ZP1_RAT
ID ZP1_RAT Reviewed; 617 AA.
AC O54766;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 122.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Ovary;
RX PubMed=9820205;
RX DOI=10.1002/(sici)1098-2795(199812)51:4<454::aid-mrd13>3.0.co;2-g;
RA Akatsuka K., Yoshida-Komiya H., Tulsiani D.R.P., Orgebin-Crist M.-C.,
RA Hiroi M., Araki Y.;
RT "Rat zona pellucida glycoproteins: molecular cloning and characterization
RT of the three major components.";
RL Mol. Reprod. Dev. 51:454-467(1998).
RN [2]
RP PROTEIN SEQUENCE OF C-TERMINUS, PYROGLUTAMATE FORMATION AT GLN-21,
RP DISULFIDE BOND FORMATION AT 447-CYS--CYS-468, GLYCOSYLATION AT ASN-49;
RP ASN-68 AND ASN-369, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16342937; DOI=10.1021/bi051883f;
RA Boja E.S., Hoodbhoy T., Garfield M., Fales H.M.;
RT "Structural conservation of mouse and rat zona pellucida glycoproteins.
RT Probing the native rat zona pellucida proteome by mass spectrometry.";
RL Biochemistry 44:16445-16460(2005).
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.
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:0000250|UniProtKB:P60852}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P48829};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in oocytes.
CC -!- DOMAIN: The ZP domain is involved in the polymerization of the ZP
CC proteins to form the zona pellucida.
CC -!- PTM: Proteolytically cleaved before the transmembrane segment to yield
CC the secreted ectodomain incorporated in the zona pellucida.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ZP domain family. ZPB 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; AB000928; BAA24486.1; -; mRNA.
DR RefSeq; NP_445961.1; NM_053509.1.
DR AlphaFoldDB; O54766; -.
DR SMR; O54766; -.
DR STRING; 10116.ENSRNOP00000028396; -.
DR GlyGen; O54766; 3 sites.
DR iPTMnet; O54766; -.
DR PaxDb; O54766; -.
DR PRIDE; O54766; -.
DR GeneID; 85271; -.
DR KEGG; rno:85271; -.
DR UCSC; RGD:620604; rat.
DR CTD; 22917; -.
DR RGD; 620604; Zp1.
DR eggNOG; ENOG502RYNN; Eukaryota.
DR InParanoid; O54766; -.
DR OrthoDB; 586615at2759; -.
DR PhylomeDB; O54766; -.
DR PRO; PR:O54766; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:RGD.
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: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; IBA:GO_Central.
DR GO; GO:0060468; P:prevention of polyspermy; IBA:GO_Central.
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 InterPro; IPR017977; ZP_dom_CS.
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; 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;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Fertilization; Glycoprotein; Membrane; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:16342937"
FT CHAIN 21..544
FT /note="Zona pellucida sperm-binding protein 1"
FT /id="PRO_0000041681"
FT CHAIN 21..?
FT /note="Processed zona pellucida sperm-binding protein 1"
FT /id="PRO_0000304555"
FT PROPEP 545..617
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:16342937"
FT /id="PRO_0000041682"
FT TOPO_DOM 21..588
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 589..609
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 610..617
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 224..264
FT /note="P-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DOMAIN 269..540
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REGION 179..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..194
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:16342937"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16342937"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16342937"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16342937"
FT DISULFID 226..251
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 235..250
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 245..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 447..468
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779,
FT ECO:0000269|PubMed:16342937"
SQ SEQUENCE 617 AA; 67853 MW; AF52D9227F8A4CCC CRC64;
MAWGCFVVLL LLVAAPLRLG QHLHLKPGFQ YSYDCGVQGM QLLVFPRPNQ TIQFKVLDEF
GNRFEVNNCS ICYHWVISEA QKPAVFSADY KGCHVLEKQD GRFHLRVFIQ AVLPNGRVDT
AQDVTLICPK PDHILTPESY LAPPTTPQPF IPHTFALHPI SGHTLAGSGH TGLTTLYPET
HPTPAPPSSE PGPVGPTVPQ SQWGTLGSWE LTELDSIGTH LLQERCQVAS GHIPCMVKGS
SEEACQQAGC CYDNTKEMPC YYGNTVTLQC FRSGYFTLVM SQETALTHGV MLDNVHLAYA
PNGCPPTQKT SAFVVFHVPL TLCGTAIQVV GKQLVYENQL VSNIEVQTGP QGSITRDGVF
RLHVRCIFNA SDFLPIRASI FSPQPPAPVT RSGPLRLELR IATDKTFSSY YQGSDYPLVR
LLQEPVYIEV RLLQRTDPGL ALMLHQCWAT PSASPFEQPQ WPILSDGCPF KGDNYRTQMV
AADRATLPFW SHYQRFTIAT FTLLDSSSQN ALRGQVYFFC SASACHPVGS ETCSTTCDSE
IARHRRSSGH HNSTIRALDI VSSPGAVGFE DAPKLEPSGS TRNSGSRPLL WVLQLLALTL
VLGDGVLVGL SWAWAWA
