ZP2_CANLF
ID ZP2_CANLF Reviewed; 715 AA.
AC P47983;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 105.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
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; U05779; AAA74386.1; -; mRNA.
DR EMBL; D45069; BAA08097.1; -; mRNA.
DR PIR; S70397; S70397.
DR RefSeq; NP_001003304.1; NM_001003304.1.
DR AlphaFoldDB; P47983; -.
DR SMR; P47983; -.
DR STRING; 9612.ENSCAFP00000026286; -.
DR PaxDb; P47983; -.
DR GeneID; 403988; -.
DR KEGG; cfa:403988; -.
DR CTD; 7783; -.
DR eggNOG; ENOG502QPI2; Eukaryota.
DR InParanoid; P47983; -.
DR OrthoDB; 586615at2759; -.
DR Proteomes; UP000002254; 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:0016234; C:inclusion body; IDA:UniProtKB.
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:0002455; P:humoral immune response mediated by circulating immunoglobulin; IDA: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..637
FT /note="Zona pellucida sperm-binding protein 2"
FT /id="PRO_0000041685"
FT CHAIN 39..?
FT /note="Processed zona pellucida sperm-binding protein 2"
FT /id="PRO_0000304557"
FT PROPEP 638..715
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT /id="PRO_0000041686"
FT TOPO_DOM 39..684
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 685..705
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 706..715
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 368..634
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REGION 466..488
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 637..638
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 459
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT DISULFID 55..138
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 88..106
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 369..462
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 400..421
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 542..612
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 563..631
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 617..627
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT CONFLICT 15
FT /note="R -> W (in Ref. 2; BAA08097)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="R -> A (in Ref. 2; BAA08097)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="L -> P (in Ref. 2; BAA08097)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="S -> A (in Ref. 2; BAA08097)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 715 AA; 79939 MW; 508D6DE804F4DC5C CRC64;
MACKQKGDSG SPSSRFSADW STYRSLSLFF ILVTSVNSVG VMQLVNPIFP GTVICHENKM
TVEFPRDLGT KKWHASVVDP FSFELLNCTS ILDPEKLTLK APYETCSRRV LGQHQMAIRL
TDNNAASRHK AFMYQISCPV MQTEETHEHA GSTICTKDSM SFTFNIIPGM ADENTNPSGG
KWMMEVDDAK AQNLTLREAL MQGYNFLFDS HRLSVQVSFN ATGVTHYMQG NSHLYTVPLK
LIHTSPGQKI ILTTRVLCMS DPVTCNATHM TLTIPEFPGK LQSVRFENTN FRVSQLHNHG
IDKEELNGLR LHFSKSLLKM NSSEKCLLYQ FYLASLKLTF AFERDTVSTV VYPECVCEPP
VTIVTGDLCT QDGFMDVKVY SHQTKPALNL DTLRVGDSSC QPTFKAPSQG LTLFHIPLNG
CGTRLKFKGD TVIYENEIHA LWTDLPPSTI SRDSEFRMTV KCHYSRDDLL INTNVQSLPP
PVASVRPGPL ALILQTYPDK SYLRPYGDKE YPVVRYLRQP IYLEVKVLNR ADPNIKLVLD
DCWATPTMDP ASLPQWNIVM DGCEYNLDNY RTTFHPVGSS VTYPTHYQRF DVKTFAFISE
AQVLSSLVYF HCTALICNRL SPDSPLCSVT CPVSSRHRRA TGSTEEEKMI VSLPGPILLL
ADSSSLRDGV DSKGHRAAGY VAFKTVVAVA ALAGLVAALG LIIYLRKKRT MVLNH
