ID   OVGP1_PIG               Reviewed;         527 AA.
AC   Q28990;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=POSP-E3;
DE   Flags: Precursor;
GN   Name=OVGP1; Synonyms=OGP;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Yorkshire X Duroc X Hampshire; TISSUE=Oviduct;
RX   PubMed=8949888; DOI=10.1095/biolreprod55.6.1305;
RA   Buhi W.C., Alvarez I.M., Choi I., Cleaver B.D., Simmen F.A.;
RT   "Molecular cloning and characterization of an estrogen-dependent porcine
RT   oviductal secretory glycoprotein.";
RL   Biol. Reprod. 55:1305-1314(1996).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}.
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DR   EMBL; U43490; AAA85445.1; -; mRNA.
DR   RefSeq; NP_999235.1; NM_214070.1.
DR   AlphaFoldDB; Q28990; -.
DR   SMR; Q28990; -.
DR   STRING; 9823.ENSSSCP00000007244; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   PaxDb; Q28990; -.
DR   PRIDE; Q28990; -.
DR   GeneID; 397140; -.
DR   KEGG; ssc:397140; -.
DR   CTD; 5016; -.
DR   eggNOG; KOG2806; Eukaryota.
DR   InParanoid; Q28990; -.
DR   OrthoDB; 826687at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0008061; F:chitin binding; IBA:GO_Central.
DR   GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006032; P:chitin catabolic process; IBA:GO_Central.
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   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..527
FT                   /note="Oviduct-specific glycoprotein"
FT                   /id="PRO_0000011977"
FT   DOMAIN          22..385
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   REGION          433..527
FT                   /note="Disordered"
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        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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   527 AA;  58519 MW;  31B78F49CA2363A2 CRC64;
     MGKLLLWVGL VLVLKHHNGA AHKLVCYFAN WAFSRPGPAS ILPRDLDPFL CTHLVFAFAS
     MNDSQIVAKD ARDESIFYPE FNQLKERNEK LKTLLSIGGW NFGTSRFTTM LSTFTNREKF
     IRSAIGLLRT HGFDGLDLFF LYPGLRGSPR RDRWNFLFLL EELLLAFRRE AQLTMRPRLL
     LSAAVSADPH VIQKAYDVRL LGRLLDFINV LSYDLHGSWE KVTGHNSPLF SLSDDPKSSA
     YTMNYWRKLG APPEKLLMGF PTYGRTFRLL KASKNELGAE AVGPASPGKY TKQAGFLAYY
     EVCSFVQRAK KRWIDHQYVP YAYRGKEWVG YDDDISFSYK AFFIKKEHFG GAMVWTLDLD
     DVRGTFCGTG PFPLVYMLND LLLKAEVSST LSPGFGLSTT VNSSRTCPES LAVTKDLTTD
     LGILPLGGEA VATETHGRSD NMTVTPGGGL VAPTRPTLSF GKLTVAPEGK TESPGEKAMT
     PVGHPSVTPG DMSVPPVPIQ TGDRITPPRR QAVAPEKMTL PSGKRSD