OST1_DICDI
ID OST1_DICDI Reviewed; 460 AA.
AC Q54C27;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1;
DE AltName: Full=Oligosaccharyl transferase subunit alpha;
DE AltName: Full=Ribophorin I;
DE Short=RPN-I;
DE AltName: Full=Ribophorin-1;
DE Flags: Precursor;
GN Name=ost1; Synonyms=rpn1; ORFNames=DDB_G0293224;
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).
RN [2]
RP INDUCTION.
RX PubMed=16469056; DOI=10.1111/j.1462-5822.2005.00633.x;
RA Farbrother P., Wagner C., Na J., Tunggal B., Morio T., Urushihara H.,
RA Tanaka Y., Schleicher M., Steinert M., Eichinger L.;
RT "Dictyostelium transcriptional host cell response upon infection with
RT Legionella.";
RL Cell. Microbiol. 8:438-456(2006).
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:P41543}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000250|UniProtKB:P41543}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}.
CC -!- INDUCTION: Upon infection by L.pneumophila.
CC {ECO:0000269|PubMed:16469056}.
CC -!- SIMILARITY: Belongs to the OST1 family. {ECO:0000305}.
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DR EMBL; AAFI02000200; EAL60811.1; -; Genomic_DNA.
DR RefSeq; XP_629239.1; XM_629237.1.
DR AlphaFoldDB; Q54C27; -.
DR SMR; Q54C27; -.
DR STRING; 44689.DDB0233146; -.
DR PaxDb; Q54C27; -.
DR EnsemblProtists; EAL60811; EAL60811; DDB_G0293224.
DR GeneID; 8629121; -.
DR KEGG; ddi:DDB_G0293224; -.
DR dictyBase; DDB_G0293224; ost1.
DR eggNOG; KOG2291; Eukaryota.
DR HOGENOM; CLU_031381_0_1_1; -.
DR InParanoid; Q54C27; -.
DR OMA; KTYMDTL; -.
DR PhylomeDB; Q54C27; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q54C27; -.
DR Proteomes; UP000002195; Chromosome 6.
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 GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
DR InterPro; IPR007676; Ribophorin_I.
DR PANTHER; PTHR21049; PTHR21049; 1.
DR Pfam; PF04597; Ribophorin_I; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..460
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 1"
FT /id="PRO_0000327398"
FT TOPO_DOM 25..425
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..460
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 460 AA; 52411 MW; 6CDD99F08E524A42 CRC64;
MKVLNNLLLF VFLIFLVGSN VVNSTSQTWI NQDVQRSIDV TTHLSKESIS IKAKSLTDKN
DIYQISFNSK YHVSIQALDS QNNELKVYLS PNSINIKEGF KTYNIELKNK VKKDEIVQLK
VKVTSMIEQM IPYPSEIKQG QTQLVLYLNN HYFTSPYKTE TQKTTVKLAS SKVESYSEEQ
PTSLKGMTVT YGPYSAIEAF SVSPMRIHYE NGSPFFVLTN LLKEYEVSHW GNLAVETHYQ
LENKGAHLVG AFSRLDYQRN PSVNPNQIAE VNEAVPLSAT DFYYRDSIGN ISTSSYQYLA
NRINFKIQPR FPLMGGWKNT FYTGYNLPIE KFLSVDTLTG QYHLNVTFGV GIDNVYVENH
ILKVVLPEGA TDIKVHAPFA FTQSEENRKT YLDTIGRPVV VINIKDTASE NYRYIQVTYN
LSSLSIFHEP LLVIGAVFTL CIFIILYSRF DLSISKSKQI
