OVGP1_MOUSE
ID OVGP1_MOUSE Reviewed; 721 AA.
AC Q62010;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 153.
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=Chit5, Ogp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR; TISSUE=Oviduct;
RX PubMed=7492680; DOI=10.1095/biolreprod53.2.285;
RA Sendai Y., Komiya H., Suzuki K., Onuma T., Kikuchi M., Hoshi H., Araki Y.;
RT "Molecular cloning and characterization of a mouse oviduct-specific
RT glycoprotein.";
RL Biol. Reprod. 53:285-294(1995).
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: Epithelial cells of the oviduct.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}.
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DR EMBL; D32137; BAA06863.1; -; mRNA.
DR CCDS; CCDS17716.1; -.
DR RefSeq; NP_031722.1; NM_007696.2.
DR AlphaFoldDB; Q62010; -.
DR SMR; Q62010; -.
DR STRING; 10090.ENSMUSP00000000573; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR GlyGen; Q62010; 3 sites.
DR iPTMnet; Q62010; -.
DR PhosphoSitePlus; Q62010; -.
DR MaxQB; Q62010; -.
DR PaxDb; Q62010; -.
DR PRIDE; Q62010; -.
DR ProteomicsDB; 294411; -.
DR Antibodypedia; 33809; 125 antibodies from 26 providers.
DR DNASU; 12659; -.
DR Ensembl; ENSMUST00000000573; ENSMUSP00000000573; ENSMUSG00000074340.
DR GeneID; 12659; -.
DR KEGG; mmu:12659; -.
DR UCSC; uc008qvq.1; mouse.
DR CTD; 5016; -.
DR MGI; MGI:106661; Ovgp1.
DR VEuPathDB; HostDB:ENSMUSG00000074340; -.
DR eggNOG; KOG2806; Eukaryota.
DR GeneTree; ENSGT00940000162223; -.
DR HOGENOM; CLU_002833_12_0_1; -.
DR InParanoid; Q62010; -.
DR OrthoDB; 826687at2759; -.
DR PhylomeDB; Q62010; -.
DR TreeFam; TF315610; -.
DR Reactome; R-MMU-2534343; Interaction With Cumulus Cells And The Zona Pellucida.
DR BioGRID-ORCS; 12659; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q62010; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q62010; protein.
DR Bgee; ENSMUSG00000074340; Expressed in superior surface of tongue and 214 other tissues.
DR ExpressionAtlas; Q62010; baseline and differential.
DR Genevisible; Q62010; MM.
DR GO; GO:0035805; C:egg coat; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0098595; C:perivitelline space; IDA:MGI.
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:2000360; P:negative regulation of binding of sperm to zona pellucida; IDA:MGI.
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; Repeat; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..721
FT /note="Oviduct-specific glycoprotein"
FT /id="PRO_0000011975"
FT DOMAIN 22..385
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REPEAT 486..492
FT /note="1"
FT REPEAT 493..499
FT /note="2"
FT REPEAT 500..506
FT /note="3"
FT REPEAT 507..513
FT /note="4"
FT REPEAT 514..520
FT /note="5"
FT REPEAT 521..527
FT /note="6"
FT REPEAT 528..534
FT /note="7"
FT REPEAT 535..541
FT /note="8"
FT REPEAT 542..548
FT /note="9"
FT REPEAT 549..555
FT /note="10"
FT REPEAT 556..562
FT /note="11"
FT REPEAT 563..569
FT /note="12"
FT REPEAT 570..576
FT /note="13"
FT REPEAT 577..583
FT /note="14"
FT REPEAT 584..590
FT /note="15"
FT REPEAT 591..597
FT /note="16"
FT REPEAT 598..604
FT /note="17"
FT REPEAT 605..611
FT /note="18"
FT REPEAT 612..618
FT /note="19"
FT REPEAT 619..625
FT /note="20"
FT REPEAT 626..632
FT /note="21"
FT REGION 444..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..632
FT /note="21 X 7 AA tandem repeats of S-K-[TAI]-[TI]-[TAP]-
FT [GED]-[IVM]"
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 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
SQ SEQUENCE 721 AA; 78808 MW; 37246C8F01665652 CRC64;
MGRLLLLAGL VLLMKHSDGT AYKLVCYFTN WAHSRPGPAS IMPHDLDPFL CTHLIFAFAS
MSNNQIVAKN LQDENVLYPE FNKLKERNRE LKTLLSIGGW NFGTSRFTAM LSTLANREKF
IDSVISFLRI HGFDGLDLFF LYPGLRGSPP HDRWNFLFLI EELQFAFERE ALLTQHPRLL
LSAAVSGIPS IIHTSYDALL LGRRLDFINV LSYDLHGSWE KFTGHNSPLF SLPEDSKSSA
YAMNYWRKLG TPADKLIMGF PTYGRNFYLL KESKNGLQTA SMGPASPGKY TKQAGFLAYY
EVCSFVQRAK KHWIDYQYVP YAFKGKEWLG YDDTISFSYK AMYVKREHFG GAMVWTLDMD
DVRGTFCGNG PFPLVHILNE LLVQTESNST PLPQFWFTSS VNASGPGSEN TALTEVLTTD
TIKILPPGGE AMTTEVHRRY ENMTTVPSDG SVTPGGTASP RKHAVTPENN TMAAEAKTMS
TLDFFSKTTT GVSKTTTGIS KTTTGVSKTT TGVSKATAGI SKTIPEISKA TAGVSKTTTG
VSKTTTGISK TITGVSKTTT GISKTTTGIS KTTTGVSKIT TGVSKTTTGI SKTTTGISQT
TTGISKTTTD ISKTTTGISK TTPGISKTTP GMTVIVQTQA NEAETTATMD HQSVTPTEMD
TTLFYLKTMT PSEKETSRKK TMVLEKATVS PREMSATPNG QSKTLKWASL ITEVETYSQD
G
