OVGP1_MESAU
ID OVGP1_MESAU Reviewed; 671 AA.
AC Q60557; Q60526;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Oviduct-specific glycoprotein;
DE AltName: Full=Estrogen-dependent oviduct protein;
DE AltName: Full=Oviductal glycoprotein;
DE AltName: Full=Oviductin;
DE AltName: Full=ZP-0;
DE Flags: Precursor;
GN Name=OVGP1; Synonyms=OGP;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Oviduct;
RX PubMed=7492686; DOI=10.1095/biolreprod53.2.345;
RA Suzuki K., Sendai Y., Onuma T., Hoshi H., Hiroi M., Araki Y.;
RT "Molecular characterization of a hamster oviduct-specific glycoprotein.";
RL Biol. Reprod. 53:345-354(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Kidney;
RX PubMed=11013431;
RX DOI=10.1002/1098-2795(200011)57:3<238::aid-mrd5>3.0.co;2-r;
RA Merlen Y., Bleau G.;
RT "Organization of a gene coding for an oviduct-specific glycoprotein
RT (oviductin) in the hamster.";
RL Mol. Reprod. Dev. 57:238-246(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE, AND SEQUENCE REVISION.
RA Paquette Y.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-671.
RC TISSUE=Oviduct;
RX PubMed=8607967; DOI=10.1002/mrd.1080420404;
RA Paquette Y., Merlen Y., Malette B., Bleau G.;
RT "Allelic polymorphism in the hamster oviductin gene is due to a variable
RT number of mucin-like tandem repeats.";
RL Mol. Reprod. Dev. 42:388-396(1995).
RN [5]
RP PROTEIN SEQUENCE OF 22-39.
RX PubMed=8240241; DOI=10.1042/bj2950437;
RA Malette B., Bleau G.;
RT "Biochemical characterization of hamster oviductin as a sulphated zona
RT pellucida-binding glycoprotein.";
RL Biochem. J. 295:437-445(1993).
CC -!- FUNCTION: Binds to oocyte zona pellucida in vivo. May play a role in
CC the fertilization process and/or early embryonic development. Might act
CC as a protective secretion influencing the first steps of the
CC reproductive process necessary for the normal triggering of
CC fertilization and early embryonic development.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle.
CC Note=Secretory granules.
CC -!- TISSUE SPECIFICITY: Oviduct.
CC -!- PTM: Highly O-glycosylated and also N-glycosylated.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}.
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DR EMBL; D32218; BAA06977.1; -; mRNA.
DR EMBL; AF026552; AAC04276.2; -; Genomic_DNA.
DR EMBL; U15048; AAC53584.2; -; mRNA.
DR RefSeq; NP_001268266.1; NM_001281337.1.
DR AlphaFoldDB; Q60557; -.
DR SMR; Q60557; -.
DR STRING; 10036.XP_005088615.1; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR GeneID; 101833736; -.
DR CTD; 5016; -.
DR eggNOG; KOG2806; Eukaryota.
DR OrthoDB; 826687at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.10; -; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF54556; SSF54556; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond;
KW Fertilization; Glycoprotein; Reference proteome; Repeat; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:8240241"
FT CHAIN 22..671
FT /note="Oviduct-specific glycoprotein"
FT /id="PRO_0000011974"
FT DOMAIN 22..385
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REPEAT 490..504
FT /note="1"
FT REPEAT 505..519
FT /note="2"
FT REPEAT 520..534
FT /note="3"
FT REPEAT 535..549
FT /note="4"
FT REPEAT 550..564
FT /note="5"
FT REPEAT 565..579
FT /note="6"
FT REPEAT 580..594
FT /note="7"
FT REPEAT 595..609
FT /note="8"
FT REGION 490..609
FT /note="8 X 15 AA tandem repeats"
FT BINDING 71..72
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 98..101
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 142
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 211..214
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 355
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 556
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 586
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CONFLICT 26
FT /note="C -> A (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="H -> I (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="V -> A (in Ref. 2, 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 531..545
FT /note="Missing (in Ref. 2, 3 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 671 AA; 73250 MW; BB57E0E514EC1972 CRC64;
MGRLLLWVGL VLLMKPNDGT AYKLVCYFTN WAHSRPVPAS ILPRDLDPFL CTHLIFAFAS
MSNNQIVANN LQDEKILYPE FNKLKERNRA LKTLLSVGGW NFGTSRFTTM LSTLASREKF
IGSVVSFLRT HGFDGLDLFF LYPGLRGSPI NDRWNFLFLI EELQFAFEKE ALLTQRPRLL
LSAAVSGIPY IIQTSYDVHL LGRRLDFINV LSYDLHGSWE KSTGHNSPLF SLPEDPKSSA
FAMNYWRNLG APADKLLMGF PAYGRTFHLL RESKNGLQAA SMGPASPGKY TKQAGFLAYY
EVCSFIQRAE KHWIDHQYVP YAYKGKEWVG YDDAVSFSYK AMFVKKEHFG GAMVWTLDMD
DVRGTFCGNG PFPLVHILNE LLVRAEFNST PLPQFWFTLP VNSSGPGSES LPVTEELTTD
TVKILPPGGE AMATEVHRKY EKVTTIPNGG FVTPAGTTSP TTHAVALERN AMAPGAKTTT
SLDLLSETMT GMTVTVQTQT AGRETMTTVG NQSVTPGGET MTTVGNQSVT PGGETVTTVG
NQSVTPGGET MTTVGNQSVT PGGETVTIVG NKSVTPVGET VTIVGNKSVT PGGQTTATVG
SQSVTPPGMD TTLVYLQTMT LSEKGTSSKK AVVLEKVTVP PREISVMPNE QNTALNRENL
IAEVESYSQD G
