ZP1_RABIT
ID ZP1_RABIT Reviewed; 627 AA.
AC I6M4H4;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Zona pellucida sperm-binding protein 1;
DE AltName: Full=Zona pellucida glycoprotein 1;
DE Short=Zp-1;
DE Contains:
DE RecName: Full=Processed zona pellucida sperm-binding protein 1;
DE Flags: Precursor;
GN Name=ZP1;
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], IDENTIFICATION BY MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke;
RG The Genome Sequencing Platform;
RA Di Palma F., Heiman D., Young S., Gnerre S., Johnson J., Lander E.S.,
RA Lindblad-Toh K.;
RT "Genome Sequence of Oryctolagus cuniculus (European rabbit).";
RL Submitted (AUG-2009) 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 ZP1 ensures the structural integrity of the zona pellucida (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: 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:P60852}.
CC -!- SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein
CC 1]: Zona pellucida {ECO:0000269|PubMed:22842159}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P48829};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in 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}.
CC -!- PTM: Proteolytically cleaved before the transmembrane segment to yield
CC the secreted ectodomain incorporated in the zona pellucida.
CC {ECO:0000250}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ZP domain family. ZPB subfamily.
CC {ECO:0000305}.
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DR EMBL; HQ702467; AEI98738.1; -; mRNA.
DR EMBL; AAGW02038248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001257409.1; NM_001270480.1.
DR AlphaFoldDB; I6M4H4; -.
DR SMR; I6M4H4; -.
DR STRING; 9986.ENSOCUP00000013464; -.
DR GeneID; 100354409; -.
DR KEGG; ocu:100354409; -.
DR CTD; 22917; -.
DR eggNOG; ENOG502RYNN; Eukaryota.
DR OrthoDB; 586615at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0035805; C:egg coat; 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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035804; F:structural constituent of egg coat; IDA:UniProtKB.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR CDD; cd00111; Trefoil; 1.
DR Gene3D; 2.60.40.4100; -; 1.
DR InterPro; IPR017957; P_trefoil_CS.
DR InterPro; IPR000519; P_trefoil_dom.
DR InterPro; IPR044913; P_trefoil_dom_sf.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR001507; ZP_dom.
DR Pfam; PF00088; Trefoil; 1.
DR Pfam; PF00100; Zona_pellucida; 1.
DR PRINTS; PR00023; ZPELLUCIDA.
DR SMART; SM00018; PD; 1.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF57492; SSF57492; 1.
DR PROSITE; PS00025; P_TREFOIL_1; 1.
DR PROSITE; PS51448; P_TREFOIL_2; 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;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..537
FT /note="Zona pellucida sperm-binding protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000425574"
FT CHAIN 21..?
FT /note="Processed zona pellucida sperm-binding protein 1"
FT /id="PRO_0000425575"
FT PROPEP 538..627
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000425576"
FT TOPO_DOM 21..585
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 586..606
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 607..627
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 217..257
FT /note="P-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DOMAIN 262..533
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REGION 537..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:Q62005"
FT DISULFID 219..244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 228..243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 238..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 440..461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
SQ SEQUENCE 627 AA; 68745 MW; FC498B1C934C15C0 CRC64;
MTGGRLVALL LLVAASLGLG QQPHPEPGLP GLQYSYDCGM RGMQLVVLPR PGRTIRFKVV
DEFGNRFEVN NCSICFHWVS AEPQAPAVFS ADYKGCHVLE KEGHSHLTVF IEAMLPDGHV
EVAQEAVLIC PKPGHTWAVG SHQVPPTTPS PTTPHALPFH LSSAHTFPIP LYLEHSLMLP
TPAGPSLGPG PTPAVLAQVE RWEVDKPDAV GSHLPQEWCQ VASGHIPCIV QSSSKEACEQ
AGCCYDSARE VPCYYGNTAT VQCFRNGYFI LVVAQEMALA HRITLANVHL AYAPTRCPPA
QKTSAFVIFH VPLTHCGTTV QVLGSQLFYE NQLVSDIDVR EGPQGSITRD SSFRLLVRCI
FNASDFLPIQ ASIFSPPLPA PVTQAGPLRL ELRIARDETF SSFYEEEDYP LVRLLREPVH
VEVRLLQRTD PSLVLELHQC WATPSANPVQ QPQWPLLSDG CPFKGDSYRT RVLALDRAEL
PFRSHYQRFT VATFTFLDSG AQRALRGLVY FFCSASACHP SGPETCSSTC SSRTAKRRRS
SGYHDGTPRA LDIVSSPGPV GFQDSHRQEP TLESTGSGRN SNPKPLLWVV LLLLAIALVL
GIGVFVGLSQ AWAHKLREGH RLTDQAQ
