ZP3_RAT
ID ZP3_RAT Reviewed; 424 AA.
AC P97708; O55084;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 2.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Zona pellucida sperm-binding protein 3;
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=Zp-3, Zpc;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Ovary;
RA MacDuff P.E., Kerr L.E., Aitken R.J.;
RT "Molecular characterisation of zona pellucida protein 3 (ZP3) in the rat.";
RL J. Reprod. Fertil. Abstr. Ser. 18:86-86(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 57-63, AND GLYCOSYLATION.
RC STRAIN=Sprague-Dawley; TISSUE=Ovary;
RX PubMed=9820205;
RX DOI=10.1002/(sici)1098-2795(199812)51:4<454::aid-mrd13>3.0.co;2-g;
RA Akatsuka K., Yoshida-Komiya H., Tulsiani D.R.P., Orgebin-Crist M.-C.,
RA Hiroi M., Araki Y.;
RT "Rat zona pellucida glycoproteins: molecular cloning and characterization
RT of the three major components.";
RL Mol. Reprod. Dev. 51:454-467(1998).
RN [3]
RP PROTEIN SEQUENCE OF C-TERMINUS, PYROGLUTAMATE FORMATION AT GLN-23,
RP DISULFIDE BOND FORMATION AT 78-CYS--CYS-98; 216-CYS--CYS-283 AND
RP 240-CYS--CYS-301, GLYCOSYLATION AT ASN-146; ASN-273; ASN-304 AND ASN-330,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16342937; DOI=10.1021/bi051883f;
RA Boja E.S., Hoodbhoy T., Garfield M., Fales H.M.;
RT "Structural conservation of mouse and rat zona pellucida glycoproteins.
RT Probing the native rat zona pellucida proteome by mass spectrometry.";
RL Biochemistry 44:16445-16460(2005).
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; N-linked glycans are of high mannose/hybrid type,
CC as well as bi-, tri- and tetra-antennary complex types.
CC -!- PTM: O-glycosylated; removal of O-linked glycans may play an important
CC role in the post-fertilization block to polyspermy.
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; Y10823; CAA71787.1; -; mRNA.
DR EMBL; D78482; BAA24456.1; -; mRNA.
DR RefSeq; NP_446214.1; NM_053762.1.
DR AlphaFoldDB; P97708; -.
DR SMR; P97708; -.
DR STRING; 10116.ENSRNOP00000001952; -.
DR GlyGen; P97708; 10 sites.
DR iPTMnet; P97708; -.
DR PaxDb; P97708; -.
DR GeneID; 114639; -.
DR KEGG; rno:114639; -.
DR UCSC; RGD:620606; rat.
DR CTD; 7784; -.
DR RGD; 620606; Zp3.
DR eggNOG; ENOG502QSZF; Eukaryota.
DR InParanoid; P97708; -.
DR OrthoDB; 495227at2759; -.
DR PhylomeDB; P97708; -.
DR PRO; PR:P97708; -.
DR Proteomes; UP000002494; 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; ISO:RGD.
DR GO; GO:0030246; F:carbohydrate binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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 GO; GO:0010469; P:regulation of signaling receptor activity; ISO:RGD.
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;
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:0000250"
FT CHAIN 23..351
FT /note="Zona pellucida sperm-binding protein 3"
FT /id="PRO_0000041721"
FT CHAIN 23..?
FT /note="Processed zona pellucida sperm-binding protein 3"
FT /id="PRO_0000304575"
FT PROPEP 352..424
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:16342937"
FT /id="PRO_0000041722"
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..308
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT MOD_RES 23
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:16342937"
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 39
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16342937"
FT CARBOHYD 155
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 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16342937"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16342937"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16342937"
FT DISULFID 46..139
FT /evidence="ECO:0000250"
FT DISULFID 78..98
FT /evidence="ECO:0000269|PubMed:16342937"
FT DISULFID 216..283
FT /evidence="ECO:0000269|PubMed:16342937"
FT DISULFID 240..301
FT /evidence="ECO:0000269|PubMed:16342937"
FT CONFLICT 55
FT /note="V -> A (in Ref. 2; BAA24456)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="N -> S (in Ref. 2; BAA24456)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="K -> M (in Ref. 2; BAA24456)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 45901 MW; 2AB42CBB14DE8701 CRC64;
MGPSCLLFLC LLLCGGPELC YPQTQWLLPG GTPTPAGSSS PVEVECKEAE LVVTVRRDLF
GTGKLVQPGD LTLGSEGCQP LVAVDTDVVR LNAQLHECSS GVQVTEDALV YNTFLLHDPR
PVNGLSILRT NRVEVPIECR YPRQGNVSSH PIQPTWVPFS ATVSSEEKLA FSLRLMEEDW
NTEKSSPTFH LGEVAHLQAE VQTGSHLPLQ LFVDHCVATP SPLPGQNSSP HHFIVDSHGC
LVDGLSESFS AFQVPRPRPE TLQFTVDVFH FANSSRNTVY ITCHLKVAPA NQIPDKLNKA
CSFNKTSQSW LPVEGDADIC DCCSNGNCSN SSSSEFETHE PAQWSTLVSR NRRHVTDEAD
VTVGPLIFLG KANDQAVEGW TSSAQTSVAL GLGLATVAFL TLAAIVLGVT RKCHTSSYLV
SLPQ
