TM258_CANLF
ID TM258_CANLF Reviewed; 79 AA.
AC E2RKN8;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Transmembrane protein 258 {ECO:0000250|UniProtKB:P61165};
DE AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TMEM258;
DE Short=Oligosaccharyl transferase subunit TMEM258;
GN Name=TMEM258 {ECO:0000250|UniProtKB:P61165};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [2]
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. {ECO:0000250|UniProtKB:P61165}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P61165}.
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 (By
CC similarity). STT3A complex assembly occurs through the formation of 3
CC subcomplexes. Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2
CC contains the STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well
CC as the core subunit OST4, and subcomplex 3 contains RPN2, DAD1, and
CC OST48. The STT3A complex can form stable complexes with the Sec61
CC complex or with both the Sec61 and TRAP complexes (PubMed:29519914).
CC {ECO:0000250|UniProtKB:P61165, ECO:0000269|PubMed:29519914}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P61165}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:29519914}. 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; AAEX03004880; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 6FTG; EM; 9.10 A; 2=-.
DR PDB; 6FTI; EM; 4.20 A; 2=-.
DR PDB; 6FTJ; EM; 4.70 A; 2=-.
DR PDBsum; 6FTG; -.
DR PDBsum; 6FTI; -.
DR PDBsum; 6FTJ; -.
DR AlphaFoldDB; E2RKN8; -.
DR SMR; E2RKN8; -.
DR STRING; 9612.ENSCAFP00000030163; -.
DR PaxDb; E2RKN8; -.
DR Ensembl; ENSCAFT00030019682; ENSCAFP00030017164; ENSCAFG00030010668.
DR eggNOG; KOG4452; Eukaryota.
DR HOGENOM; CLU_180449_0_0_1; -.
DR InParanoid; E2RKN8; -.
DR OMA; MERYVGP; -.
DR TreeFam; TF300295; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002254; Unplaced.
DR Bgee; ENSCAFG00000029055; Expressed in smooth muscle tissue and 7 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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:0034998; C:oligosaccharyltransferase I complex; IEA:InterPro.
DR GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IEA:InterPro.
DR InterPro; IPR007915; TMEM258/Ost5.
DR PANTHER; PTHR13636; PTHR13636; 1.
DR Pfam; PF05251; Ost5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..79
FT /note="Transmembrane protein 258"
FT /id="PRO_0000445978"
FT TOPO_DOM 1..16
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..79
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P61165"
SQ SEQUENCE 79 AA; 9019 MW; 8105E4012938FC46 CRC64;
MELEAMSRYT SPVNPAVFPH LTVVLLAIGM FFTAWFFVYE VTSTKYTRDI CKELLISLVA
SLFMGFGVLF LLLWVGIYV
