ZP3_FELCA
ID ZP3_FELCA Reviewed; 424 AA.
AC P48832;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
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 Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
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.
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://web.expasy.org/spotlight/back_issues/093";
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DR EMBL; U05778; AAA74390.1; -; mRNA.
DR EMBL; D45068; BAA08096.1; -; mRNA.
DR PIR; S70399; S70399.
DR RefSeq; NP_001009330.1; NM_001009330.2.
DR AlphaFoldDB; P48832; -.
DR SMR; P48832; -.
DR STRING; 9685.ENSFCAP00000012496; -.
DR GeneID; 493925; -.
DR KEGG; fca:493925; -.
DR CTD; 7784; -.
DR eggNOG; ENOG502QSZF; Eukaryota.
DR HOGENOM; CLU_047091_1_1_1; -.
DR InParanoid; P48832; -.
DR OMA; ECHYPRH; -.
DR OrthoDB; 495227at2759; -.
DR Proteomes; UP000011712; 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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; Receptor;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..348
FT /note="Zona pellucida sperm-binding protein 3"
FT /id="PRO_0000041707"
FT CHAIN 23..?
FT /note="Processed zona pellucida sperm-binding protein 3"
FT /id="PRO_0000304568"
FT PROPEP 349..424
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041708"
FT TOPO_DOM 23..383
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 43..305
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 154
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 160
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 161
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT DISULFID 44..138
FT /evidence="ECO:0000250"
FT DISULFID 76..97
FT /evidence="ECO:0000250"
FT DISULFID 215..280
FT /evidence="ECO:0000250"
FT DISULFID 237..298
FT /evidence="ECO:0000250"
FT CONFLICT 72
FT /note="G -> W (in Ref. 2; BAA08096)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="D -> Y (in Ref. 2; BAA08096)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 46854 MW; CFC62F35F9AAFC0D CRC64;
MGLSYGLFIC FLLWAGTGLC YPPTTTEDKT HPSLPSSPSV VVECRHAWLV VNVSKNLFGT
GRLVRPADLT LGPENCEPLI SGDSDDTVRF EVELHKCGNS VQVTEDALVY STFLLHNPRP
MGNLSILRTN RAEVPIECRY PRHSNVSSEA ILPTWVPFRT TMLSEEKLAF SLRLMEEDWG
SEKQSPTFQL GDLAHLQAEV HTGRHIPLRL FVDYCVATLT PDQNASPHHT IVDFHGCLVD
GLSDASSAFK APRPRPETLQ FTVDTFHFAN DPRNMIYITC HLKVTPASRV PDQLNKACSF
IKSSNRWFPV EGPADICNCC NKGSCGLQGR SWRLSHLDRP WHKMASRNRR HVTEEADITV
GPLIFLGKAA DRGVEGSTSP HTSVMVGIGL ATVLSLTLAT IVLGLARRHH TASRPMICPV
SASQ
