ZP2_RAT
ID ZP2_RAT Reviewed; 695 AA.
AC O54767;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 102.
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=Zpa;
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], PROTEIN SEQUENCE OF 27-31, AND TISSUE
RP SPECIFICITY.
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 [2]
RP PROTEIN SEQUENCE OF N-TERMINUS, DISULFIDE BOND FORMATION AT 73-CYS--CYS-91;
RP 354-CYS--CYS-447 AND 385-CYS--CYS-406, GLYCOSYLATION AT ASN-72; ASN-161;
RP ASN-173; ASN-206; ASN-253; ASN-382 AND ASN-563, AND IDENTIFICATION BY MASS
RP 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 ZP2 may act as a secondary sperm receptor.
CC {ECO:0000250|UniProtKB:P20239}.
CC -!- SUBUNIT: Can form homopolymers that assemble into long fibers (in
CC vitro). 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:Q05996}.
CC -!- SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein
CC 2]: Zona pellucida {ECO:0000250|UniProtKB:P20239}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20239};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in oocytes. {ECO:0000269|PubMed:9820205}.
CC -!- DOMAIN: The ZP domain is involved in the polymerization of the ZP
CC proteins to form the zona pellucida. {ECO:0000250|UniProtKB:P20239}.
CC -!- PTM: Proteolytically cleaved before the transmembrane segment to yield
CC the secreted ectodomain incorporated in the zona pellucida.
CC {ECO:0000250|UniProtKB:P20239}.
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:0000250|UniProtKB:P20239}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P20239}.
CC -!- PTM: O-glycosylated; contains sulfate-substituted glycans.
CC {ECO:0000250|UniProtKB:P20239}.
CC -!- SIMILARITY: Belongs to the ZP domain family. ZPA subfamily.
CC {ECO:0000305}.
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DR EMBL; AB000929; BAA24487.1; -; mRNA.
DR RefSeq; NP_112412.1; NM_031150.1.
DR AlphaFoldDB; O54767; -.
DR SMR; O54767; -.
DR STRING; 10116.ENSRNOP00000064370; -.
DR GlyGen; O54767; 8 sites.
DR iPTMnet; O54767; -.
DR PaxDb; O54767; -.
DR GeneID; 81828; -.
DR KEGG; rno:81828; -.
DR CTD; 7783; -.
DR RGD; 620605; Zp2.
DR eggNOG; ENOG502QPI2; Eukaryota.
DR InParanoid; O54767; -.
DR OrthoDB; 586615at2759; -.
DR PhylomeDB; O54767; -.
DR PRO; PR:O54767; -.
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:0005783; C:endoplasmic reticulum; 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:0005771; C:multivesicular body; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032190; F:acrosin binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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:0060468; P:prevention of polyspermy; ISS:UniProtKB.
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 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..24
FT /evidence="ECO:0000269|PubMed:16342937"
FT CHAIN 25..619
FT /note="Zona pellucida sperm-binding protein 2"
FT /id="PRO_0000041699"
FT CHAIN 25..?
FT /note="Processed zona pellucida sperm-binding protein 2"
FT /id="PRO_0000304564"
FT PROPEP 620..695
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT /id="PRO_0000041700"
FT TOPO_DOM 25..664
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 665..685
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 686..695
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 353..616
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REGION 451..473
FT /note="Disordered"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT SITE 156..157
FT /note="Cleavage; by ASTL"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT SITE 619..620
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine; partial"
FT /evidence="ECO:0000269|PubMed:16342937"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine; partial"
FT /evidence="ECO:0000269|PubMed:16342937"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16342937"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16342937"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16342937"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16342937"
FT CARBOHYD 444
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16342937"
FT DISULFID 40..123
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 73..91
FT /evidence="ECO:0000269|PubMed:16342937"
FT DISULFID 354..447
FT /evidence="ECO:0000269|PubMed:16342937"
FT DISULFID 385..406
FT /evidence="ECO:0000269|PubMed:16342937"
FT DISULFID 527..597
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 548..613
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 602..609
FT /evidence="ECO:0000250|UniProtKB:P20239"
SQ SEQUENCE 695 AA; 78444 MW; B1660D35C01D1635 CRC64;
MARWQRVYWL RSLFFALVTS VNSLSLPQSE NPAFPGTLIC DKDEVRVEFS SRFDMEKWNP
SLVDTFGNEI SNCTYALDLE KFILKFPYET CTIKVIGGYQ VNIRVQDTNA DVSYKDDVHH
FFCPAIQAEI HEVSEIVVCM EDLISFSFPQ LFSRLADENQ NVSEMGWIIK IGNGTRVHTL
PLKDAIVQGF NLLIDSQKIT LHVPANATGV AHYVQESSYL YTVQLKLLFS SPGQKITFSS
QAICAPDLSV ACNVTHMSLT IPEFPGKLKS VGFGQRNIPE DQWHANGIDK EATNGLRLHF
RKSLLKTKPS EKCPFYQFYF SSLELTFNFQ GDMLSTVIDP ECHCESPVSI DELCTRDGFM
DFEVYSHQTK PALNLESLLV GNSSCQPIFK VQSLGLARFH IPLNGCGTRQ KFEGDKVIYE
NEIHALWENP PSNIIFRNSE FRMTVRCHYI RDSMLLRAHI KSHSSPVASV KPGPLALVLQ
TYPDISYQRP YRKNEYPLVR YLRQPIYMEV TVLNRNDPNI KLVLDDCWAT TFEDPASVPQ
WQIIMDGCEY ELDNYRTTFH AANSSAAHSG HYQRFDVKTF AFVSESRGLS SLIYFHCSAL
ICNQASPLCS VTCPAPLRNK REASKEGTMT VSLPGPIILL SDDSSSKGVM NPDSYEITKD
IASKTLGAVA ALVGSAVIIG FICYLHKKRI VRFNS
