OST3_DICDI
ID OST3_DICDI Reviewed; 351 AA.
AC Q54N33;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3;
DE Flags: Precursor;
GN Name=ost3; ORFNames=DDB_G0285537;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that
CC catalyzes the initial transfer of a defined glycan
CC (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-
CC pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr
CC consensus motif in nascent polypeptide chains, the first step in
CC protein N-glycosylation. N-glycosylation occurs cotranslationally and
CC the complex associates with the Sec61 complex at the channel-forming
CC translocon complex that mediates protein translocation across the
CC endoplasmic reticulum (ER). All subunits are required for a maximal
CC enzyme activity. {ECO:0000250|UniProtKB:P48439}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000250|UniProtKB:P48439}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the OST3/OST6 family. {ECO:0000305}.
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DR EMBL; AAFI02000079; EAL64606.1; -; Genomic_DNA.
DR RefSeq; XP_638110.1; XM_633018.1.
DR AlphaFoldDB; Q54N33; -.
DR SMR; Q54N33; -.
DR STRING; 44689.DDB0233177; -.
DR TCDB; 1.A.76.1.4; the magnesium transporter1 (magt1) family.
DR PaxDb; Q54N33; -.
DR EnsemblProtists; EAL64606; EAL64606; DDB_G0285537.
DR GeneID; 8625158; -.
DR KEGG; ddi:DDB_G0285537; -.
DR dictyBase; DDB_G0285537; ost3.
DR eggNOG; KOG2603; Eukaryota.
DR HOGENOM; CLU_790909_0_0_1; -.
DR InParanoid; Q54N33; -.
DR OMA; MAISYIH; -.
DR PhylomeDB; Q54N33; -.
DR Reactome; R-DDI-5223345; Miscellaneous transport and binding events.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR PRO; PR:Q54N33; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISS:dictyBase.
DR GO; GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; ISS:dictyBase.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:dictyBase.
DR InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6.
DR PANTHER; PTHR12692; PTHR12692; 1.
DR Pfam; PF04756; OST3_OST6; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Endoplasmic reticulum; Membrane; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..351
FT /note="Probable dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 3"
FT /id="PRO_0000328632"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 49..185
FT /note="Thioredoxin"
FT DISULFID 93..96
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 351 AA; 40264 MW; E1EF3CD6D1C3F01A CRC64;
MMKSSKVSTI LLLLFVVIIG SFCLTYGAPS TTNQKPLTSS EKKLLNDLYD RAKKAGGVVE
FKSNLDSKKF VTAQNRPYDL LALFTSSNPK YGCSGCVQLK NQIESFSLSY EPYLNSAGFL
EKPIFIVILE VDYNMEVFQT IGLNTIPHLL FIPSGSKPIT QKGYAYTGFE QTSSQSISDF
IYSHSKIRIE PVKTFYEKYS VQILSFVVFL ASVRFLITAY RKRKSPMFWY FLTILLFACV
IMGIFYDFIH KPNFYEFDHR QQTYNYFSRG SRSQTVSEGM IMGVSTIAIT LIFVFLSDIL
PNYTNFSSKS KGLLFFMGMS SIIVLLFFQS LAFQIKYYRP LFFIPSVTYH Y
