ID OSTC_HUMAN Reviewed; 149 AA. AC Q9NRP0; A8MYS2; B2R5H1; D6RH22; Q9P075; Q9P1R4; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 28-JUN-2023, entry version 155. DE RecName: Full=Oligosaccharyltransferase complex subunit OSTC {ECO:0000305}; DE AltName: Full=Hydrophobic protein HSF-28; GN Name=OSTC {ECO:0000312|HGNC:HGNC:24448}; ORFNames=DC2, HDCMD45P, HSPC307; 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] (ISOFORM 1). RC TISSUE=Kidney; RA Favier A.-L., Harsi C., Chrobozcek J.; RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Dendritic cell; RA Zhao Z., Huang X., Li N., Zhu X., Cao X.; RT "A novel gene from human dendritic cell."; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Umbilical cord blood; RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.; RT "Human partial CDS from CD34+ stem cells."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Dendritic cell; RA Peng Y., Li Y., Li N., Gu W., Han Z., Fu G., Chen Z.; RT "Novel genes expressed in human dendritic cell."; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=15146197; DOI=10.1038/nbt971; RA Brandenberger R., Wei H., Zhang S., Lei S., Murage J., Fisk G.J., Li Y., RA Xu C., Fang R., Guegler K., Rao M.S., Mandalam R., Lebkowski J., RA Stanton L.W.; RT "Transcriptome characterization elucidates signaling networks that control RT human ES cell growth and differentiation."; RL Nat. Biotechnol. 22:707-716(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Mesangial cell; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [8] 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 [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and Urinary bladder; 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 [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PSEN1 AND NCSTN. RX PubMed=21768116; DOI=10.1074/jbc.m111.249748; RA Wilson C.M., Magnaudeix A., Yardin C., Terro F.; RT "DC2 and keratinocyte-associated protein 2 (KCP2), subunits of the RT oligosaccharyltransferase complex, are regulators of the gamma-secretase- RT directed processing of amyloid precursor protein (APP)."; RL J. Biol. Chem. 286:31080-31091(2011). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [13] {ECO:0007744|PDB:6S7O} RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), IDENTIFICATION AS RP COMPONENT OF THE STT3A-CONTAINING OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX, RP 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). RN [14] RP VARIANT [LARGE SCALE ANALYSIS] LEU-9. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). 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 (PubMed:31831667). N- CC glycosylation occurs cotranslationally and the complex associates with CC the Sec61 complex at the channel-forming translocon complex that CC mediates protein translocation across the endoplasmic reticulum (ER). CC All subunits are required for a maximal enzyme activity. May be CC involved in N-glycosylation of APP (amyloid-beta precursor protein). CC Can modulate gamma-secretase cleavage of APP by enhancing CC endoprotelysis of PSEN1. {ECO:0000269|PubMed:21768116, CC ECO:0000269|PubMed:31831667}. CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000269|PubMed:31831667}. CC -!- SUBUNIT: Specific component of the STT3A-containing form of the CC oligosaccharyltransferase (OST) complex (PubMed:31831667). OST exists CC in 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 (PubMed:21768116, CC PubMed:31831667). STT3A complex assembly occurs through the formation CC of 3 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 (By similarity). CC Interacts with PSEN1 and NCSTN; indicative for an association with the CC gamma-secretase complex (PubMed:21768116). CC {ECO:0000250|UniProtKB:P86218, ECO:0000269|PubMed:21768116, CC ECO:0000269|PubMed:31831667}. CC -!- INTERACTION: CC Q9NRP0; Q92838: EDA; NbExp=3; IntAct=EBI-1044658, EBI-529425; CC Q9NRP0; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-1044658, EBI-11988865; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum CC {ECO:0000269|PubMed:21768116}. Membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9NRP0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NRP0-2; Sequence=VSP_047376; CC -!- SIMILARITY: Belongs to the OSTC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF28985.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAF65186.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CN430159; Type=Frameshift; 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; AF343342; AAK69656.1; -; mRNA. DR EMBL; AF068297; AAF65186.1; ALT_INIT; mRNA. DR EMBL; AF161425; AAF28985.1; ALT_INIT; mRNA. DR EMBL; AF201937; AAF86873.1; -; mRNA. DR EMBL; CN430159; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK312185; BAG35118.1; -; mRNA. DR EMBL; AC107071; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471057; EAX06233.1; -; Genomic_DNA. DR EMBL; BC016321; AAH16321.1; -; mRNA. DR EMBL; BC054857; AAH54857.1; -; mRNA. DR CCDS; CCDS3681.1; -. [Q9NRP0-1] DR CCDS; CCDS58921.1; -. [Q9NRP0-2] DR RefSeq; NP_001254746.1; NM_001267817.1. DR RefSeq; NP_001254747.1; NM_001267818.1. [Q9NRP0-2] DR RefSeq; NP_067050.1; NM_021227.3. [Q9NRP0-1] DR PDB; 6S7O; EM; 3.50 A; H=1-149. DR PDB; 8B6L; EM; 7.60 A; J=1-149. DR PDBsum; 6S7O; -. DR PDBsum; 8B6L; -. DR AlphaFoldDB; Q9NRP0; -. DR SMR; Q9NRP0; -. DR BioGRID; 121833; 77. DR ComplexPortal; CPX-5621; Oligosaccharyltransferase complex A. DR IntAct; Q9NRP0; 26. DR MINT; Q9NRP0; -. DR STRING; 9606.ENSP00000426167; -. DR TCDB; 1.A.76.2.9; the magnesium transporter1 (magt1) family. DR TCDB; 9.B.142.3.17; the integral membrane glycosyltransferase family 39 (gt39) family. DR GlyGen; Q9NRP0; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NRP0; -. DR PhosphoSitePlus; Q9NRP0; -. DR SwissPalm; Q9NRP0; -. DR BioMuta; OSTC; -. DR DMDM; 74734324; -. DR EPD; Q9NRP0; -. DR jPOST; Q9NRP0; -. DR MassIVE; Q9NRP0; -. DR MaxQB; Q9NRP0; -. DR PaxDb; Q9NRP0; -. DR PeptideAtlas; Q9NRP0; -. DR ProteomicsDB; 14790; -. DR ProteomicsDB; 82398; -. [Q9NRP0-1] DR TopDownProteomics; Q9NRP0-1; -. [Q9NRP0-1] DR Antibodypedia; 26281; 98 antibodies from 21 providers. DR DNASU; 58505; -. DR Ensembl; ENST00000361564.9; ENSP00000354676.4; ENSG00000198856.13. [Q9NRP0-1] DR Ensembl; ENST00000512478.2; ENSP00000426167.2; ENSG00000198856.13. [Q9NRP0-2] DR GeneID; 58505; -. DR KEGG; hsa:58505; -. DR MANE-Select; ENST00000361564.9; ENSP00000354676.4; NM_021227.4; NP_067050.1. DR UCSC; uc003hzb.3; human. [Q9NRP0-1] DR AGR; HGNC:24448; -. DR CTD; 58505; -. DR DisGeNET; 58505; -. DR GeneCards; OSTC; -. DR HGNC; HGNC:24448; OSTC. DR HPA; ENSG00000198856; Low tissue specificity. DR MIM; 619023; gene. DR neXtProt; NX_Q9NRP0; -. DR OpenTargets; ENSG00000198856; -. DR PharmGKB; PA164724280; -. DR VEuPathDB; HostDB:ENSG00000198856; -. DR eggNOG; KOG3356; Eukaryota. DR GeneTree; ENSGT00390000001376; -. DR HOGENOM; CLU_109136_1_0_1; -. DR InParanoid; Q9NRP0; -. DR OMA; ILDRTHN; -. DR OrthoDB; 5388489at2759; -. DR PhylomeDB; Q9NRP0; -. DR TreeFam; TF323315; -. DR BRENDA; 2.4.99.18; 2681. DR PathwayCommons; Q9NRP0; -. DR SignaLink; Q9NRP0; -. DR SIGNOR; Q9NRP0; -. DR UniPathway; UPA00378; -. DR BioGRID-ORCS; 58505; 444 hits in 1134 CRISPR screens. DR ChiTaRS; OSTC; human. DR GenomeRNAi; 58505; -. DR Pharos; Q9NRP0; Tbio. DR PRO; PR:Q9NRP0; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q9NRP0; protein. DR Bgee; ENSG00000198856; Expressed in stromal cell of endometrium and 180 other tissues. DR ExpressionAtlas; Q9NRP0; baseline and differential. DR Genevisible; Q9NRP0; HS. DR GO; GO:0005789; C:endoplasmic reticulum membrane; NAS:ComplexPortal. DR GO; GO:0008250; C:oligosaccharyltransferase complex; IDA:HGNC. DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:ComplexPortal. DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IC:HGNC-UCL. DR InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6. DR InterPro; IPR042416; OSTC. DR PANTHER; PTHR13160; OLIGOSACCHARYLTRANSFERASE COMPLEX SUBUNIT OSTC; 1. DR PANTHER; PTHR13160:SF9; OLIGOSACCHARYLTRANSFERASE COMPLEX SUBUNIT OSTC; 1. DR Pfam; PF04756; OST3_OST6; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Endoplasmic reticulum; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..149 FT /note="Oligosaccharyltransferase complex subunit OSTC" FT /id="PRO_0000320602" 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" FT VAR_SEQ 145..149 FT /note="GYLMG -> RSLALLPRLECSGVISAHYKLCLPGAI (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15146197" FT /id="VSP_047376" FT VARIANT 9 FT /note="F -> L (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_039231" FT CONFLICT 119 FT /note="L -> P (in Ref. 2; AAF65186)" FT /evidence="ECO:0000305" FT TURN 29..31 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 32..45 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 48..53 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 84..107 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 114..142 FT /evidence="ECO:0007829|PDB:6S7O" SQ SEQUENCE 149 AA; 16829 MW; E59289BB927442B4 CRC64; METLYRVPFL VLECPNLKLK KPPWLHMPSA MTVYALVVVS YFLITGGIIY DVIVEPPSVG SMTDEHGHQR PVAFLAYRVN GQYIMEGLAS SFLFTMGGLG FIILDRSNAP NIPKLNRFLL LFIGFVCVLL SFFMARVFMR MKLPGYLMG //