ZP3_RABIT
ID ZP3_RABIT Reviewed; 415 AA.
AC P48833;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 106.
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; Fragment;
GN Name=ZP3; Synonyms=ZPC;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
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 IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Ovary;
RX PubMed=22842159; DOI=10.1016/j.jprot.2012.07.027;
RA Stetson I., Izquierdo-Rico M.J., Moros C., Chevret P., Lorenzo P.L.,
RA Ballesta J., Rebollar P.G., Gutierrez-Gallego R., Aviles M.;
RT "Rabbit zona pellucida composition: a molecular, proteomic and phylogenetic
RT approach.";
RL J. Proteomics 75:5920-5935(2012).
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:0000269|PubMed:22842159}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22842159};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in oocytes (at protein level).
CC {ECO:0000269|PubMed:22842159}.
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; U05782; AAA74392.1; -; mRNA.
DR PIR; S70401; S70401.
DR AlphaFoldDB; P48833; -.
DR SMR; P48833; -.
DR STRING; 9986.ENSOCUP00000013539; -.
DR PRIDE; P48833; -.
DR eggNOG; ENOG502QSZF; Eukaryota.
DR InParanoid; P48833; -.
DR Proteomes; UP000001811; 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; IDA: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 1: Evidence at protein 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..18
FT /evidence="ECO:0000250"
FT CHAIN 19..341
FT /note="Zona pellucida sperm-binding protein 3"
FT /id="PRO_0000041719"
FT CHAIN 19..?
FT /note="Processed zona pellucida sperm-binding protein 3"
FT /id="PRO_0000304574"
FT PROPEP 342..415
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041720"
FT TOPO_DOM 19..378
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..415
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 41..301
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT MOD_RES 19
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P21754"
FT CARBOHYD 28
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 150
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 156
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 157
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 42..134
FT /evidence="ECO:0000250"
FT DISULFID 74..93
FT /evidence="ECO:0000250"
FT DISULFID 211..276
FT /evidence="ECO:0000250"
FT DISULFID 233..294
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 415 AA; 44987 MW; 77396CF1BAA3F5CB CRC64;
YGLFVCLLLW GGSELCCPQP LWFWQGGTRQ PAPSVTPVVV ECLEARLVVT VSRDLFGTGK
LIQEADLSLG PEGCEPQAST DAVVRFEVGL HECGNSVQVT DDSLVYSSFL LHDPRPAGNL
SILRTNRAEV PIECRYPRQG NVSSRAILPT WVPFWTTVLS EERLVFSLRL MEENWSREKM
SPTFHLGDTA HLQAEVRTGS HPPLLLFVDR CVATPTRDQS GSPYHTIVDL HGCLVDGLSD
GASKFKAPRP KPDVLQFMVA VFHFANDSRH TVYITCHLRV IPAQQAPDRL NKACSFNQSS
SSWAPVEGSA DICECCGNGD CDLIAGSPMN QNHAARSSLR SRRHVTEEAD VTVGPLIFLG
KAGDPAGTEG LASAAQATLV LGLRMATIVF LAVAAVVLGL TRGRHAASHP RSASQ
