ID OVGP1_PAPAN Reviewed; 623 AA.
AC P36718;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 22-FEB-2023, entry version 106.
DE RecName: Full=Oviduct-specific glycoprotein;
DE AltName: Full=Estrogen-dependent oviduct protein;
DE AltName: Full=Oviductal glycoprotein;
DE AltName: Full=Oviductin;
DE Flags: Precursor;
GN Name=OVGP1; Synonyms=OGP;
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oviduct;
RX PubMed=9584944; DOI=10.1093/humupd/3.6.541;
RA Verhage H.G., Fazleabas A.T., Mavrogianis P.A., O'Day-Bowman M.B.,
RA Donnelly K.M., Arias E.B., Jaffe R.C.;
RT "The baboon oviduct: characteristics of an oestradiol-dependent oviduct-
RT specific glycoprotein.";
RL Hum. Reprod. Update 3:541-552(1997).
RN [2]
RP PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE.
RC TISSUE=Oviduct;
RX PubMed=1716345; DOI=10.1210/mend-5-3-356;
RA Donnelly K.M., Fazleabas A.T., Verhage H.G., Mavrogianis P.A., Jaffe R.C.;
RT "Cloning of a recombinant complementary DNA to a baboon (Papio anubis)
RT estradiol-dependent oviduct-specific glycoprotein.";
RL Mol. Endocrinol. 5:356-364(1991).
CC -!- FUNCTION: Binds to oocyte zona pellucida in vivo. May play a role in
CC the fertilization process and/or early embryonic development.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle.
CC Note=Secretory granules.
CC -!- TISSUE SPECIFICITY: Oviduct.
CC -!- DEVELOPMENTAL STAGE: At the time of ovulation.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}.
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DR EMBL; M59903; AAB39765.1; -; mRNA.
DR PIR; A37954; A37954.
DR RefSeq; NP_001106087.1; NM_001112617.1.
DR AlphaFoldDB; P36718; -.
DR SMR; P36718; -.
DR STRING; 9555.ENSPANP00000004617; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR GlyCosmos; P36718; 2 sites, No reported glycans.
DR GeneID; 100126696; -.
DR KEGG; panu:100126696; -.
DR CTD; 5016; -.
DR eggNOG; KOG2806; Eukaryota.
DR OrthoDB; 1752999at2759; -.
DR Proteomes; UP000028761; 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 CDD; cd02872; GH18_chitolectin_chitotriosidase; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 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 PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF385; OVIDUCT-SPECIFIC GLYCOPROTEIN; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Disulfide bond; Fertilization; Glycoprotein;
KW Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..623
FT /note="Oviduct-specific glycoprotein"
FT /id="PRO_0000011976"
FT DOMAIN 22..385
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REGION 539..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
SQ SEQUENCE 623 AA; 69292 MW; 9E21CE481FFF1268 CRC64;
MWKLLLWVGL VLVLKHHDGA AHKLVCYFTN WAHSRPGPAS ILPHDLDPFL CTHLIFAFAS
MNNNQIVAKD LQDEKILYPE FNKLKERNRE LKTLLSIGGW NFGTSRFTTM LSTFANREKF
IASVISLLRT HDFDGLDLFF LYPGLRGSPM HDRWTFLFLI EELLFAFRKE ALLTMRPRLL
LSAAVSGVPH IVQTSYDVRF LGRLLDFINV LSYDLHGSWE KFTGHNSPLF SLPEDPKSSA
YAMNYWRKLG APSEKLIMGI PTYGRTFRLL KASKNGLQAT AIGPASPGKY TKQAGFLAYF
EICSFVWGAK KHWIDYQYVP YANKGKEWVG YDDAISFSYK AWFIRREHFG GAMVWTLDMD
DVRGTFCGTG PFPLVYVMND ILVRAEFSST SLPQFWLSSA VNSSSTDPER LAVTKAWTTD
IKILPPGGEA GVTEIHGKCE NMTITPRVTI VTPTKETVSL GKHTVALGEK TEITGATTMT
SVGHQSMTPG EKALTPVGHQ SELPGKKTLT PVGHQSVTTG QKTLISVGYH SVTPGEKTLT
PVGHPSVTPV SHQSVSPGGM TMTPVHFQTE TLRQNTMAPR RKAVAHEKVT VPSRKISVTP
EGQTVPLRGE YLTSETGTHP QDG
//
