ZP2_PIG
ID ZP2_PIG Reviewed; 716 AA.
AC P42099;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 109.
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 AltName: Full=pZP1 {ECO:0000303|PubMed:7864874};
DE Contains:
DE RecName: Full=Processed zona pellucida sperm-binding protein 2;
DE Flags: Precursor;
GN Name=ZP2; Synonyms=ZPA;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RA Okazaki Y., Isojima S., Sugimoto M.;
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RA Yurewicz E.C., Hibler D., Fontenot G.K., Harris J.;
RL Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=7864874; DOI=10.1006/bbrc.1995.1256;
RA Taya T., Yamasaki N., Tsubamoto H., Hasegawa A., Koyama K.;
RT "Cloning of a cDNA coding for porcine zona pellucida glycoprotein ZP1 and
RT its genomic organization.";
RL Biochem. Biophys. Res. Commun. 207:790-799(1995).
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:7864874}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D45064; BAA08092.1; -; mRNA.
DR EMBL; L22170; AAA31144.1; -; mRNA.
DR EMBL; S74651; AAB33431.2; -; mRNA.
DR PIR; S70434; S70434.
DR RefSeq; NP_999013.1; NM_213848.2.
DR AlphaFoldDB; P42099; -.
DR SMR; P42099; -.
DR STRING; 9823.ENSSSCP00000008380; -.
DR PaxDb; P42099; -.
DR PRIDE; P42099; -.
DR Ensembl; ENSSSCT00030029668; ENSSSCP00030013325; ENSSSCG00030021372.
DR Ensembl; ENSSSCT00040052907; ENSSSCP00040021996; ENSSSCG00040039539.
DR Ensembl; ENSSSCT00060105621; ENSSSCP00060046460; ENSSSCG00060076887.
DR GeneID; 396846; -.
DR KEGG; ssc:396846; -.
DR CTD; 7783; -.
DR eggNOG; ENOG502QPI2; Eukaryota.
DR InParanoid; P42099; -.
DR OrthoDB; 586615at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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: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 2: Evidence at transcript level;
KW Cell membrane; Cleavage on pair of basic residues; Disulfide bond;
KW Extracellular matrix; Fertilization; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT CHAIN 36..638
FT /note="Zona pellucida sperm-binding protein 2"
FT /id="PRO_0000041695"
FT CHAIN 36..?
FT /note="Processed zona pellucida sperm-binding protein 2"
FT /id="PRO_0000304562"
FT PROPEP 639..716
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT /id="PRO_0000041696"
FT TOPO_DOM 36..686
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 687..706
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 707..716
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 370..635
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REGION 467..489
FT /note="Disordered"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT SITE 168..169
FT /note="Cleavage; by ASTL"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT SITE 638..639
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..135
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 85..103
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 371..463
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 402..423
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 543..613
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 564..632
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 618..628
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT CONFLICT 1..3
FT /note="MAC -> IPG (in Ref. 2; AAA31144)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="R -> K (in Ref. 3; AAB33431)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="L -> Q (in Ref. 1; BAA08092)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="K -> R (in Ref. 1; BAA08092)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="E -> G (in Ref. 3; AAB33431)"
FT /evidence="ECO:0000305"
FT CONFLICT 465..466
FT /note="YS -> SR (in Ref. 2; AAA31144)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 716 AA; 79728 MW; 4CF39353D3A0F1E7 CRC64;
MACRHRGDSG RPLSWLSASW RSLLLFFPLV TSVNSIGVNQ LVNTAFPGIV TCHENRMVVE
FPRILGTKIQ YTSVVDPLGL EMMNCTYVLD PENLTLKAPY EACTKRVRGH HQMTIRLIDD
NAALRQEALM YHISCPVMGA EGPDQHSGST ICMKDFMSFT FNFFPGMADE NVKREDSKQR
MGWSLVVGDG ERARTLTFQE AMTQGYNFLI ENQKMNIQVS FHATGVTRYS QGNSHLYMVP
LKLKHVSHGQ SLILASQLIC VADPVTCNAT HVTLAIPEFP GKLKSVNLGS GNIAVSQLHK
HGIEMETTNG LRLHFNQTLL KTNVSEKCLP HQLYLSSLKL TFHSQLEAVS MVIYPECLCE
STVSLVSEEL CTQDGFMDVK VHSHQTKPAL NLDTLRVGDS SCQPTFKAPA QGLVQFRIPL
NGCGTRHKFK NDKVIYENEI HALWADPPSA VSRDSEFRMT VRCSYSSSNM LINTNVESLP
SPEASVKPGP LTLTLQTYPD NAYLQPYGDK EYPVVKYLRQ PIYLEVRILN RTDPNIKLVL
DDCWATSTED PASLPQWNVV MDGCEYNLDN HRTTFHPVGS SVTYPNHHQR FDVKTFAFVS
GAQGVSQLVY FHCSVFICNQ LSPTFSLCSV TCHGPSRSRR ATGTTEEEKM IVSLPGPILL
LSDGSSLRDA VNSKGSRTNG YVAFKTMVAM VASAGIVATL GLISYLHKKR IMMLNH
