OST48_RAT
ID OST48_RAT Reviewed; 441 AA.
AC Q641Y0;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit {ECO:0000305};
DE Short=DDOST 48 kDa subunit;
DE Short=Oligosaccharyl transferase 48 kDa subunit;
DE Flags: Precursor;
GN Name=Ddost {ECO:0000312|RGD:1308970};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
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).
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 (By similarity). N-glycosylation occurs
CC cotranslationally and the complex associates with the Sec61 complex at
CC the channel-forming translocon complex that mediates protein
CC translocation across the endoplasmic reticulum (ER). All subunits are
CC required for a maximal enzyme activity (By similarity). Required for
CC the assembly of both SST3A- and SS3B-containing OST complexes (By
CC similarity). {ECO:0000250|UniProtKB:P39656,
CC ECO:0000250|UniProtKB:Q05052}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P39656}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex (By
CC similarity). OST exists in two different complex forms which contain
CC common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either
CC STT3A or STT3B as catalytic subunits, and form-specific accessory
CC subunits (By similarity). STT3A complex assembly occurs through the
CC formation of 3 subcomplexes. Subcomplex 1 contains RPN1 and TMEM258,
CC subcomplex 2 contains the STT3A-specific subunits STT3A, DC2/OSTC, and
CC KCP2 as well as the core subunit OST4, and subcomplex 3 contains RPN2,
CC DAD1, and OST48. The STT3A complex can form stable complexes with the
CC Sec61 complex or with both the Sec61 and TRAP complexes. Interacts with
CC SMIM22 (By similarity). {ECO:0000250|UniProtKB:P39656,
CC ECO:0000250|UniProtKB:Q05052}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q29381}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q29381}.
CC -!- SIMILARITY: Belongs to the DDOST 48 kDa subunit family. {ECO:0000305}.
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DR EMBL; BC082075; AAH82075.1; -; mRNA.
DR RefSeq; NP_001012104.1; NM_001012104.1.
DR AlphaFoldDB; Q641Y0; -.
DR SMR; Q641Y0; -.
DR BioGRID; 260501; 1.
DR IntAct; Q641Y0; 1.
DR STRING; 10116.ENSRNOP00000062365; -.
DR iPTMnet; Q641Y0; -.
DR PhosphoSitePlus; Q641Y0; -.
DR SwissPalm; Q641Y0; -.
DR jPOST; Q641Y0; -.
DR PaxDb; Q641Y0; -.
DR PRIDE; Q641Y0; -.
DR GeneID; 313648; -.
DR KEGG; rno:313648; -.
DR UCSC; RGD:1308970; rat.
DR CTD; 1650; -.
DR RGD; 1308970; Ddost.
DR VEuPathDB; HostDB:ENSRNOG00000015079; -.
DR eggNOG; KOG2754; Eukaryota.
DR HOGENOM; CLU_031804_0_0_1; -.
DR InParanoid; Q641Y0; -.
DR OMA; YQFKVDY; -.
DR OrthoDB; 975158at2759; -.
DR PhylomeDB; Q641Y0; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q641Y0; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000015079; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q641Y0; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:RGD.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008047; F:enzyme activator activity; ISO:RGD.
DR GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISO:RGD.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
DR GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
DR GO; GO:0034097; P:response to cytokine; ISO:RGD.
DR GO; GO:0042110; P:T cell activation; ISO:RGD.
DR InterPro; IPR005013; DDOST_48_kDa_subunit.
DR PANTHER; PTHR10830; PTHR10830; 1.
DR Pfam; PF03345; DDOST_48kD; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000250"
FT CHAIN 29..441
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase 48 kDa subunit"
FT /id="PRO_0000357447"
FT TOPO_DOM 29..412
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 441 AA; 48896 MW; DB057B01AA5CB6AD CRC64;
MKMVPRLAVR AWPLCGLLLA ALGCVCASGP RTLVLLDNLN VRDTHSLFFR SLKDRGFELT
FKTADDPSLS LIKYGEFLYD NLIIFSPSVE DFGGNINVET ISAFIDGGGS VLVAASSDIG
DPLRELGSEC GIEFDEEKTA VIDHHNYDVS DLGQHTLIVA DTENLLKAPT IVGKSSLNPI
LFRGVGMVAD PDNPLVLDIL TGSSTSYSFF PDKPITQYPH AVGRNTLLIA GLQARNNARV
IFSGSLDFFS DAFFNSAVQK AAPGAQRYSQ TGNYELAVAL SRWVFKEEGV LRVGPVSHHR
VGETAPPNAY TVTDLVEYSI VIEQLSNGKW VPFDGDDIQL EFVRIDPFVR TFLKRKGGKY
SVQFKLPDVY GVFQFKVDYN RLGYTHLYSS TQVSVRPLQH TQYERFIPSA YPYYASAFSM
MAGLFLFSVV FLHMKEKEKS D