OSTC_CANLF
ID OSTC_CANLF Reviewed; 149 AA.
AC P86218;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Oligosaccharyltransferase complex subunit OSTC {ECO:0000250|UniProtKB:Q9NRP0};
GN Name=OSTC {ECO:0000250|UniProtKB:Q9NRP0};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-107.
RC STRAIN=Cocker spaniel {ECO:0000269|PubMed:12692157};
RC TISSUE=Kidney {ECO:0000269|PubMed:12692157};
RX PubMed=12692157; DOI=10.1093/jhered/esg003;
RA Palmer L.E., O'Shaughnessy A.L., Preston R.R., Santos L., Balija V.S.,
RA Nascimento L.U., Zutavern T.L., Henthorn P.S., Hannon G.J., McCombie W.R.;
RT "A survey of canine expressed sequence tags and a display of their
RT annotations through a flexible web-based interface.";
RL J. Hered. 94:15-22(2003).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 70-149.
RC STRAIN=Beagle; TISSUE=Heart atrium;
RA Staten N.R.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
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 STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) OF 30-149.
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: Specific component of the STT3A-containing form of the
CC oligosaccharyl transferase (OST) complex that catalyzes the initial
CC transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from
CC the lipid carrier dolichol-pyrophosphate to an asparagine residue
CC within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains,
CC the first step in protein N-glycosylation. 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. May be involved in N-
CC glycosylation of APP (amyloid-beta precursor protein). Can modulate
CC gamma-secretase cleavage of APP by enhancing endoprotelysis of PSEN1.
CC {ECO:0000250|UniProtKB:Q9NRP0}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q9NRP0}.
CC -!- SUBUNIT: Specific component of the STT3A-containing form of the
CC oligosaccharyltransferase (OST) complex. OST exists in two different
CC complex forms which contain common core subunits RPN1, RPN2, OST48,
CC OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic subunits,
CC and form-specific accessory subunits (PubMed:15835887). 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 PSEN1
CC and NCSTN; indicative for an association with the gamma-secretase
CC complex (By similarity). {ECO:0000250|UniProtKB:Q9NRP0,
CC ECO:0000269|PubMed:15835887, ECO:0000269|PubMed:29519914}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9NRP0}. Membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the OSTC family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BF228912; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; DN368674; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001153593.1; NM_001160121.1.
DR RefSeq; XP_005622639.1; XM_005622582.1.
DR PDB; 6FTG; EM; 9.10 A; 3=30-149.
DR PDB; 6FTI; EM; 4.20 A; 3=30-149.
DR PDB; 6FTJ; EM; 4.70 A; 3=30-149.
DR PDBsum; 6FTG; -.
DR PDBsum; 6FTI; -.
DR PDBsum; 6FTJ; -.
DR AlphaFoldDB; P86218; -.
DR SMR; P86218; -.
DR CORUM; P86218; -.
DR STRING; 9612.ENSCAFP00000042288; -.
DR PaxDb; P86218; -.
DR Ensembl; ENSCAFT00030045454; ENSCAFP00030039699; ENSCAFG00030024696.
DR Ensembl; ENSCAFT00040040804; ENSCAFP00040035588; ENSCAFG00040021980.
DR Ensembl; ENSCAFT00845008212; ENSCAFP00845006453; ENSCAFG00845004592.
DR Ensembl; ENSCAFT00845052121; ENSCAFP00845040882; ENSCAFG00845029437.
DR GeneID; 100688081; -.
DR GeneID; 477512; -.
DR KEGG; cfa:100688081; -.
DR KEGG; cfa:477512; -.
DR CTD; 58505; -.
DR VEuPathDB; HostDB:ENSCAFG00845004592; -.
DR VEuPathDB; HostDB:ENSCAFG00845029437; -.
DR eggNOG; KOG3356; Eukaryota.
DR GeneTree; ENSGT00390000001376; -.
DR HOGENOM; CLU_109136_1_0_1; -.
DR InParanoid; P86218; -.
DR OMA; WIFMRMK; -.
DR OrthoDB; 1575260at2759; -.
DR TreeFam; TF323315; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002254; Chromosome 32.
DR Proteomes; UP000002254; Chromosome 7.
DR Bgee; ENSCAFG00000011286; Expressed in pancreas and 48 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6.
DR InterPro; IPR042416; OSTC.
DR PANTHER; PTHR13160; PTHR13160; 1.
DR Pfam; PF04756; OST3_OST6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..149
FT /note="Oligosaccharyltransferase complex subunit OSTC"
FT /id="PRO_0000370225"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29519914"
FT TOPO_DOM 54..83
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29519914"
FT TOPO_DOM 105..117
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29519914"
FT TOPO_DOM 139..149
FT /note="Extracellular"
FT /evidence="ECO:0000305"
SQ SEQUENCE 149 AA; 16815 MW; E5929C5B9D9458B4 CRC64;
METLYRVPFL VLECPNLKLK KPPWVHMPSA MTVYALVVVS YFLITGGIIY DVIVEPPSVG
SMTDEHGHQR PVAFLAYRVN GQYIMEGLAS SFLFTMGGLG FIILDRSNAP NIPKLNRFLL
LFIGFVCVLL SFFMARVFMR MKLPGYLMG
