ZP2_MOUSE
ID ZP2_MOUSE Reviewed; 713 AA.
AC P20239;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Zona pellucida sperm-binding protein 2;
DE AltName: Full=Zona pellucida glycoprotein 2;
DE Short=Zp-2;
DE AltName: Full=Zona pellucida protein A;
DE Contains:
DE RecName: Full=Processed zona pellucida sperm-binding protein 2;
DE Flags: Precursor;
GN Name=Zp2; Synonyms=Zp-2, Zpa;
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 35-50 AND 428-437, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Ovary;
RX PubMed=1690843; DOI=10.1128/mcb.10.4.1507-1515.1990;
RA Liang L.-F., Chamow S.M., Dean J.;
RT "Oocyte-specific expression of mouse Zp-2: developmental regulation of the
RT zona pellucida genes.";
RL Mol. Cell. Biol. 10:1507-1515(1990).
RN [2]
RP PROTEIN SEQUENCE OF N-TERMINUS AND C-TERMINUS, DISULFIDE BOND FORMATION AT
RP 84-CYS--CYS-102; 365-CYS--CYS-458; 396-CYS--CYS-417; 608-CYS--CYS-613;
RP 623-CYS--CYS-627, GLYCOSYLATION AT ASN-83; ASN-172; ASN-184; ASN-217;
RP ASN-264 AND ASN-393, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
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).
RN [3]
RP SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND STRUCTURE BY
RP ELECTRON MICROSCOPY.
RX PubMed=3845123; DOI=10.1016/0022-2836(85)90089-0;
RA Greve J.M., Wassarman P.M.;
RT "Mouse egg extracellular coat is a matrix of interconnected filaments
RT possessing a structural repeat.";
RL J. Mol. Biol. 181:253-264(1985).
RN [4]
RP SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=17559063; DOI=10.1002/jcp.21174;
RA Litscher E.S., Janssen W.G., Darie C.C., Wassarman P.M.;
RT "Purified mouse egg zona pellucida glycoproteins polymerize into homomeric
RT fibrils under non-denaturing conditions.";
RL J. Cell. Physiol. 214:153-157(2008).
RN [5]
RP FUNCTION IN POLYSPERMY INHIBITION, PROTEOLYTIC PROCESSING, CLEAVAGE BY
RP ASTL, AND SUBCELLULAR LOCATION.
RX PubMed=22472438; DOI=10.1083/jcb.201112094;
RA Burkart A.D., Xiong B., Baibakov B., Jimenez-Movilla M., Dean J.;
RT "Ovastacin, a cortical granule protease, cleaves ZP2 in the zona pellucida
RT to prevent polyspermy.";
RL J. Cell Biol. 197:37-44(2012).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 463-664, DISULFIDE BOND,
RP MUTAGENESIS OF 634-LYS-ARG-635, AND DOMAIN.
RX PubMed=26811476; DOI=10.1073/pnas.1519803113;
RA Bokhove M., Nishimura K., Brunati M., Han L., de Sanctis D., Rampoldi L.,
RA Jovine L.;
RT "A structured interdomain linker directs self-polymerization of human
RT uromodulin.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:1552-1557(2016).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (0.95 ANGSTROMS) OF 35-138, AND DISULFIDE BONDS.
RX PubMed=28622512; DOI=10.1016/j.cell.2017.05.033;
RA Raj I., Sadat Al Hosseini H., Dioguardi E., Nishimura K., Han L., Villa A.,
RA de Sanctis D., Jovine L.;
RT "Structural basis of egg coat-sperm recognition at fertilization.";
RL Cell 169:1315-1326(2017).
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 ZP2 may act as a secondary sperm receptor.
CC {ECO:0000269|PubMed:22472438}.
CC -!- SUBUNIT: Can form homopolymers that assemble into long fibers (in
CC vitro) (PubMed:17559063). Polymers of ZP2 and ZP3 organized into long
CC filaments cross-linked by ZP1 homodimers (PubMed:3845123). Interacts
CC with ZP3 (By similarity). {ECO:0000250|UniProtKB:Q05996,
CC ECO:0000269|PubMed:17559063, ECO:0000269|PubMed:3845123}.
CC -!- SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein
CC 2]: Zona pellucida {ECO:0000269|PubMed:12799386,
CC ECO:0000269|PubMed:17559063, ECO:0000269|PubMed:22472438,
CC ECO:0000269|PubMed:3845123}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22472438};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in oocytes (at protein level).
CC {ECO:0000269|PubMed:12799386, ECO:0000269|PubMed:1690843,
CC ECO:0000269|PubMed:17559063, ECO:0000269|PubMed:3845123}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the 2-week growth phase of
CC oogenesis, prior to ovulation. {ECO:0000269|PubMed:1690843}.
CC -!- DOMAIN: The ZP domain is involved in the polymerization of the ZP
CC proteins to form the zona pellucida. {ECO:0000269|PubMed:26811476}.
CC -!- PTM: Proteolytically cleaved before the transmembrane segment to yield
CC the secreted ectodomain incorporated in the zona pellucida.
CC {ECO:0000269|PubMed:22472438, ECO:0000269|PubMed:26811476}.
CC -!- PTM: Proteolytically cleaved in the N-terminal part by the
CC metalloendopeptidase ASTL exocytosed from cortical granules after
CC fertilization, yielding a N-terminal peptide of about 30 kDa which
CC remains covalently attached to the C-terminal peptide via disulfide
CC bond(s). This cleavage may play an important role in the post-
CC fertilization block to polyspermy. Additional proteolytically cleavage
CC of the N-terminal peptide of 30 kDa occurs in one-cell and two-cell
CC embryos. {ECO:0000269|PubMed:22472438}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12799386}.
CC -!- PTM: O-glycosylated; contains sulfate-substituted glycans.
CC {ECO:0000269|PubMed:12799386}.
CC -!- SIMILARITY: Belongs to the ZP domain family. ZPA subfamily.
CC {ECO:0000305}.
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DR EMBL; M34148; AAA40586.1; -; mRNA.
DR CCDS; CCDS21792.1; -.
DR PIR; A34782; A34782.
DR RefSeq; NP_035905.1; NM_011775.7.
DR PDB; 5BUP; X-ray; 2.25 A; A=463-664.
DR PDB; 5II6; X-ray; 0.95 A; A=35-138.
DR PDBsum; 5BUP; -.
DR PDBsum; 5II6; -.
DR AlphaFoldDB; P20239; -.
DR SMR; P20239; -.
DR BioGRID; 204708; 1.
DR STRING; 10090.ENSMUSP00000033207; -.
DR GlyConnect; 630; 4 O-Linked glycans.
DR GlyConnect; 635; 24 N-Linked glycans, 10 O-Linked glycans.
DR GlyGen; P20239; 8 sites, 48 N-linked glycans (1 site), 22 O-linked glycans (1 site).
DR iPTMnet; P20239; -.
DR PhosphoSitePlus; P20239; -.
DR MaxQB; P20239; -.
DR PaxDb; P20239; -.
DR PRIDE; P20239; -.
DR ProteomicsDB; 275048; -.
DR ABCD; P20239; 1 sequenced antibody.
DR Antibodypedia; 2312; 131 antibodies from 24 providers.
DR DNASU; 22787; -.
DR Ensembl; ENSMUST00000033207; ENSMUSP00000033207; ENSMUSG00000030911.
DR GeneID; 22787; -.
DR KEGG; mmu:22787; -.
DR UCSC; uc009jmi.1; mouse.
DR CTD; 7783; -.
DR MGI; MGI:99214; Zp2.
DR VEuPathDB; HostDB:ENSMUSG00000030911; -.
DR eggNOG; ENOG502QPI2; Eukaryota.
DR GeneTree; ENSGT00940000160133; -.
DR HOGENOM; CLU_024386_0_0_1; -.
DR InParanoid; P20239; -.
DR OMA; CHYSRDD; -.
DR OrthoDB; 586615at2759; -.
DR PhylomeDB; P20239; -.
DR TreeFam; TF332794; -.
DR Reactome; R-MMU-2534343; Interaction With Cumulus Cells And The Zona Pellucida.
DR BioGRID-ORCS; 22787; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Zp2; mouse.
DR PRO; PR:P20239; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P20239; protein.
DR Bgee; ENSMUSG00000030911; Expressed in primary oocyte and 21 other tissues.
DR ExpressionAtlas; P20239; baseline and differential.
DR Genevisible; P20239; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB.
DR GO; GO:0035805; C:egg coat; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA: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:0005771; C:multivesicular body; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032190; F:acrosin binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0035804; F:structural constituent of egg coat; ISS:UniProtKB.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IDA:UniProtKB.
DR GO; GO:0060468; P:prevention of polyspermy; IDA:UniProtKB.
DR DisProt; DP01645; -.
DR Gene3D; 2.60.40.4100; -; 1.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR001507; ZP_dom.
DR InterPro; IPR017977; ZP_dom_CS.
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 3D-structure; Cell membrane; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Fertilization; Glycoprotein; Membrane; Receptor; Reference proteome;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|PubMed:12799386,
FT ECO:0000269|PubMed:1690843"
FT CHAIN 35..633
FT /note="Zona pellucida sperm-binding protein 2"
FT /id="PRO_0000041693"
FT CHAIN 35..?
FT /note="Processed zona pellucida sperm-binding protein 2"
FT /id="PRO_0000304561"
FT PROPEP 634..713
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:12799386,
FT ECO:0000305|PubMed:26811476"
FT /id="PRO_0000041694"
FT TOPO_DOM 35..683
FT /note="Extracellular"
FT TRANSMEM 684..703
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 704..713
FT /note="Cytoplasmic"
FT DOMAIN 364..630
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REGION 462..484
FT /note="Disordered"
FT /evidence="ECO:0000269|PubMed:26811476"
FT SITE 167..168
FT /note="Cleavage; by ASTL"
FT /evidence="ECO:0000269|PubMed:22472438"
FT SITE 633..634
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:12799386,
FT ECO:0000305|PubMed:26811476"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12799386"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12799386"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12799386"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12799386"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12799386"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12799386"
FT CARBOHYD 455
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305"
FT DISULFID 51..134
FT /evidence="ECO:0000269|PubMed:28622512,
FT ECO:0007744|PDB:5II6"
FT DISULFID 84..102
FT /evidence="ECO:0000269|PubMed:12799386,
FT ECO:0000269|PubMed:28622512, ECO:0007744|PDB:5II6"
FT DISULFID 365..458
FT /evidence="ECO:0000269|PubMed:12799386"
FT DISULFID 396..417
FT /evidence="ECO:0000269|PubMed:12799386"
FT DISULFID 538..608
FT /evidence="ECO:0000269|PubMed:26811476,
FT ECO:0007744|PDB:5BUP"
FT DISULFID 559..627
FT /evidence="ECO:0000269|PubMed:26811476,
FT ECO:0007744|PDB:5BUP"
FT DISULFID 613..623
FT /evidence="ECO:0000269|PubMed:26811476,
FT ECO:0007744|PDB:5BUP"
FT MUTAGEN 634..635
FT /note="KR->NA: Abolishes proteolytic cleavage of the
FT propeptide."
FT /evidence="ECO:0000269|PubMed:26811476"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:5II6"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:5II6"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:5II6"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:5II6"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:5II6"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:5II6"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:5II6"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:5II6"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:5II6"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:5II6"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:5II6"
FT STRAND 487..495
FT /evidence="ECO:0007829|PDB:5BUP"
FT HELIX 504..506
FT /evidence="ECO:0007829|PDB:5BUP"
FT STRAND 508..512
FT /evidence="ECO:0007829|PDB:5BUP"
FT STRAND 517..524
FT /evidence="ECO:0007829|PDB:5BUP"
FT STRAND 532..544
FT /evidence="ECO:0007829|PDB:5BUP"
FT STRAND 549..556
FT /evidence="ECO:0007829|PDB:5BUP"
FT STRAND 565..570
FT /evidence="ECO:0007829|PDB:5BUP"
FT HELIX 580..582
FT /evidence="ECO:0007829|PDB:5BUP"
FT STRAND 583..590
FT /evidence="ECO:0007829|PDB:5BUP"
FT STRAND 602..613
FT /evidence="ECO:0007829|PDB:5BUP"
FT HELIX 621..623
FT /evidence="ECO:0007829|PDB:5BUP"
FT TURN 634..636
FT /evidence="ECO:0007829|PDB:5BUP"
FT STRAND 643..646
FT /evidence="ECO:0007829|PDB:5BUP"
FT STRAND 651..654
FT /evidence="ECO:0007829|PDB:5BUP"
SQ SEQUENCE 713 AA; 80210 MW; DCF9AE6CCD3461EF CRC64;
MARWQRKASV SSPCGRSIYR FLSLLFTLVT SVNSVSLPQS ENPAFPGTLI CDKDEVRIEF
SSRFDMEKWN PSVVDTLGSE ILNCTYALDL ERFVLKFPYE TCTIKVVGGY QVNIRVGDTT
TDVRYKDDMY HFFCPAIQAE THEISEIVVC RRDLISFSFP QLFSRLADEN QNVSEMGWIV
KIGNGTRAHI LPLKDAIVQG FNLLIDSQKV TLHVPANATG IVHYVQESSY LYTVQLELLF
STTGQKIVFS SHAICAPDLS VACNATHMTL TIPEFPGKLE SVDFGQWSIP EDQWHANGID
KEATNGLRLN FRKSLLKTKP SEKCPFYQFY LSSLKLTFYF QGNMLSTVID PECHCESPVS
IDELCAQDGF MDFEVYSHQT KPALNLDTLL VGNSSCQPIF KVQSVGLARF HIPLNGCGTR
QKFEGDKVIY ENEIHALWEN PPSNIVFRNS EFRMTVRCYY IRDSMLLNAH VKGHPSPEAF
VKPGPLVLVL QTYPDQSYQR PYRKDEYPLV RYLRQPIYME VKVLSRNDPN IKLVLDDCWA
TSSEDPASAP QWQIVMDGCE YELDNYRTTF HPAGSSAAHS GHYQRFDVKT FAFVSEARGL
SSLIYFHCSA LICNQVSLDS PLCSVTCPAS LRSKREANKE DTMTVSLPGP ILLLSDVSSS
KGVDPSSSEI TKDIIAKDIA SKTLGAVAAL VGSAVILGFI CYLYKKRTIR FNH
