OSTC_MOUSE
ID OSTC_MOUSE Reviewed; 149 AA.
AC Q78XF5; Q9CPZ2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Oligosaccharyltransferase complex subunit OSTC {ECO:0000305};
GN Name=Ostc {ECO:0000312|MGI:MGI:1913607};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Liver, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). OST exists in
CC two different complex forms which contain common core subunits RPN1,
CC RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic
CC subunits, and form-specific accessory subunits (By similarity). STT3A
CC complex assembly occurs through the formation of 3 subcomplexes.
CC Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2 contains the
CC STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well as the core
CC subunit OST4, and subcomplex 3 contains RPN2, DAD1, and OST48. The
CC STT3A complex can form stable complexes with the Sec61 complex or with
CC both the Sec61 and TRAP complexes (By similarity). Interacts with PSEN1
CC and NCSTN; indicative for an association with the gamma-secretase
CC complex (By similarity). {ECO:0000250|UniProtKB:P86218,
CC ECO:0000250|UniProtKB:Q9NRP0}.
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:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB28595.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AK009237; BAB26158.1; -; mRNA.
DR EMBL; AK011085; BAB27389.1; -; mRNA.
DR EMBL; AK013011; BAB28595.2; ALT_INIT; mRNA.
DR EMBL; AK135332; BAE22491.1; -; mRNA.
DR EMBL; BC021935; AAH21935.1; -; mRNA.
DR CCDS; CCDS38639.1; -.
DR RefSeq; NP_079785.1; NM_025509.3.
DR AlphaFoldDB; Q78XF5; -.
DR SMR; Q78XF5; -.
DR BioGRID; 211409; 1.
DR ComplexPortal; CPX-5821; Oligosaccharyltransferase complex A.
DR IntAct; Q78XF5; 1.
DR STRING; 10090.ENSMUSP00000046480; -.
DR iPTMnet; Q78XF5; -.
DR PhosphoSitePlus; Q78XF5; -.
DR SwissPalm; Q78XF5; -.
DR EPD; Q78XF5; -.
DR jPOST; Q78XF5; -.
DR MaxQB; Q78XF5; -.
DR PaxDb; Q78XF5; -.
DR PeptideAtlas; Q78XF5; -.
DR PRIDE; Q78XF5; -.
DR ProteomicsDB; 295482; -.
DR Antibodypedia; 26281; 91 antibodies from 20 providers.
DR DNASU; 66357; -.
DR Ensembl; ENSMUST00000043937; ENSMUSP00000046480; ENSMUSG00000041084.
DR GeneID; 66357; -.
DR KEGG; mmu:66357; -.
DR UCSC; uc008rjc.2; mouse.
DR CTD; 58505; -.
DR MGI; MGI:1913607; Ostc.
DR VEuPathDB; HostDB:ENSMUSG00000041084; -.
DR eggNOG; KOG3356; Eukaryota.
DR GeneTree; ENSGT00390000001376; -.
DR HOGENOM; CLU_109136_1_0_1; -.
DR InParanoid; Q78XF5; -.
DR OMA; WIFMRMK; -.
DR OrthoDB; 1575260at2759; -.
DR PhylomeDB; Q78XF5; -.
DR TreeFam; TF323315; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 66357; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Ostc; mouse.
DR PRO; PR:Q78XF5; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q78XF5; protein.
DR Bgee; ENSMUSG00000041084; Expressed in humerus cartilage element and 179 other tissues.
DR Genevisible; Q78XF5; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISO:MGI.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISO:MGI.
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 Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..149
FT /note="Oligosaccharyltransferase complex subunit OSTC"
FT /id="PRO_0000320603"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..83
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..117
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..149
FT /note="Extracellular"
FT /evidence="ECO:0000255"
SQ SEQUENCE 149 AA; 16815 MW; E5929C5B9D9458B4 CRC64;
METLYRVPFL VLECPNLKLK KPPWVHMPSA MTVYALVVVS YFLITGGIIY DVIVEPPSVG
SMTDEHGHQR PVAFLAYRVN GQYIMEGLAS SFLFTMGGLG FIILDRSNAP NIPKLNRFLL
LFIGFVCVLL SFFMARVFMR MKLPGYLMG