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   12-AUG-2020, entry version 119.
DE   RecName: Full=Transmembrane protein 258;
DE   AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TMEM258;
DE            Short=Oligosaccharyl transferase subunit TMEM258;
GN   Name=TMEM258; Synonyms=C11orf10; 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   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   [9]
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   [10]
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   [11]
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   [12]
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).
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 (PubMed:26472760, PubMed:27974209). Involved in ER
CC       homeostasis in the colonic epithelium (By similarity).
CC       {ECO:0000250|UniProtKB:P61166, ECO:0000269|PubMed:26472760,
CC       ECO:0000269|PubMed:27974209}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
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
CC       (PubMed:26472760, PubMed:27974209). STT3A complex assembly occurs
CC       through the formation of 3 subcomplexes. Subcomplex 1 contains RPN1 and
CC       TMEM258, subcomplex 2 contains the STT3A-specific subunits STT3A,
CC       DC2/OSTC, and KCP2 as well as the core subunit OST4, and subcomplex 3
CC       contains RPN2, DAD1, and OST48. The STT3A complex can form stable
CC       complexes with the Sec61 complex or with both the Sec61 and TRAP
CC       complexes (By similarity). {ECO:0000250|UniProtKB:E2RKN8,
CC       ECO:0000269|PubMed:26472760, ECO:0000269|PubMed:27974209}.
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}. Endoplasmic reticulum
CC       {ECO:0000269|PubMed:26472760, ECO:0000269|PubMed:27974209}.
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   SMR; P61165; -.
DR   BioGRID; 107204; 19.
DR   IntAct; P61165; 7.
DR   STRING; 9606.ENSP00000443216; -.
DR   TCDB; 9.B.142.3.17; the integral membrane glycosyltransferase family 39 (gt39) family.
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.
DR   Ensembl; ENST00000257262; ENSP00000257262; ENSG00000134825.
DR   Ensembl; ENST00000537328; ENSP00000443216; ENSG00000134825.
DR   GeneID; 746; -.
DR   KEGG; hsa:746; -.
DR   UCSC; uc001nsf.4; human.
DR   CTD; 746; -.
DR   DisGeNET; 746; -.
DR   EuPathDB; HostDB:ENSG00000134825.13; -.
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   eggNOG; KOG4452; Eukaryota.
DR   GeneTree; ENSGT00390000010089; -.
DR   InParanoid; P61165; -.
DR   OMA; MVRYASP; -.
DR   OrthoDB; 1627291at2759; -.
DR   PhylomeDB; P61165; -.
DR   TreeFam; TF300295; -.
DR   PathwayCommons; P61165; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 746; 569 hits in 876 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 saliva-secreting gland and 244 other tissues.
DR   ExpressionAtlas; P61165; baseline and differential.
DR   Genevisible; P61165; HS.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043227; C:membrane-bounded organelle; IBA:GO_Central.
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; IMP:UniProtKB.
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; 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:0000244|PubMed:19413330,
FT                   ECO:0000244|PubMed:22223895"
FT   STRAND          4..8
FT                   /evidence="ECO:0000244|PDB:6S7T"
FT   HELIX           15..17
FT                   /evidence="ECO:0000244|PDB:6S7O"
FT   HELIX           18..42
FT                   /evidence="ECO:0000244|PDB:6S7O"
FT   HELIX           45..47
FT                   /evidence="ECO:0000244|PDB:6S7O"
FT   HELIX           50..75
FT                   /evidence="ECO:0000244|PDB:6S7O"
SQ   SEQUENCE   79 AA;  9079 MW;  8105E40132994646 CRC64;
     MELEAMSRYT SPVNPAVFPH LTVVLLAIGM FFTAWFFVYE VTSTKYTRDI YKELLISLVA
     SLFMGFGVLF LLLWVGIYV
//