OVGP1_HUMAN
ID OVGP1_HUMAN Reviewed; 678 AA.
AC Q12889; A0AV19; B9EGE1; Q15841;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Oviduct-specific glycoprotein;
DE AltName: Full=Estrogen-dependent oviduct protein;
DE AltName: Full=Mucin-9;
DE AltName: Full=Oviductal glycoprotein;
DE AltName: Full=Oviductin;
DE Flags: Precursor;
GN Name=OVGP1; Synonyms=MUC9, OGP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oviduct;
RX PubMed=7819450; DOI=10.1095/biolreprod51.4.685;
RA Arias E.B., Verhage H.G., Jaffe R.C.;
RT "Complementary deoxyribonucleic acid cloning and molecular characterization
RT of an estrogen-dependent human oviductal glycoprotein.";
RL Biol. Reprod. 51:685-694(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-477; HIS-514 AND
RP GLN-676.
RA Jaffe R.C.;
RT "Human oviductal glycoprotein gene.";
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-662.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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; U09550; AAA86946.1; -; mRNA.
DR EMBL; U58010; AAB04126.1; -; Genomic_DNA.
DR EMBL; U58001; AAB04126.1; JOINED; Genomic_DNA.
DR EMBL; U58002; AAB04126.1; JOINED; Genomic_DNA.
DR EMBL; U58003; AAB04126.1; JOINED; Genomic_DNA.
DR EMBL; U58004; AAB04126.1; JOINED; Genomic_DNA.
DR EMBL; U58005; AAB04126.1; JOINED; Genomic_DNA.
DR EMBL; U58006; AAB04126.1; JOINED; Genomic_DNA.
DR EMBL; U58007; AAB04126.1; JOINED; Genomic_DNA.
DR EMBL; U58008; AAB04126.1; JOINED; Genomic_DNA.
DR EMBL; U58009; AAB04126.1; JOINED; Genomic_DNA.
DR EMBL; AL390195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC126177; AAI26178.1; -; mRNA.
DR EMBL; BC136406; AAI36407.1; -; mRNA.
DR CCDS; CCDS834.1; -.
DR RefSeq; NP_002548.3; NM_002557.3.
DR AlphaFoldDB; Q12889; -.
DR SMR; Q12889; -.
DR BioGRID; 111056; 4.
DR IntAct; Q12889; 2.
DR STRING; 9606.ENSP00000358747; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR GlyGen; Q12889; 6 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q12889; -.
DR PhosphoSitePlus; Q12889; -.
DR BioMuta; OVGP1; -.
DR DMDM; 2493676; -.
DR CPTAC; CPTAC-1322; -.
DR CPTAC; CPTAC-1526; -.
DR CPTAC; CPTAC-1527; -.
DR MassIVE; Q12889; -.
DR PaxDb; Q12889; -.
DR PeptideAtlas; Q12889; -.
DR PRIDE; Q12889; -.
DR ProteomicsDB; 59005; -.
DR Antibodypedia; 33809; 125 antibodies from 26 providers.
DR DNASU; 5016; -.
DR Ensembl; ENST00000369732.4; ENSP00000358747.3; ENSG00000085465.13.
DR GeneID; 5016; -.
DR KEGG; hsa:5016; -.
DR MANE-Select; ENST00000369732.4; ENSP00000358747.3; NM_002557.4; NP_002548.3.
DR UCSC; uc001eba.4; human.
DR CTD; 5016; -.
DR DisGeNET; 5016; -.
DR GeneCards; OVGP1; -.
DR HGNC; HGNC:8524; OVGP1.
DR HPA; ENSG00000085465; Tissue enriched (fallopian).
DR MIM; 603578; gene.
DR neXtProt; NX_Q12889; -.
DR OpenTargets; ENSG00000085465; -.
DR PharmGKB; PA32852; -.
DR VEuPathDB; HostDB:ENSG00000085465; -.
DR eggNOG; KOG2806; Eukaryota.
DR GeneTree; ENSGT00940000162223; -.
DR HOGENOM; CLU_002833_12_0_1; -.
DR InParanoid; Q12889; -.
DR OMA; RARKHWI; -.
DR OrthoDB; 826687at2759; -.
DR PhylomeDB; Q12889; -.
DR TreeFam; TF315610; -.
DR PathwayCommons; Q12889; -.
DR Reactome; R-HSA-2534343; Interaction With Cumulus Cells And The Zona Pellucida.
DR SignaLink; Q12889; -.
DR BioGRID-ORCS; 5016; 41 hits in 1072 CRISPR screens.
DR ChiTaRS; OVGP1; human.
DR GeneWiki; OVGP1; -.
DR GenomeRNAi; 5016; -.
DR Pharos; Q12889; Tbio.
DR PRO; PR:Q12889; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q12889; protein.
DR Bgee; ENSG00000085465; Expressed in right uterine tube and 154 other tissues.
DR Genevisible; Q12889; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0035805; C:egg coat; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0098595; C:perivitelline space; IEA:Ensembl.
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:0007565; P:female pregnancy; TAS:ProtInc.
DR GO; GO:2000360; P:negative regulation of binding of sperm to zona pellucida; IEA:Ensembl.
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..678
FT /note="Oviduct-specific glycoprotein"
FT /id="PRO_0000011973"
FT DOMAIN 22..385
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REGION 524..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..666
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 CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 596
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 648
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT VARIANT 332
FT /note="D -> E (in dbSNP:rs17027633)"
FT /id="VAR_049199"
FT VARIANT 477
FT /note="M -> T (in dbSNP:rs2485319)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_024459"
FT VARIANT 479
FT /note="M -> V (in dbSNP:rs3767607)"
FT /id="VAR_049200"
FT VARIANT 514
FT /note="Y -> H (in dbSNP:rs1126656)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_049201"
FT VARIANT 526
FT /note="P -> S (in dbSNP:rs12096782)"
FT /id="VAR_061190"
FT VARIANT 536
FT /note="S -> G (in dbSNP:rs3767609)"
FT /id="VAR_049202"
FT VARIANT 604
FT /note="H -> Q (in dbSNP:rs10067)"
FT /id="VAR_024460"
FT VARIANT 662
FT /note="L -> H (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035752"
FT VARIANT 676
FT /note="E -> Q (in dbSNP:rs7825)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_016109"
FT CONFLICT 511
FT /note="S -> P (in Ref. 2; AAB04126)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 678 AA; 75421 MW; 245F2CEDCE92768B CRC64;
MWKLLLWVGL VLVLKHHDGA AHKLVCYFTN WAHSRPGPAS ILPHDLDPFL CTHLIFAFAS
MNNNQIVAKD LQDEKILYPE FNKLKERNRE LKTLLSIGGW NFGTSRFTTM LSTFANREKF
IASVISLLRT HDFDGLDLFF LYPGLRGSPM HDRWTFLFLI EELLFAFRKE ALLTMRPRLL
LSAAVSGVPH IVQTSYDVRF LGRLLDFINV LSYDLHGSWE RFTGHNSPLF SLPEDPKSSA
YAMNYWRKLG APSEKLIMGI PTYGRTFRLL KASKNGLQAR AIGPASPGKY TKQEGFLAYF
EICSFVWGAK KHWIDYQYVP YANKGKEWVG YDNAISFSYK AWFIRREHFG GAMVWTLDMD
DVRGTFCGTG PFPLVYVLND ILVRAEFSST SLPQFWLSSA VNSSSTDPER LAVTTAWTTD
SKILPPGGEA GVTEIHGKCE NMTITPRGTT VTPTKETVSL GKHTVALGEK TEITGAMTMT
SVGHQSMTPG EKALTPVGHQ SVTTGQKTLT SVGYQSVTPG EKTLTPVGHQ SVTPVSHQSV
SPGGTTMTPV HFQTETLRQN TVAPRRKAVA REKVTVPSRN ISVTPEGQTM PLRGENLTSE
VGTHPRMGNL GLQMEAENRM MLSSSPVIQL PEQTPLAFDN RFVPIYGNHS SVNSVTPQTS
PLSLKKEIPE NSAVDEEA
