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   13-SEP-2023, entry version 176.
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   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   GlyCosmos; Q12889; 5 sites, No reported glycans.
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   ProteomicsDB; 59005; -.
DR   Antibodypedia; 33809; 141 antibodies from 26 providers.
DR   DNASU; 5016; -.
DR   Ensembl; ENST00000369732.4; ENSP00000358747.3; ENSG00000085465.13.
DR   KEGG; hsa:5016; -.
DR   MANE-Select; ENST00000369732.4; ENSP00000358747.3; NM_002557.4; NP_002548.3.
DR   UCSC; uc001eba.4; human.
DR   AGR; HGNC:8524; -.
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; VKREHFG; -.
DR   OrthoDB; 1752999at2759; -.
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; 42 hits in 1150 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   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..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
//