ZP2_MACRA
ID ZP2_MACRA Reviewed; 745 AA.
AC O77726;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 83.
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 Macaca radiata (Bonnet macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9548;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Ovary;
RX PubMed=9590540;
RX DOI=10.1002/(sici)1098-2795(199806)50:2<229::aid-mrd14>3.0.co;2-1;
RA Jethanandani P., Santhanam R., Gupta S.K.;
RT "Molecular cloning and expression in Escherichia coli of cDNA encoding
RT bonnet monkey (Macaca radiata) zona pellucida glycoprotein-ZP2.";
RL Mol. Reprod. Dev. 50:229-239(1998).
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:0000269|PubMed:9590540}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20239};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P20239}.
CC -!- TISSUE SPECIFICITY: Expressed in oocytes (at protein level).
CC {ECO:0000269|PubMed:9590540}.
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; Y10690; CAA71693.1; -; mRNA.
DR AlphaFoldDB; O77726; -.
DR SMR; O77726; -.
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 1: Evidence at protein level;
KW Cell membrane; Cleavage on pair of basic residues; Disulfide bond;
KW Extracellular matrix; Fertilization; Glycoprotein; Membrane; Receptor;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..38
FT CHAIN 39..640
FT /note="Zona pellucida sperm-binding protein 2"
FT /id="PRO_0000041691"
FT CHAIN 39..?
FT /note="Processed zona pellucida sperm-binding protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000304560"
FT PROPEP 641..745
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT /id="PRO_0000041692"
FT TOPO_DOM 39..716
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 717..736
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 737..745
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 371..637
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REGION 469..491
FT /note="Disordered"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT REGION 673..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 172..173
FT /note="Cleavage; by ASTL"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT SITE 640..641
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
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 372..465
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 403..424
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 545..615
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 566..634
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 620..630
FT /evidence="ECO:0000250|UniProtKB:P20239"
SQ SEQUENCE 745 AA; 82710 MW; 731D9AFA4D3EE028 CRC64;
MACGQRGGSW RPSGWFNAGW STYRSISLFF ALVTSVNSID VFQLVNPAFP GTVICDERGI
TVEFPSSPGT KKWHASVVDP LGLNVPNCTY ILNPEKFTLR VTYENCTRRV HGGYQMTIRV
MNDSAALRHG AVMYQFFCPA MQVEETQGLS ASTICKKDFM SFSLPRVFSG LADDNKVTKL
KMGWSIEVGD GARVKTLTLP EAMKEGFSLL IDNHRMIFHV PFNATGVTHY VQGNSHLYMV
SLKLTFISPG QKVIFSSQAI CAPDPVNCNA THMTLTIPEF PGKLKSVSFE NQNIDVSQLH
DNGIDLEATN GTKLHFSKTL LKTKLSEKCL LHQFYLASLR LTFLLQSETV SMVIYPECVC
ESPVSIVTGE LCTQDGFMDF EVYSYQTQPA LDLDTLRVGN SSCQPVFKAQ SQGLVRFHIP
LNGCGTRYKF EDDKVIYENE IHALWTDLPP SKISRDSEFR MTVKCSYSRN DMLLNINVES
LTPPVASVKL GPFTLILQSY PDNSYQQPYG ENEYPLVRFL RQPIYMEVRV INRDDPNIKL
VLDDCWATST MDPDSFPQWN IVVDGCAYEL DNYQTTFHPV GSSVTHPDHY QRFDMKAFAF
VSEAHVLSSL VYFHCSALIC NRLSPDSPLC SVTCPVSSRH RRATEATEAE KMTVSLPGPI
LLLSDDSSFR GVGSSDLKAS GSSGENSRSE TGEEVGSRDV MDTKGHRTAG DVGSKAVAAV
AALAGVVATL GFICYLYKKR TVSNH
