TM258_MOUSE
ID TM258_MOUSE Reviewed; 79 AA.
AC P61166; Q9D953; Q9Y2Q7;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Transmembrane protein 258 {ECO:0000305};
DE AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TMEM258;
DE Short=Oligosaccharyl transferase subunit TMEM258;
GN Name=Tmem258 {ECO:0000312|MGI:MGI:1916288};
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=Pancreas;
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 FUNCTION, AND IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE COMPLEX.
RX PubMed=27974209; DOI=10.1016/j.celrep.2016.11.042;
RA Graham D.B., Lefkovith A., Deelen P., de Klein N., Varma M., Boroughs A.,
RA Desch A.N., Ng A.C., Guzman G., Schenone M., Petersen C.P., Bhan A.K.,
RA Rivas M.A., Daly M.J., Carr S.A., Wijmenga C., Xavier R.J.;
RT "TMEM258 is a component of the oligosaccharyltransferase complex
RT controlling ER stress and intestinal inflammation.";
RL Cell Rep. 17:2955-2965(2016).
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. Involved in ER homeostasis in
CC the colonic epithelium. {ECO:0000250|UniProtKB:P61165,
CC ECO:0000269|PubMed:27974209}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P61165}.
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 (Probable). 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 (By
CC similarity). {ECO:0000250|UniProtKB:E2RKN8,
CC ECO:0000250|UniProtKB:P61165, ECO:0000305|PubMed:27974209}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P61165}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:P61165}. Endoplasmic
CC reticulum {ECO:0000250|UniProtKB:P61165}. Cytoplasm
CC {ECO:0000250|UniProtKB:P61165}.
CC -!- SIMILARITY: Belongs to the OST5 family. {ECO:0000305}.
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DR EMBL; AK007351; BAB24978.1; -; mRNA.
DR CCDS; CCDS50385.1; -.
DR RefSeq; NP_081195.1; NM_026919.1.
DR AlphaFoldDB; P61166; -.
DR SMR; P61166; -.
DR ComplexPortal; CPX-5821; Oligosaccharyltransferase complex A.
DR ComplexPortal; CPX-5822; Oligosaccharyltransferase complex B.
DR STRING; 10090.ENSMUSP00000044751; -.
DR PhosphoSitePlus; P61166; -.
DR EPD; P61166; -.
DR PaxDb; P61166; -.
DR PeptideAtlas; P61166; -.
DR PRIDE; P61166; -.
DR ProteomicsDB; 260694; -.
DR TopDownProteomics; P61166; -.
DR Antibodypedia; 51765; 8 antibodies from 6 providers.
DR Ensembl; ENSMUST00000040372; ENSMUSP00000044751; ENSMUSG00000036372.
DR GeneID; 69038; -.
DR KEGG; mmu:69038; -.
DR UCSC; uc008gpi.2; mouse.
DR CTD; 746; -.
DR MGI; MGI:1916288; Tmem258.
DR VEuPathDB; HostDB:ENSMUSG00000036372; -.
DR eggNOG; KOG4452; Eukaryota.
DR GeneTree; ENSGT00390000010089; -.
DR InParanoid; P61166; -.
DR OMA; MERYVGP; -.
DR OrthoDB; 1627291at2759; -.
DR PhylomeDB; P61166; -.
DR TreeFam; TF300295; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 69038; 20 hits in 74 CRISPR screens.
DR ChiTaRS; Tmem258; mouse.
DR PRO; PR:P61166; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P61166; protein.
DR Bgee; ENSMUSG00000036372; Expressed in dorsal pancreas and 75 other tissues.
DR ExpressionAtlas; P61166; baseline and differential.
DR Genevisible; P61166; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
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:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0043227; C:membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISO:MGI.
DR GO; GO:0034998; C:oligosaccharyltransferase I complex; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISO:MGI.
DR InterPro; IPR007915; TMEM258/Ost5.
DR PANTHER; PTHR13636; PTHR13636; 1.
DR Pfam; PF05251; Ost5; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..79
FT /note="Transmembrane protein 258"
FT /id="PRO_0000221143"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P61165"
SQ SEQUENCE 79 AA; 9079 MW; 8105E40132994646 CRC64;
MELEAMSRYT SPVNPAVFPH LTVVLLAIGM FFTAWFFVYE VTSTKYTRDI YKELLISLVA
SLFMGFGVLF LLLWVGIYV
