ZP1_MOUSE
ID ZP1_MOUSE Reviewed; 623 AA.
AC Q62005; Q62016;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Zona pellucida sperm-binding protein 1;
DE AltName: Full=Zona pellucida glycoprotein 1;
DE Short=Zp-1;
DE Contains:
DE RecName: Full=Processed zona pellucida sperm-binding protein 1;
DE Flags: Precursor;
GN Name=Zp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-31; 106-114; 409-418 AND
RP 423-433, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=NIH Swiss; TISSUE=Ovary;
RX PubMed=7635043; DOI=10.1242/dev.121.7.1947;
RA Epifano O., Liang L.-F., Familari M., Moos M.C. Jr., Dean J.;
RT "Coordinate expression of the three zona pellucida genes during mouse
RT oogenesis.";
RL Development 121:1947-1956(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=7592984; DOI=10.1074/jbc.270.45.27254;
RA Epifano O., Liang L.-F., Dean J.;
RT "Mouse Zp1 encodes a zona pellucida protein homologous to egg envelope
RT proteins in mammals and fish.";
RL J. Biol. Chem. 270:27254-27258(1995).
RN [3]
RP PROTEIN SEQUENCE OF C-TERMINUS, PYROGLUTAMATE FORMATION AT GLN-21,
RP DISULFIDE BOND FORMATION AT 449-CYS--CYS-470, GLYCOSYLATION AT ASN-49;
RP ASN-68; ASN-240 AND ASN-371, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12799386; DOI=10.1074/jbc.m304026200;
RA Boja E.S., Hoodbhoy T., Fales H.M., Dean J.;
RT "Structural characterization of native mouse zona pellucida proteins using
RT mass spectrometry.";
RL J. Biol. Chem. 278:34189-34202(2003).
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 ZP1 ensures the structural integrity of the zona pellucida.
CC -!- SUBUNIT: Polymers of ZP2 and ZP3 organized into long filaments cross-
CC linked by ZP1 homodimers. Interacts with ZP3.
CC {ECO:0000250|UniProtKB:P20239, ECO:0000250|UniProtKB:P60852}.
CC -!- SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein
CC 1]: Zona pellucida {ECO:0000250|UniProtKB:P60852}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P48829};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in oocytes. {ECO:0000269|PubMed:7635043}.
CC -!- DEVELOPMENTAL STAGE: Not detected in resting oocytes. As oocytes begin
CC to grow, levels increase to reach a maximum in midsized oocytes. Levels
CC decrease in later stages of oocyte growth.
CC {ECO:0000269|PubMed:7635043}.
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: O-glycosylated. {ECO:0000269|PubMed:12799386}.
CC -!- SIMILARITY: Belongs to the ZP domain family. ZPB subfamily.
CC {ECO:0000305}.
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DR EMBL; U24230; AAB60507.1; -; Genomic_DNA.
DR EMBL; U24227; AAB60507.1; JOINED; Genomic_DNA.
DR EMBL; U24228; AAB60507.1; JOINED; Genomic_DNA.
DR EMBL; U24229; AAB60507.1; JOINED; Genomic_DNA.
DR EMBL; U20448; AAC48480.1; -; mRNA.
DR CCDS; CCDS37918.1; -.
DR PIR; I46382; I46382.
DR RefSeq; NP_033606.2; NM_009580.2.
DR AlphaFoldDB; Q62005; -.
DR SMR; Q62005; -.
DR STRING; 10090.ENSMUSP00000025641; -.
DR GlyConnect; 635; 24 N-Linked glycans, 10 O-Linked glycans.
DR GlyGen; Q62005; 7 sites, 48 N-linked glycans (1 site), 15 O-linked glycans (1 site).
DR iPTMnet; Q62005; -.
DR PhosphoSitePlus; Q62005; -.
DR PaxDb; Q62005; -.
DR PRIDE; Q62005; -.
DR ProteomicsDB; 275047; -.
DR Antibodypedia; 43518; 171 antibodies from 23 providers.
DR DNASU; 22786; -.
DR Ensembl; ENSMUST00000025641; ENSMUSP00000025641; ENSMUSG00000024734.
DR GeneID; 22786; -.
DR KEGG; mmu:22786; -.
DR UCSC; uc008grh.2; mouse.
DR CTD; 22917; -.
DR MGI; MGI:103073; Zp1.
DR VEuPathDB; HostDB:ENSMUSG00000024734; -.
DR eggNOG; ENOG502RYNN; Eukaryota.
DR GeneTree; ENSGT00940000161188; -.
DR HOGENOM; CLU_034433_0_0_1; -.
DR InParanoid; Q62005; -.
DR OMA; RHSYDCG; -.
DR OrthoDB; 586615at2759; -.
DR PhylomeDB; Q62005; -.
DR TreeFam; TF332794; -.
DR Reactome; R-MMU-2534343; Interaction With Cumulus Cells And The Zona Pellucida.
DR BioGRID-ORCS; 22786; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Zp1; mouse.
DR PRO; PR:Q62005; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q62005; protein.
DR Bgee; ENSMUSG00000024734; Expressed in primary oocyte and 16 other tissues.
DR ExpressionAtlas; Q62005; baseline and differential.
DR Genevisible; Q62005; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB.
DR GO; GO:0035805; C:egg coat; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032190; F:acrosin binding; IBA:GO_Central.
DR GO; GO:0035804; F:structural constituent of egg coat; ISS:UniProtKB.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IBA:GO_Central.
DR GO; GO:0060468; P:prevention of polyspermy; IBA:GO_Central.
DR CDD; cd00111; Trefoil; 1.
DR Gene3D; 2.60.40.4100; -; 1.
DR InterPro; IPR017957; P_trefoil_CS.
DR InterPro; IPR000519; P_trefoil_dom.
DR InterPro; IPR044913; P_trefoil_dom_sf.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR001507; ZP_dom.
DR InterPro; IPR017977; ZP_dom_CS.
DR Pfam; PF00088; Trefoil; 1.
DR Pfam; PF00100; Zona_pellucida; 1.
DR PRINTS; PR00023; ZPELLUCIDA.
DR SMART; SM00018; PD; 1.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF57492; SSF57492; 1.
DR PROSITE; PS00025; P_TREFOIL_1; 1.
DR PROSITE; PS51448; P_TREFOIL_2; 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 Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:12799386,
FT ECO:0000269|PubMed:7635043"
FT CHAIN 21..546
FT /note="Zona pellucida sperm-binding protein 1"
FT /id="PRO_0000041679"
FT CHAIN 21..?
FT /note="Processed zona pellucida sperm-binding protein 1"
FT /id="PRO_0000304554"
FT PROPEP 547..623
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:12799386"
FT /id="PRO_0000041680"
FT TOPO_DOM 21..590
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 591..611
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 612..623
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 226..266
FT /note="P-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DOMAIN 271..542
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REGION 182..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:12799386"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12799386"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12799386"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12799386"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12799386"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 228..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 237..252
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 247..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 449..470
FT /evidence="ECO:0000305|PubMed:12799386"
FT CONFLICT 246
FT /note="T -> A (in Ref. 1; AAC48480)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="V -> L (in Ref. 1; AAC48480)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="R -> K (in Ref. 1; AAC48480)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 623 AA; 68723 MW; 9D95B8613B3B95C8 CRC64;
MAWGCFVVLL LLAAAPLRLG QRLHLEPGFE YSYDCGVRGM QLLVFPRPNQ TVQFKVLDEF
GNRFEVNNCS ICYHWVTSEA QEHTVFSADY KGCHVLEKDG RFHLRVFIQA VLPNGRVDIA
QDVTLICPKP DHTVTPDPYL APPTTPEPFT PHAFALHPIP DHTLAGSGHT GLTTLYPEQS
FIHPTPAPPS LGPGPAGSTV PHSQWGTLEP WELTELDSVG THLPQERCQV ASGHIPCMVN
GSSKETCQQA GCCYDSTKEE PCYYGNTVTL QCFKSGYFTL VMSQETALTH GVLLDNVHLA
YAPNGCPPTQ KTSAFVVFHV PLTLCGTAIQ VVGEQLIYEN QLVSDIDVQK GPQGSITRDS
AFRLHVRCIF NASDFLPIQA SIFSPQPPAP VTQSGPLRLE LRIATDKTFS SYYQGSDYPL
VRLLREPVYV EVRLLQRTDP SLVLVLHQCW ATPTTSPFEQ PQWPILSDGC PFKGDNYRTQ
VVAADREALP FWSHYQRFTI TTFMLLDSSS QNALRGQVYF FCSASACHPL GSDTCSTTCD
SGIARRRRSS GHHNITLRAL DIVSSPGAVG FEDAAKLEPS GSSRNSSSRM LLLLLAITLA
LAAGIFVGLI WAWAQKLWEG IRY
