OVGP1_SHEEP
ID OVGP1_SHEEP Reviewed; 539 AA.
AC Q28542; Q28543;
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=Estrus-associated oviductal glycoprotein;
DE Short=OEGP;
DE AltName: Full=Oviductal glycoprotein;
DE AltName: Full=Oviductin;
DE Flags: Precursor;
GN Name=OVGP1; Synonyms=OGP;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 22-39.
RC TISSUE=Oviduct;
RX PubMed=7750470; DOI=10.1210/endo.136.6.7750470;
RA Desouza M.M., Murray M.K.;
RT "An estrogen-dependent secretory protein, which shares identity with
RT chitinases, is expressed in a temporally and regionally specific manner in
RT the sheep oviduct at the time of fertilization and embryo development.";
RL Endocrinology 136:2485-2496(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-539.
RC STRAIN=Merino; TISSUE=Oviduct;
RX PubMed=8726871; DOI=10.1071/rd9960305;
RA Marshall J.T.A., Nancarrow C.D., Brownlee A.G.;
RT "Cloning and sequencing of a cDNA encoding an ovine oestrus-associated
RT oviducal protein.";
RL Reprod. Fertil. Dev. 8:305-310(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 -!- DEVELOPMENTAL STAGE: Levels are highest in the fimbria and ampulla at
CC estrus and on day 1 of pregnancy, when gamete transport and
CC fertilization occurs in the E2-dominated fallopian tube. Levels decline
CC significantly on day 2 and undergo a further significant reduction on
CC day 3 of pregnancy coincident with transport of the embryo from the
CC oviduct to the uterus, a reproductive stage associated with rising
CC progesterone levels.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}.
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DR EMBL; U16719; AAC48471.1; -; mRNA.
DR EMBL; U17988; AAB01052.1; -; mRNA.
DR PIR; I46470; I46470.
DR RefSeq; NP_001009779.1; NM_001009779.1.
DR AlphaFoldDB; Q28542; -.
DR SMR; Q28542; -.
DR STRING; 9940.ENSOARP00000021050; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR GeneID; 443344; -.
DR KEGG; oas:443344; -.
DR CTD; 5016; -.
DR eggNOG; KOG2806; Eukaryota.
DR OrthoDB; 826687at2759; -.
DR Proteomes; UP000002356; 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; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..539
FT /note="Oviduct-specific glycoprotein"
FT /id="PRO_0000011978"
FT DOMAIN 22..385
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REGION 433..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..461
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 DISULFID 26..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CONFLICT 13
FT /note="M -> V (in Ref. 2; AAB01052)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="K -> N (in Ref. 2; AAB01052)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="A -> V (in Ref. 2; AAB01052)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="A -> V (in Ref. 2; AAB01052)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="R -> H (in Ref. 2; AAB01052)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="I -> T (in Ref. 2; AAB01052)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 539 AA; 59536 MW; F35000269987C193 CRC64;
MGKLLLWVGL LLMLKHHDGA AHKLVCYFTN WAFSRPGSAS ILPRDLDPFL CTHLVFAFAS
MNNNQIVPKD PLDEKILYPE FNKLKERNRG LKTLLSVGGW NFGTSRFTKM LSTFSNRERF
VKSVIALLRT HGFDGLDLFF LYPGLRGSPA RDRWTFVFLL EELLQAFKNE AQLTMRPRLL
LSAAVSGDPH VIQKAYDARL LGRLLDFISV LSYDLHGSWE KVTGHNSPLF SLPGDPKSSA
YAMSYWRQLG VPPEKLLMGL PTYGRTFHLL RASQNELGAG AAGPASPGKY TKQAGFLAYY
EVCSFVQRAK KRWINDQYVP YAFKGKEWVG YDDAISFGYK AFFIKREHFG GAMVWTLDLD
DFRGNFCGTG PFPLAHTLNN LLVNDEFSST PSPKFWFSTA VNSSRIGPEM PTMTRDLTTG
LGILPLGGEA VATETHRKSA TMTTTPRGET ATPTRTPLSS GRRTAAPEGK TESPGEKPLT
SVGRLAVSPG GIAVGPVHLQ IGQKVTPPGR KAGVPEKVTI PSGKMTVTPD GRAETLERL
