ZP2_FELCA
ID ZP2_FELCA Reviewed; 716 AA.
AC P47984;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 101.
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 Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=7841460; DOI=10.3109/10425179409010186;
RA Harris J.D., Hibler D.W., Fontenot G.K., Hsu K.T., Yurewicz E.C.,
RA Sacco A.G.;
RT "Cloning and characterization of zona pellucida genes and cDNAs from a
RT variety of mammalian species: the ZPA, ZPB and ZPC gene families.";
RL DNA Seq. 4:361-393(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RA Okazaki Y., Isojima S., Sugimoto M.;
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; U05776; AAA74388.1; -; mRNA.
DR EMBL; D45067; BAA08095.1; -; mRNA.
DR PIR; S70398; S70398.
DR RefSeq; NP_001009875.1; NM_001009875.1.
DR AlphaFoldDB; P47984; -.
DR SMR; P47984; -.
DR STRING; 9685.ENSFCAP00000014068; -.
DR PRIDE; P47984; -.
DR GeneID; 493977; -.
DR KEGG; fca:493977; -.
DR CTD; 7783; -.
DR eggNOG; ENOG502QPI2; Eukaryota.
DR InParanoid; P47984; -.
DR OrthoDB; 586615at2759; -.
DR Proteomes; UP000011712; 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; 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; 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..38
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT CHAIN 39..639
FT /note="Zona pellucida sperm-binding protein 2"
FT /id="PRO_0000041687"
FT CHAIN 39..?
FT /note="Processed zona pellucida sperm-binding protein 2"
FT /id="PRO_0000304558"
FT PROPEP 640..716
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT /id="PRO_0000041688"
FT TOPO_DOM 39..686
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 687..707
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 708..716
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 370..636
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REGION 468..490
FT /note="Disordered"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT SITE 171..172
FT /note="Cleavage; by ASTL"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT SITE 639..640
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..138
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 88..106
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 371..464
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 402..423
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 544..614
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 565..633
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 619..629
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT CONFLICT 397
FT /note="V -> G (in Ref. 2; BAA08095)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="L -> P (in Ref. 2; BAA08095)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="F -> S (in Ref. 2; BAA08095)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 716 AA; 80136 MW; C5745496E82CB671 CRC64;
MASRQKGDSG SPSSWFNADW STYRSLFLLF ILVTSVNSIG VLQLVNPVFP GTVTCYETRM
AVEFPSDFGT KKWHTSVVDP FSFELLNCTY ILDPENLTLK APYETCTRRT LGQHRMIIRL
KDHNAASRHN SLMYQINCPV MQAEETHEHA GSTICTKDSM SFTFNVIPGL ADENTDIKNP
MGWSIEVGDG TKAKTLTLQD VLRQGYNILF DNHKITFQVS FNATGVTHYM QGNSHLYMVP
LKLIHESLGQ KIILTTRVLC MSDAVTCNAT HVTLTIPEFP GKLKSVSSEN RNFAVSQLHN
NGIDKEESSG LTLHFSKTLL KMEFSEKCLP YQFYLASLKL TFAFNQETIS TVLYPECVCE
SPVSIVTGDL CTQDGFMDIK VYSHQTKPAL NLETLRVGDS SCQPTFQAAS QGLILFHIPL
NGCGTRHKFK EGKVIYENEI HAVWADLPPS TISRDSEFRM TVQCHYSKGD LLINTRVQSL
PPLEASVRPG PLALILQTYP DKSYLQPYGE KEYPVVRYLR QPIYLEVRVL NRSDPNIKLV
LDDCWATPTM DPASVPQWNI IMDGCEYNLD NHRTTFHPVG SSVTYPTHYR RFDVKTFAFV
SEAQVLSSLV YFHCSVLICS RLSADSPLCS VTCPVSFRHR RATGTTEEEK MIVSLPGPIL
LLSDSSSLRD VVDSKGYGAA GYVAFKTVVA VAALAGLVAT LGFITYLRKN RTMINH
