STT3A_HUMAN
ID STT3A_HUMAN Reviewed; 705 AA.
AC P46977; B4DJ24; E9PNQ1; Q86XU9; Q8TE35; Q8WUB4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A {ECO:0000305};
DE Short=Oligosaccharyl transferase subunit STT3A;
DE Short=STT3-A;
DE EC=2.4.99.18;
DE AltName: Full=B5;
DE AltName: Full=Integral membrane protein 1;
DE AltName: Full=Transmembrane protein TMC;
GN Name=STT3A {ECO:0000312|HGNC:HGNC:6172}; Synonyms=ITM1, TMC;
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).
RX PubMed=8838310; DOI=10.1006/geno.1996.0051;
RA Hong G., Deleersnjider W., Kozak C.A., van Marck E., Tylzanowski P.,
RA Merregaert J.;
RT "Molecular cloning of a highly conserved mouse and human integral membrane
RT protein (Itm1) and genetic mapping to mouse chromosome 9.";
RL Genomics 31:295-300(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8634329; DOI=10.1016/0167-4781(96)00025-5;
RA Lissy N.A., Bellacosa A., Sonoda G., Miller P.D., Jhanwar S.C., Testa J.R.;
RT "Isolation, characterization, and mapping to human chromosome 11q24-25 of a
RT cDNA encoding a highly conserved putative transmembrane protein, TMC.";
RL Biochim. Biophys. Acta 1306:137-141(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Hippocampus;
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 MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Duodenum, and Lung;
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 [8]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12887896; DOI=10.1016/s1097-2765(03)00243-0;
RA Kelleher D.J., Karaoglu D., Mandon E.C., Gilmore R.;
RT "Oligosaccharyltransferase isoforms that contain different catalytic STT3
RT subunits have distinct enzymatic properties.";
RL Mol. Cell 12:101-111(2003).
RN [9]
RP FUNCTION.
RX PubMed=19167329; DOI=10.1016/j.cell.2008.11.047;
RA Ruiz-Canada C., Kelleher D.J., Gilmore R.;
RT "Cotranslational and posttranslational N-glycosylation of polypeptides by
RT distinct mammalian OST isoforms.";
RL Cell 136:272-283(2009).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-537; ASN-544 AND ASN-548.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [11]
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 [12]
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 [13]
RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE COMPLEX.
RX PubMed=25135935; DOI=10.1083/jcb.201404083;
RA Cherepanova N.A., Shrimal S., Gilmore R.;
RT "Oxidoreductase activity is necessary for N-glycosylation of cysteine-
RT proximal acceptor sites in glycoproteins.";
RL J. Cell Biol. 206:525-539(2014).
RN [14]
RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE COMPLEX.
RX PubMed=23606741; DOI=10.1242/jcs.115410;
RA Dumax-Vorzet A., Roboti P., High S.;
RT "OST4 is a subunit of the mammalian oligosaccharyltransferase required for
RT efficient N-glycosylation.";
RL J. Cell Sci. 126:2595-2606(2013).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
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 [17] {ECO:0007744|PDB:6S7O}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), IDENTIFICATION OF OST
RP COMPLEX, FUNCTION, PATHWAY, AND COFACTOR.
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 [18]
RP VARIANT CDG1W ALA-626, AND CHARACTERIZATION OF VARIANT CDG1W ALA-626.
RX PubMed=23842455; DOI=10.1093/hmg/ddt312;
RA Shrimal S., Ng B.G., Losfeld M.E., Gilmore R., Freeze H.H.;
RT "Mutations in STT3A and STT3B cause two congenital disorders of
RT glycosylation.";
RL Hum. Mol. Genet. 22:4638-4645(2013).
CC -!- FUNCTION: Catalytic subunit of the oligosaccharyl transferase (OST)
CC complex that 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. This subunit contains the
CC active site and the acceptor peptide and donor lipid-linked
CC oligosaccharide (LLO) binding pockets (By similarity). STT3A is present
CC in the majority of OST complexes and mediates cotranslational N-
CC glycosylation of most sites on target proteins, while STT3B-containing
CC complexes are required for efficient post-translational glycosylation
CC and mediate glycosylation of sites that have been skipped by STT3A
CC (PubMed:19167329). {ECO:0000250|UniProtKB:P39007,
CC ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:31831667}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl diphosphooligosaccharide + L-asparaginyl-[protein]
CC = a dolichyl diphosphate + H(+) + N(4)-(oligosaccharide-(1->4)-N-
CC acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)-L-
CC asparaginy-[protein]; Xref=Rhea:RHEA:22980, Rhea:RHEA-COMP:9529,
CC Rhea:RHEA-COMP:12635, Rhea:RHEA-COMP:12804, Rhea:RHEA-COMP:12805,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:50347, ChEBI:CHEBI:57497,
CC ChEBI:CHEBI:57570, ChEBI:CHEBI:132529; EC=2.4.99.18;
CC Evidence={ECO:0000250|UniProtKB:P39007};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:31831667};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:B9KDD4};
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:23606741, PubMed:25135935, 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).
CC {ECO:0000250|UniProtKB:F1PJP5, ECO:0000269|PubMed:23606741,
CC ECO:0000269|PubMed:25135935, ECO:0000269|PubMed:31831667}.
CC -!- INTERACTION:
CC P46977; O43187: IRAK2; NbExp=2; IntAct=EBI-719212, EBI-447733;
CC P46977; P16284: PECAM1; NbExp=3; IntAct=EBI-719212, EBI-716404;
CC P46977; Q9H5K3: POMK; NbExp=2; IntAct=EBI-719212, EBI-11337900;
CC P46977; Q86WV6: STING1; NbExp=2; IntAct=EBI-719212, EBI-2800345;
CC P46977; P37173: TGFBR2; NbExp=3; IntAct=EBI-719212, EBI-296151;
CC P46977; P55072: VCP; NbExp=3; IntAct=EBI-719212, EBI-355164;
CC P46977; O76024: WFS1; NbExp=3; IntAct=EBI-719212, EBI-720609;
CC P46977; Q6PDS3: Sarm1; Xeno; NbExp=2; IntAct=EBI-719212, EBI-6117196;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:12887896}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P46978}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P46978}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P46977-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P46977-2; Sequence=VSP_055106;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in placenta, liver, muscle
CC and pancreas, and at very low levels in brain, lung and kidney.
CC Expressed in skin fibroblasts (at protein level).
CC {ECO:0000269|PubMed:12887896}.
CC -!- DOMAIN: Despite low primary sequence conservation between eukaryotic
CC catalytic subunits and bacterial and archaeal single subunit OSTs
CC (ssOST), structural comparison revealed several common motifs at
CC spatially equivalent positions, like the DXD motif 1 on the external
CC loop 1 and the DXD motif 2 on the external loop 2 involved in binding
CC of the metal ion cofactor and the carboxamide group of the acceptor
CC asparagine, the conserved Glu residue of the TIXE/SVSE motif on the
CC external loop 5 involved in catalysis, as well as the WWDYG and the
CC DK/MI motifs in the globular domain that define the binding pocket for
CC the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg
CC residue was found to interact with a negatively charged side chain at
CC the -2 position of the sequon. This Arg is conserved in bacterial
CC enzymes and correlates with an extended sequon requirement (Asp-X-Asn-
CC X-Ser/Thr) for bacterial N-glycosylation.
CC {ECO:0000250|UniProtKB:P39007}.
CC -!- DISEASE: Congenital disorder of glycosylation 1W (CDG1W) [MIM:615596]:
CC A form of congenital disorder of glycosylation, a multisystem disorder
CC caused by a defect in glycoprotein biosynthesis and characterized by
CC under-glycosylated serum glycoproteins. Congenital disorders of
CC glycosylation result in a wide variety of clinical features, such as
CC defects in the nervous system development, psychomotor retardation,
CC dysmorphic features, hypotonia, coagulation disorders, and
CC immunodeficiency. The broad spectrum of features reflects the critical
CC role of N-glycoproteins during embryonic development, differentiation,
CC and maintenance of cell functions. {ECO:0000269|PubMed:23842455}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the STT3 family. {ECO:0000305}.
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DR EMBL; L38961; AAB05994.1; -; mRNA.
DR EMBL; L47337; AAL77539.1; -; mRNA.
DR EMBL; AK290040; BAF82729.1; -; mRNA.
DR EMBL; AK290657; BAF83346.1; -; mRNA.
DR EMBL; AK295892; BAG58686.1; -; mRNA.
DR EMBL; BT007100; AAP35764.1; -; mRNA.
DR EMBL; AP001132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471065; EAW67647.1; -; Genomic_DNA.
DR EMBL; BC020965; AAH20965.1; -; mRNA.
DR EMBL; BC048348; AAH48348.2; -; mRNA.
DR CCDS; CCDS60998.1; -. [P46977-2]
DR CCDS; CCDS8458.1; -. [P46977-1]
DR PIR; S70029; S70029.
DR RefSeq; NP_001265432.1; NM_001278503.1. [P46977-1]
DR RefSeq; NP_001265433.1; NM_001278504.1. [P46977-2]
DR RefSeq; NP_689926.1; NM_152713.4. [P46977-1]
DR RefSeq; XP_011541109.1; XM_011542807.2. [P46977-1]
DR PDB; 6S7O; EM; 3.50 A; A=1-705.
DR PDBsum; 6S7O; -.
DR AlphaFoldDB; P46977; -.
DR SMR; P46977; -.
DR BioGRID; 109908; 139.
DR ComplexPortal; CPX-5621; Oligosaccharyltransferase complex A.
DR CORUM; P46977; -.
DR IntAct; P46977; 81.
DR MINT; P46977; -.
DR STRING; 9606.ENSP00000376472; -.
DR CAZy; GT66; Glycosyltransferase Family 66.
DR TCDB; 9.B.142.3.17; the integral membrane glycosyltransferase family 39 (gt39) family.
DR TCDB; 9.B.142.3.4; the integral membrane glycosyltransferase family 39 (gt39) family.
DR GlyConnect; 1188; 8 N-Linked glycans (2 sites).
DR GlyGen; P46977; 7 sites, 10 N-linked glycans (3 sites), 1 O-linked glycan (2 sites).
DR iPTMnet; P46977; -.
DR PhosphoSitePlus; P46977; -.
DR SwissPalm; P46977; -.
DR BioMuta; STT3A; -.
DR DMDM; 182676409; -.
DR EPD; P46977; -.
DR jPOST; P46977; -.
DR MassIVE; P46977; -.
DR MaxQB; P46977; -.
DR PaxDb; P46977; -.
DR PeptideAtlas; P46977; -.
DR PRIDE; P46977; -.
DR ProteomicsDB; 22482; -.
DR ProteomicsDB; 55782; -. [P46977-1]
DR Antibodypedia; 32954; 111 antibodies from 25 providers.
DR DNASU; 3703; -.
DR Ensembl; ENST00000392708.9; ENSP00000376472.3; ENSG00000134910.14. [P46977-1]
DR Ensembl; ENST00000529196.5; ENSP00000436962.1; ENSG00000134910.14. [P46977-1]
DR Ensembl; ENST00000531491.5; ENSP00000432820.1; ENSG00000134910.14. [P46977-2]
DR Ensembl; ENST00000649491.1; ENSP00000497336.1; ENSG00000134910.14. [P46977-1]
DR GeneID; 3703; -.
DR KEGG; hsa:3703; -.
DR MANE-Select; ENST00000392708.9; ENSP00000376472.3; NM_152713.5; NP_689926.1.
DR UCSC; uc001qcd.4; human. [P46977-1]
DR CTD; 3703; -.
DR DisGeNET; 3703; -.
DR GeneCards; STT3A; -.
DR HGNC; HGNC:6172; STT3A.
DR HPA; ENSG00000134910; Tissue enhanced (parathyroid).
DR MalaCards; STT3A; -.
DR MIM; 601134; gene.
DR MIM; 615596; phenotype.
DR neXtProt; NX_P46977; -.
DR OpenTargets; ENSG00000134910; -.
DR Orphanet; 370921; STT3A-CDG.
DR PharmGKB; PA29969; -.
DR VEuPathDB; HostDB:ENSG00000134910; -.
DR eggNOG; KOG2292; Eukaryota.
DR GeneTree; ENSGT00940000156655; -.
DR HOGENOM; CLU_009279_1_0_1; -.
DR InParanoid; P46977; -.
DR OMA; VAYSSWY; -.
DR OrthoDB; 187775at2759; -.
DR PhylomeDB; P46977; -.
DR TreeFam; TF300822; -.
DR BRENDA; 2.4.99.18; 2681.
DR PathwayCommons; P46977; -.
DR Reactome; R-HSA-446203; Asparagine N-linked glycosylation.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR SignaLink; P46977; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 3703; 190 hits in 1095 CRISPR screens.
DR ChiTaRS; STT3A; human.
DR GenomeRNAi; 3703; -.
DR Pharos; P46977; Tbio.
DR PRO; PR:P46977; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P46977; protein.
DR Bgee; ENSG00000134910; Expressed in stromal cell of endometrium and 177 other tissues.
DR ExpressionAtlas; P46977; baseline and differential.
DR Genevisible; P46977; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IDA:ARUK-UCL.
DR GO; GO:0035000; C:oligosaccharyltransferase III complex; ISS:UniProtKB.
DR GO; GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043686; P:co-translational protein modification; IMP:UniProtKB.
DR GO; GO:0043687; P:post-translational protein modification; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:ComplexPortal.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IMP:UniProtKB.
DR InterPro; IPR003674; Oligo_trans_STT3.
DR PANTHER; PTHR13872; PTHR13872; 1.
DR Pfam; PF02516; STT3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Congenital disorder of glycosylation;
KW Disease variant; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW Magnesium; Manganese; Membrane; Metal-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..705
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit STT3A"
FT /id="PRO_0000072290"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..119
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 120..138
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 139..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 141..158
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 159..169
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 170..189
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 190..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 192..206
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 207..211
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 212..228
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 229..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 234..259
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 260..267
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 268..287
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 288..300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..356
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 357..379
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 380..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 386..402
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 403..406
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 407..428
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 429..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 454..473
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 474..705
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 525..527
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT MOTIF 47..49
FT /note="DXD motif 1"
FT /evidence="ECO:0000250|UniProtKB:Q5HTX9"
FT MOTIF 167..169
FT /note="DXD motif 2"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT MOTIF 348..351
FT /note="SVSE motif"
FT /evidence="ECO:0000250|UniProtKB:Q5HTX9"
FT MOTIF 525..529
FT /note="WWDYG motif"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT MOTIF 592..599
FT /note="DK motif"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT BINDING 49
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 167
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 169
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 405
FT /ligand="dolichyl diphosphooligosaccharide"
FT /ligand_id="ChEBI:CHEBI:57570"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 530
FT /ligand="dolichyl diphosphooligosaccharide"
FT /ligand_id="ChEBI:CHEBI:57570"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 49
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 160
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 351
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 595
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VAR_SEQ 1..92
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055106"
FT VARIANT 626
FT /note="V -> A (in CDG1W; affects activity resulting in
FT hypoglycosylation of STT3A-specific substrates;
FT dbSNP:rs587777216)"
FT /evidence="ECO:0000269|PubMed:23842455"
FT /id="VAR_070944"
FT CONFLICT 61
FT /note="A -> S (in Ref. 2; AAL77539)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="V -> M (in Ref. 3; BAG58686)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="T -> S (in Ref. 1; AAB05994)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="H -> L (in Ref. 1; AAB05994)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="M -> R (in Ref. 1; AAB05994)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="A -> G (in Ref. 1; AAB05994)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="C -> S (in Ref. 1; AAB05994)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="N -> I (in Ref. 1; AAB05994)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="G -> D (in Ref. 2; AAL77539)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="A -> G (in Ref. 1; AAB05994)"
FT /evidence="ECO:0000305"
FT HELIX 11..34
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 50..63
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 91..105
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 119..138
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 155..159
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 169..189
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 192..208
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:6S7O"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 219..229
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 234..252
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 268..289
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 292..298
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:6S7O"
FT TURN 344..348
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 357..363
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 371..380
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 386..402
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 405..410
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 411..429
FT /evidence="ECO:0007829|PDB:6S7O"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 455..481
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 487..491
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 504..514
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 521..523
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 530..535
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 539..541
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 549..560
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 563..573
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 577..581
FT /evidence="ECO:0007829|PDB:6S7O"
FT TURN 584..587
FT /evidence="ECO:0007829|PDB:6S7O"
FT TURN 592..595
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 596..603
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 606..608
FT /evidence="ECO:0007829|PDB:6S7O"
FT TURN 610..612
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:6S7O"
FT TURN 632..636
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 638..641
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 653..656
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 658..661
FT /evidence="ECO:0007829|PDB:6S7O"
FT TURN 662..665
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 676..683
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 689..694
FT /evidence="ECO:0007829|PDB:6S7O"
SQ SEQUENCE 705 AA; 80530 MW; 71426CA5598B51C4 CRC64;
MTKFGFLRLS YEKQDTLLKL LILSMAAVLS FSTRLFAVLR FESVIHEFDP YFNYRTTRFL
AEEGFYKFHN WFDDRAWYPL GRIIGGTIYP GLMITSAAIY HVLHFFHITI DIRNVCVFLA
PLFSSFTTIV TYHLTKELKD AGAGLLAAAM IAVVPGYISR SVAGSYDNEG IAIFCMLLTY
YMWIKAVKTG SICWAAKCAL AYFYMVSSWG GYVFLINLIP LHVLVLMLTG RFSHRIYVAY
CTVYCLGTIL SMQISFVGFQ PVLSSEHMAA FGVFGLCQIH AFVDYLRSKL NPQQFEVLFR
SVISLVGFVL LTVGALLMLT GKISPWTGRF YSLLDPSYAK NNIPIIASVS EHQPTTWSSY
YFDLQLLVFM FPVGLYYCFS NLSDARIFII MYGVTSMYFS AVMVRLMLVL APVMCILSGI
GVSQVLSTYM KNLDISRPDK KSKKQQDSTY PIKNEVASGM ILVMAFFLIT YTFHSTWVTS
EAYSSPSIVL SARGGDGSRI IFDDFREAYY WLRHNTPEDA KVMSWWDYGY QITAMANRTI
LVDNNTWNNT HISRVGQAMA STEEKAYEIM RELDVSYVLV IFGGLTGYSS DDINKFLWMV
RIGGSTDTGK HIKENDYYTP TGEFRVDREG SPVLLNCLMY KMCYYRFGQV YTEAKRPPGF
DRVRNAEIGN KDFELDVLEE AYTTEHWLVR IYKVKDLDNR GLSRT
