ZP2_RABIT
ID ZP2_RABIT Reviewed; 666 AA.
AC P48829;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Zona pellucida sperm-binding protein 2;
DE AltName: Full=75 kDa zona pellucida protein;
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; Fragment;
GN Name=ZP2; Synonyms=ZPA;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Ovary;
RX PubMed=7685342; DOI=10.1016/s0021-9258(18)31405-4;
RA Lee V.H., Schwoebel E.D., Prasad S.V., Cheung P., Timmons T.M., Cook R.G.,
RA Dunbar B.S.;
RT "Identification and structural characterization of the 75-kDa rabbit zona
RT pellucida protein.";
RL J. Biol. Chem. 268:12412-12417(1993).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Ovary;
RX PubMed=22842159; DOI=10.1016/j.jprot.2012.07.027;
RA Stetson I., Izquierdo-Rico M.J., Moros C., Chevret P., Lorenzo P.L.,
RA Ballesta J., Rebollar P.G., Gutierrez-Gallego R., Aviles M.;
RT "Rabbit zona pellucida composition: a molecular, proteomic and phylogenetic
RT approach.";
RL J. Proteomics 75:5920-5935(2012).
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: Oocytes (at protein level).
CC {ECO:0000269|PubMed:22842159}.
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; L12167; AAA31502.1; -; mRNA.
DR AlphaFoldDB; P48829; -.
DR SMR; P48829; -.
DR STRING; 9986.ENSOCUP00000011114; -.
DR PRIDE; P48829; -.
DR eggNOG; ENOG502QPI2; Eukaryota.
DR InParanoid; P48829; -.
DR Proteomes; UP000001811; 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; IDA: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 Reference proteome; Secreted; Transmembrane; Transmembrane helix.
FT CHAIN <1..588
FT /note="Zona pellucida sperm-binding protein 2"
FT /id="PRO_0000041697"
FT CHAIN <1..?
FT /note="Processed zona pellucida sperm-binding protein 2"
FT /id="PRO_0000304563"
FT PROPEP 589..666
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT /id="PRO_0000041698"
FT TOPO_DOM <1..636
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 637..656
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 657..666
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 319..585
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REGION 417..439
FT /note="Disordered"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT SITE 120..121
FT /note="Cleavage; by ASTL"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT SITE 588..589
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 613
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 6..89
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 39..57
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 320..413
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 351..372
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 493..563
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 514..582
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 568..578
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT NON_TER 1
SQ SEQUENCE 666 AA; 73644 MW; D6C8E2BA2D21020B CRC64;
PGTVTCNENE IIVEFPSYVG TKTLHASVVD PLGVEMLNCT YILDPEKLTL RVPYKACTRA
VHGGYQMSIR VMNNSAALRH TDVEYQFFCP VEQTLEFSKS AACTKDFMSL SFPHIPTGLG
DSTMVNESQM GWMVQAGHGP GAQTLSLEEA KGQGFGVLID DNKMTLSVLL NATGVTHYVE
GTSHLHTMFL KLSLVSPGQK MPFPSRAICL SGPVTCNATH MTLTIPEFPG KLESVSIENR
NITVSQLHDQ GIDVEAINGL RLHFSKTVLK TKFSEKCLHD QLYISSLKLT FNLELDTVST
VINPECPCDS PASIVSGELC TQDGFMDFEV YTHQTKPALN LDTLRVGSSS CQPVFKAQSQ
GLVRFRIPLN GCGTRHKFED EKVIYENEVH ALWENLPPSK ISRDSEFRMT VQCYYTRDDM
LLNANIKSLP PPVASVKPGP LALSLQTYPD ESYQQPYRVN EYPIVKYLRQ PIYMEVRVLN
RNDPNIKLAL DDCWATSSMD PASLPKWSIV MDGCEYSLDN YQTNFHPVGS SVTHPEHYQR
FDVKTFAFVS EAQARSSLVY FHCSALICNQ HYPDSPLCSV TCPGSSRHRR ATGNTEEERV
TASLPGPILL LPNGSSFRGV GDSKEHGMAG DVTSKTMAAV AAVAGVVATL GFISYLCKKR
TMMLSH
