OST4_DICDI
ID OST4_DICDI Reviewed; 40 AA.
AC Q54V54;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4;
GN Name=ost4; ORFNames=DDB_G0280609;
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:Q99380}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000250|UniProtKB:Q99380}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type III membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the OST4 family. {ECO:0000305}.
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DR EMBL; AAFI02000037; EAL67106.1; -; Genomic_DNA.
DR RefSeq; XP_641077.1; XM_635985.1.
DR AlphaFoldDB; Q54V54; -.
DR SMR; Q54V54; -.
DR STRING; 44689.DDB0233179; -.
DR PaxDb; Q54V54; -.
DR EnsemblProtists; EAL67106; EAL67106; DDB_G0280609.
DR GeneID; 8622636; -.
DR KEGG; ddi:DDB_G0280609; -.
DR dictyBase; DDB_G0280609; ost4.
DR HOGENOM; CLU_186352_2_0_1; -.
DR InParanoid; Q54V54; -.
DR PhylomeDB; Q54V54; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q54V54; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISS:dictyBase.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:dictyBase.
DR InterPro; IPR018943; Oligosaccaryltransferase.
DR InterPro; IPR036330; Ost4p_sf.
DR Pfam; PF10215; Ost4; 1.
DR SUPFAM; SSF103464; SSF103464; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..40
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 4"
FT /id="PRO_0000328641"
FT TOPO_DOM 1..6
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 40 AA; 4447 MW; 0889D73FF622B113 CRC64;
MITDTQLTLL SNTLGATIFL LIVYYHYVAT KTVTAAKKDN