TM258_HUMAN
ID TM258_HUMAN Reviewed; 79 AA.
AC P61165; A8K6L8; Q9D953; Q9Y2Q7;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
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|HGNC:HGNC:1164}; Synonyms=C11orf10;
GN ORFNames=HSPC005;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Marquardt A., Stoehr H., Rivera A., Weber B.H.F.;
RT "Identification and genomic characterization of seven novel genes from a
RT 288 kb interval in 11q12-q13.1.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Uterus;
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 [7]
RP PROTEIN SEQUENCE OF 1-8.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=12427278; DOI=10.1089/15362310260256927;
RA Adachi N., Karanjawala Z.E., Matsuzaki Y., Koyama H., Lieber M.R.;
RT "Two overlapping divergent transcription units in the human genome: the
RT FEN1/C11orf10 locus.";
RL OMICS 6:273-279(2002).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP FUNCTION, IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=26472760; DOI=10.1126/science.aac7557;
RA Blomen V.A., Majek P., Jae L.T., Bigenzahn J.W., Nieuwenhuis J.,
RA Staring J., Sacco R., van Diemen F.R., Olk N., Stukalov A., Marceau C.,
RA Janssen H., Carette J.E., Bennett K.L., Colinge J., Superti-Furga G.,
RA Brummelkamp T.R.;
RT "Gene essentiality and synthetic lethality in haploid human cells.";
RL Science 350:1092-1096(2015).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, IDENTIFICATION IN THE
RP OLIGOSACCHARYLTRANSFERASE COMPLEX, AND INTERACTION WITH RPN1.
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).
RN [14]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SYNE1; SYNE2 AND SUN1.
RX PubMed=28716842; DOI=10.1083/jcb.201606043;
RA Ding Z.Y., Wang Y.H., Huang Y.C., Lee M.C., Tseng M.J., Chi Y.H.,
RA Huang M.L.;
RT "Outer nuclear membrane protein Kuduk modulates the LINC complex and
RT nuclear envelope architecture.";
RL J. Cell Biol. 216:2827-2841(2017).
RN [15] {ECO:0007744|PDB:6S7O, ECO:0007744|PDB:6S7T}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), IDENTIFICATION IN THE
RP OLIGOSACCHARYL TRANSFERASE (OST) COMPLEX, FUNCTION, AND PATHWAY.
RX PubMed=31831667; DOI=10.1126/science.aaz3505;
RA Ramirez A.S., Kowal J., Locher K.P.;
RT "Cryo-electron microscopy structures of human oligosaccharyltransferase
RT complexes OST-A and OST-B.";
RL Science 366:1372-1375(2019).
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 (PubMed:31831667). 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 (PubMed:26472760,
CC PubMed:27974209). Involved in ER homeostasis in the colonic epithelium
CC (By similarity). {ECO:0000250|UniProtKB:P61166,
CC ECO:0000269|PubMed:26472760, ECO:0000269|PubMed:27974209,
CC ECO:0000269|PubMed:31831667}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:31831667}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex
CC (PubMed:31831667). OST exists in two different complex forms which
CC contain common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258,
CC either STT3A or STT3B as catalytic subunits, and form-specific
CC accessory subunits (PubMed:26472760, PubMed:27974209, PubMed:31831667).
CC STT3A 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 SYNE1
CC (via KASH domain), SYNE2 (via KASH domain) and SUN1 (PubMed:28716842).
CC {ECO:0000250|UniProtKB:E2RKN8, ECO:0000269|PubMed:26472760,
CC ECO:0000269|PubMed:27974209, ECO:0000269|PubMed:28716842,
CC ECO:0000269|PubMed:31831667}.
CC -!- INTERACTION:
CC P61165; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-12019210, EBI-714543;
CC P61165; Q9Y5U9: IER3IP1; NbExp=3; IntAct=EBI-12019210, EBI-725665;
CC P61165; Q6ZSS7: MFSD6; NbExp=3; IntAct=EBI-12019210, EBI-2858252;
CC P61165; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-12019210, EBI-741480;
CC P61165; P0DTC4: E; Xeno; NbExp=3; IntAct=EBI-12019210, EBI-25475850;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:28716842}; Multi-
CC pass membrane protein {ECO:0000305}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:26472760, ECO:0000269|PubMed:27974209}. Cytoplasm
CC {ECO:0000269|PubMed:12427278, ECO:0000269|PubMed:28716842}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:27974209}.
CC -!- SIMILARITY: Belongs to the OST5 family. {ECO:0000305}.
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DR EMBL; AF086763; AAF28401.1; -; mRNA.
DR EMBL; AF070661; AAD20967.1; -; mRNA.
DR EMBL; AK291683; BAF84372.1; -; mRNA.
DR EMBL; AP002380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW73970.1; -; Genomic_DNA.
DR EMBL; BC002750; AAH02750.1; -; mRNA.
DR EMBL; BC015968; AAH15968.1; -; mRNA.
DR CCDS; CCDS8009.1; -.
DR RefSeq; NP_055021.1; NM_014206.3.
DR PDB; 6S7O; EM; 3.50 A; C=1-79.
DR PDB; 6S7T; EM; 3.50 A; C=1-79.
DR PDBsum; 6S7O; -.
DR PDBsum; 6S7T; -.
DR AlphaFoldDB; P61165; -.
DR SMR; P61165; -.
DR BioGRID; 107204; 39.
DR ComplexPortal; CPX-5621; Oligosaccharyltransferase complex A.
DR ComplexPortal; CPX-5622; Oligosaccharyltransferase complex B.
DR IntAct; P61165; 10.
DR STRING; 9606.ENSP00000443216; -.
DR TCDB; 9.B.142.3.17; the integral membrane glycosyltransferase family 39 (gt39) family.
DR GlyGen; P61165; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61165; -.
DR PhosphoSitePlus; P61165; -.
DR BioMuta; TMEM258; -.
DR DMDM; 47117653; -.
DR EPD; P61165; -.
DR jPOST; P61165; -.
DR MassIVE; P61165; -.
DR MaxQB; P61165; -.
DR PaxDb; P61165; -.
DR PeptideAtlas; P61165; -.
DR PRIDE; P61165; -.
DR ProteomicsDB; 57271; -.
DR TopDownProteomics; P61165; -.
DR Antibodypedia; 51765; 8 antibodies from 6 providers.
DR DNASU; 746; -.
DR Ensembl; ENST00000257262.12; ENSP00000257262.8; ENSG00000134825.16.
DR Ensembl; ENST00000537328.6; ENSP00000443216.1; ENSG00000134825.16.
DR GeneID; 746; -.
DR KEGG; hsa:746; -.
DR MANE-Select; ENST00000537328.6; ENSP00000443216.1; NM_014206.4; NP_055021.1.
DR UCSC; uc001nsf.4; human.
DR CTD; 746; -.
DR DisGeNET; 746; -.
DR GeneCards; TMEM258; -.
DR HGNC; HGNC:1164; TMEM258.
DR HPA; ENSG00000134825; Low tissue specificity.
DR MIM; 617615; gene.
DR neXtProt; NX_P61165; -.
DR OpenTargets; ENSG00000134825; -.
DR PharmGKB; PA25478; -.
DR VEuPathDB; HostDB:ENSG00000134825; -.
DR eggNOG; KOG4452; Eukaryota.
DR GeneTree; ENSGT00390000010089; -.
DR InParanoid; P61165; -.
DR OMA; MERYVGP; -.
DR OrthoDB; 1627291at2759; -.
DR PhylomeDB; P61165; -.
DR TreeFam; TF300295; -.
DR BRENDA; 2.4.99.18; 2681.
DR PathwayCommons; P61165; -.
DR SignaLink; P61165; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 746; 587 hits in 1075 CRISPR screens.
DR ChiTaRS; TMEM258; human.
DR GenomeRNAi; 746; -.
DR Pharos; P61165; Tdark.
DR PRO; PR:P61165; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P61165; protein.
DR Bgee; ENSG00000134825; Expressed in type B pancreatic cell and 203 other tissues.
DR ExpressionAtlas; P61165; baseline and differential.
DR Genevisible; P61165; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0043227; C:membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IPI:ComplexPortal.
DR GO; GO:0034998; C:oligosaccharyltransferase I complex; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:ComplexPortal.
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; Direct protein sequencing;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..79
FT /note="Transmembrane protein 258"
FT /id="PRO_0000221142"
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:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 18..42
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 50..75
FT /evidence="ECO:0007829|PDB:6S7O"
SQ SEQUENCE 79 AA; 9079 MW; 8105E40132994646 CRC64;
MELEAMSRYT SPVNPAVFPH LTVVLLAIGM FFTAWFFVYE VTSTKYTRDI YKELLISLVA
SLFMGFGVLF LLLWVGIYV
