OrthoDB; 495227at2759; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 transcription, DNA-templated; 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: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:0032729; P:positive regulation of interferon-gamma production; 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:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0001809; P:positive regulation of type IV hypersensitivity; ISS:UniProtKB.
DR Gene3D; 2.60.40.4100; -; 1.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR040196; ZP3.
DR InterPro; IPR001507; ZP_dom.
DR InterPro; IPR017977; ZP_dom_CS.
DR PANTHER; PTHR11576:SF2; PTHR11576:SF2; 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
