OST48_PIG
ID OST48_PIG Reviewed; 439 AA.
AC Q29381; Q9GL02;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit {ECO:0000250|UniProtKB:P39656};
DE Short=DDOST 48 kDa subunit;
DE Short=Oligosaccharyl transferase 48 kDa subunit;
DE Flags: Precursor;
GN Name=DDOST {ECO:0000250|UniProtKB:P39656}; Synonyms=OST48;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-43, MUTAGENESIS OF
RP LYS-437, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=11443278; DOI=10.1023/a:1010980524785;
RA Hardt B., Aparicio R., Bause E.;
RT "The oligosaccharyltransferase complex from pig liver: cDNA cloning,
RT expression and functional characterisation.";
RL Glycoconj. J. 17:767-779(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 27-129.
RC TISSUE=Small intestine;
RX PubMed=8672129; DOI=10.1007/s003359900153;
RA Winteroe A.K., Fredholm M., Davies W.;
RT "Evaluation and characterization of a porcine small intestine cDNA library:
RT analysis of 839 clones.";
RL Mamm. Genome 7:509-517(1996).
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 (PubMed:11443278). 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, ECO:0000269|PubMed:11443278}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:11443278}.
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:0000269|PubMed:11443278}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:11443278}.
CC -!- SIMILARITY: Belongs to the DDOST 48 kDa subunit family. {ECO:0000305}.
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DR EMBL; AJ293581; CAC10570.1; -; mRNA.
DR EMBL; F14593; CAA23144.1; -; mRNA.
DR RefSeq; NP_999353.1; NM_214188.1.
DR AlphaFoldDB; Q29381; -.
DR SMR; Q29381; -.
DR STRING; 9823.ENSSSCP00000003805; -.
DR PaxDb; Q29381; -.
DR PeptideAtlas; Q29381; -.
DR PRIDE; Q29381; -.
DR GeneID; 397385; -.
DR KEGG; ssc:397385; -.
DR CTD; 1650; -.
DR eggNOG; KOG2754; Eukaryota.
DR InParanoid; Q29381; -.
DR OrthoDB; 975158at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
DR InterPro; IPR005013; DDOST_48_kDa_subunit.
DR PANTHER; PTHR10830; PTHR10830; 1.
DR Pfam; PF03345; DDOST_48kD; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:11443278"
FT CHAIN 26..439
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase 48 kDa subunit"
FT /id="PRO_0000058095"
FT TOPO_DOM 27..410
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 437
FT /note="K->L: Abolishes ER localization resulting in plasma
FT membrane localization."
FT /evidence="ECO:0000269|PubMed:11443278"
SQ SEQUENCE 439 AA; 48863 MW; 480F8196B14F8C72 CRC64;
MELGAAARAW SLLWLLLPLL GLVGASGPRT LVLLDNLNLR ETHSLFFRSL KDRGFVLTFK
TADDPSLSLI KYGEFLYDNL IVFSPSVEDF GGNINVETIS TFIDGGGSVL VAASSDIGDP
LRELGSECGI EFDEEKTAVI DHHNYDVSDL AQHTLIVADT ENLLKAPTIV GKSSLNPILF
RGVGMVADPD NPLVLDILTG SSTSYSFFPD KPITQYPHAV GKNTLLIAGL QARNNARVIF
SGSLDFFSDA FFNSAVQKAT PGSQRYPQTG NYELAVALSR WVFKEEGVLR VGPVSHHRVG
EKAPPNAYTV TDLVEYSIVI EQLSEGRWVP FDGDDIQLEF VRIDPFVRTF LKRKGGKYSV
QFKFPDVYGV FQFKVDYNRL GYTHLYSSTQ VSVRPLQHTQ YERFIPSAYP YYASAFSMMV
GLFIFSVVFL HMKEKEKSD
