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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
 
 
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