ID   OST48_CANLF             Reviewed;         445 AA.
AC   Q05052;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 116.
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   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Cocker spaniel; TISSUE=Kidney;
RX   PubMed=1429707; DOI=10.1016/s0021-9258(18)35889-7;
RA   Silberstein S., Kelleher D.J., Gilmore R.;
RT   "The 48-kDa subunit of the mammalian oligosaccharyltransferase complex is
RT   homologous to the essential yeast protein WBP1.";
RL   J. Biol. Chem. 267:23658-23663(1992).
RN   [2]
RP   IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX, FUNCTION OF
RP   THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX, AND SUBCELLULAR LOCATION.
RX   PubMed=12887896; DOI=10.1016/s1097-2765(03)00243-0;
RA   Kelleher D.J., Karaoglu D., Mandon E.C., Gilmore R.;
RT   "Oligosaccharyltransferase isoforms that contain different catalytic STT3
RT   subunits have distinct enzymatic properties.";
RL   Mol. Cell 12:101-111(2003).
RN   [3]
RP   IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE COMPLEX.
RX   PubMed=15835887; DOI=10.1021/bi047328f;
RA   Shibatani T., David L.L., McCormack A.L., Frueh K., Skach W.R.;
RT   "Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple
RT   subcomplexes that contain Sec61, TRAP, and two potential new subunits.";
RL   Biochemistry 44:5982-5992(2005).
RN   [4]
RP   IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE COMPLEX.
RX   PubMed=25135935; DOI=10.1083/jcb.201404083;
RA   Cherepanova N.A., Shrimal S., Gilmore R.;
RT   "Oxidoreductase activity is necessary for N-glycosylation of cysteine-
RT   proximal acceptor sites in glycoproteins.";
RL   J. Cell Biol. 206:525-539(2014).
RN   [5]
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS).
RX   PubMed=29519914; DOI=10.1126/science.aar7899;
RA   Braunger K., Pfeffer S., Shrimal S., Gilmore R., Berninghausen O.,
RA   Mandon E.C., Becker T., Foerster F., Beckmann R.;
RT   "Structural basis for coupling protein transport and N-glycosylation at the
RT   mammalian endoplasmic reticulum.";
RL   Science 360:215-219(2018).
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 (PubMed:12887896). Required for the assembly of both
CC       SST3A- and SS3B-containing OST complexes (By similarity).
CC       {ECO:0000250|UniProtKB:P39656, ECO:0000269|PubMed:12887896}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:P39656}.
CC   -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex. OST
CC       exists in two different complex forms which contain common core
CC       subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or
CC       STT3B as catalytic subunits, and form-specific accessory subunits
CC       (PubMed:12887896, PubMed:15835887, PubMed:25135935). STT3A complex
CC       assembly occurs through the formation of 3 subcomplexes. Subcomplex 1
CC       contains RPN1 and TMEM258, subcomplex 2 contains the STT3A-specific
CC       subunits STT3A, DC2/OSTC, and KCP2 as well as the core subunit OST4,
CC       and subcomplex 3 contains RPN2, DAD1, and OST48. The STT3A complex can
CC       form stable complexes with the Sec61 complex or with both the Sec61 and
CC       TRAP complexes (PubMed:15835887, PubMed:29519914). Interacts with
CC       SMIM22 (By similarity). {ECO:0000250|UniProtKB:P39656,
CC       ECO:0000269|PubMed:12887896, ECO:0000269|PubMed:15835887,
CC       ECO:0000269|PubMed:25135935, ECO:0000269|PubMed:29519914}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000269|PubMed:12887896}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q29381}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:29519914}.
CC   -!- SIMILARITY: Belongs to the DDOST 48 kDa subunit family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-7 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; M98392; AAA30880.1; -; mRNA.
DR   PIR; A45139; A45139.
DR   RefSeq; NP_001003321.1; NM_001003321.1.
DR   PDB; 6FTG; EM; 9.10 A; 7=-.
DR   PDB; 6FTI; EM; 4.20 A; 7=-.
DR   PDB; 6FTJ; EM; 4.70 A; 7=-.
DR   PDBsum; 6FTG; -.
DR   PDBsum; 6FTI; -.
DR   PDBsum; 6FTJ; -.
DR   AlphaFoldDB; Q05052; -.
DR   SMR; Q05052; -.
DR   CORUM; Q05052; -.
DR   IntAct; Q05052; 1.
DR   STRING; 9612.ENSCAFP00000022169; -.
DR   PaxDb; Q05052; -.
DR   PRIDE; Q05052; -.
DR   GeneID; 404012; -.
DR   KEGG; cfa:404012; -.
DR   CTD; 1650; -.
DR   eggNOG; KOG2754; Eukaryota.
DR   InParanoid; Q05052; -.
DR   OrthoDB; 975158at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; IDA:UniProtKB.
DR   GO; GO:0006486; P:protein glycosylation; IDA: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   3D-structure; Direct protein sequencing; Endoplasmic reticulum; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000250"
FT   CHAIN           33..445
FT                   /note="Dolichyl-diphosphooligosaccharide--protein
FT                   glycosyltransferase 48 kDa subunit"
FT                   /id="PRO_0000021955"
FT   TOPO_DOM        33..415
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:29519914"
FT   TRANSMEM        416..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        437..445
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:29519914"
SQ   SEQUENCE   445 AA;  49634 MW;  C4F3384B4CE4CF66 CRC64;
     MRRRRKMEAG AAARAWSLLW LLLPLLGPVC ASGPRTLVLL DNLNLRETHS LFFRSLKDRA
     FELTFKTADD PSLSLIKYGE FLYDNLIIFS PSVEDFGGNI NVETISTFID GGGSVLVAAS
     SDIGDPLREL GSECGIEFDE EKTAVIDHHN YDVSDLGQHT LIVADPENLL KAPTIVGRSS
     LNPILFRGVG MVADPDNPLV LDILTGSSTS YSFFPDKPIT QYPHAVGKNT LLIAGLQARN
     NARVVFSGSL DFFSDAFFNS AVQKAAPGSQ RYSQTGNYEL AVALSRWVFK EEGVLRVGPV
     SHHRVGETAP PNAYTVTDLV EYSIVIEQLS NGRWVPFDGD DIQLEFVRID PFVRTFLKKK
     GGKYSVQFKL PDVYGVFQFK VDYNRLGYTH LHSSTQVSVR PLQHTQYERF IPSAYPYYAS
     AFSMMLGLFI FSTVFLHMKE KEKSD