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OVGP1_BOVIN
ID   OVGP1_BOVIN             Reviewed;         537 AA.
AC   Q28042;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 115.
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; Fragment;
GN   Name=OVGP1; Synonyms=OGP;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 19-47.
RC   TISSUE=Oviduct;
RX   PubMed=8199272; DOI=10.1095/biolreprod50.4.927;
RA   Sendai Y., Abe H., Kikuchi M., Satoh T., Hoshi H.;
RT   "Purification and molecular cloning of bovine oviduct-specific
RT   glycoprotein.";
RL   Biol. Reprod. 50:927-934(1994).
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; D16639; BAA04065.1; -; mRNA.
DR   PIR; S57197; S57197.
DR   AlphaFoldDB; Q28042; -.
DR   SMR; Q28042; -.
DR   STRING; 9913.ENSBTAP00000046210; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   PaxDb; Q28042; -.
DR   PRIDE; Q28042; -.
DR   eggNOG; KOG2806; Eukaryota.
DR   InParanoid; Q28042; -.
DR   OrthoDB; 826687at2759; -.
DR   Proteomes; UP000009136; 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   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond;
KW   Fertilization; Glycoprotein; Reference proteome; Signal.
FT   SIGNAL          <1..18
FT                   /evidence="ECO:0000269|PubMed:8199272"
FT   CHAIN           19..537
FT                   /note="Oviduct-specific glycoprotein"
FT                   /id="PRO_0000011972"
FT   DOMAIN          19..382
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   REGION          446..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          498..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         68..69
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         95..98
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         139
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         208..211
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         352
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   CARBOHYD        399
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        23..48
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   NON_TER         1
SQ   SEQUENCE   537 AA;  59618 MW;  CFDCEE6F0212D791 CRC64;
     LLLCVGLLLV LKHHDGAAHK LVCYFTNWAF SRPGPASILP RDLDPFLCTH LVFAFASMSN
     NQIVPKDPQD EKILYPEFNK LKERNRGLKT LLSIGGWNFG TVRFTTMLST FSNRERFVSS
     VIALLRTHGF DGLDLFFLYP GLRGSPARDR WTFVFLLEEL LQAFKNEAQL TMRPRLLLSA
     AVSGDPHVVQ KAYEARLLGR LLDFISVLSY DLHGSWEKVT GHNSPLFSLP GDPKSSAYAM
     NYWRQLGVPP EKLLMGLPTY GRTFHLLKAS QNELRAQAVG PASPGKYTKQ AGFLAYYEIC
     CFVRRAKKRW INDQYVPYAF KGKEWVGYDD AISFGYKAFF IKREHFGGAM VWTLDLDDFR
     GYFCGTGPFP LVHTLNNLLV NDEFSSTPSP KFWFSTAVNS SRIGPEMPTM TRDLTTGLGI
     LPPGGEAVAT ETHRKSETMT ITPKGEIATP TRTPLSFGRH TAAPEGKTES PGEKPLTTVG
     HLAVSPGGIA VGPVRLQTGQ KVTPPGRKAG VPEKVTTPSG KMTVTPDGRA ETLERRL
 
 
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