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Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A (Oligosaccharyl transferase subunit STT3A) (STT3-A) (EC 2.4.99.18) (B5) (Integral membrane protein 1) (Transmembrane protein TMC)

 STT3A_HUMAN             Reviewed;         705 AA.
P46977; B4DJ24; E9PNQ1; Q86XU9; Q8TE35; Q8WUB4;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
08-APR-2008, sequence version 2.
10-OCT-2018, entry version 156.
RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A;
Short=Oligosaccharyl transferase subunit STT3A;
Short=STT3-A;
EC=2.4.99.18;
AltName: Full=B5;
AltName: Full=Integral membrane protein 1;
AltName: Full=Transmembrane protein TMC;
Name=STT3A; Synonyms=ITM1, TMC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8838310; DOI=10.1006/geno.1996.0051;
Hong G., Deleersnjider W., Kozak C.A., van Marck E., Tylzanowski P.,
Merregaert J.;
"Molecular cloning of a highly conserved mouse and human integral
membrane protein (Itm1) and genetic mapping to mouse chromosome 9.";
Genomics 31:295-300(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8634329; DOI=10.1016/0167-4781(96)00025-5;
Lissy N.A., Bellacosa A., Sonoda G., Miller P.D., Jhanwar S.C.,
Testa J.R.;
"Isolation, characterization, and mapping to human chromosome 11q24-25
of a cDNA encoding a highly conserved putative transmembrane protein,
TMC.";
Biochim. Biophys. Acta 1306:137-141(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Duodenum, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=12887896; DOI=10.1016/S1097-2765(03)00243-0;
Kelleher D.J., Karaoglu D., Mandon E.C., Gilmore R.;
"Oligosaccharyltransferase isoforms that contain different catalytic
STT3 subunits have distinct enzymatic properties.";
Mol. Cell 12:101-111(2003).
[9]
FUNCTION.
PubMed=19167329; DOI=10.1016/j.cell.2008.11.047;
Ruiz-Canada C., Kelleher D.J., Gilmore R.;
"Cotranslational and posttranslational N-glycosylation of polypeptides
by distinct mammalian OST isoforms.";
Cell 136:272-283(2009).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-537; ASN-544 AND ASN-548.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[13]
IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE COMPLEX.
PubMed=25135935; DOI=10.1083/jcb.201404083;
Cherepanova N.A., Shrimal S., Gilmore R.;
"Oxidoreductase activity is necessary for N-glycosylation of cysteine-
proximal acceptor sites in glycoproteins.";
J. Cell Biol. 206:525-539(2014).
[14]
IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE COMPLEX.
PubMed=23606741; DOI=10.1242/jcs.115410;
Dumax-Vorzet A., Roboti P., High S.;
"OST4 is a subunit of the mammalian oligosaccharyltransferase required
for efficient N-glycosylation.";
J. Cell Sci. 126:2595-2606(2013).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[17]
VARIANT CDG1W ALA-626, AND CHARACTERIZATION OF VARIANT CDG1W ALA-626.
PubMed=23842455; DOI=10.1093/hmg/ddt312;
Shrimal S., Ng B.G., Losfeld M.E., Gilmore R., Freeze H.H.;
"Mutations in STT3A and STT3B cause two congenital disorders of
glycosylation.";
Hum. Mol. Genet. 22:4638-4645(2013).
-!- FUNCTION: Catalytic subunit of the oligosaccharyl transferase
(OST) complex that catalyzes the initial transfer of a defined
glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid
carrier dolichol-pyrophosphate to an asparagine residue within an
Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the
first step in protein N-glycosylation. N-glycosylation occurs
cotranslationally and the complex associates with the Sec61
complex at the channel-forming translocon complex that mediates
protein translocation across the endoplasmic reticulum (ER). All
subunits are required for a maximal enzyme activity. This subunit
contains the active site and the acceptor peptide and donor lipid-
linked oligosaccharide (LLO) binding pockets (By similarity).
STT3A is present in the majority of OST complexes and mediates
cotranslational N-glycosylation of most sites on target proteins,
while STT3B-containing complexes are required for efficient post-
translational glycosylation and mediate glycosylation of sites
that have been skipped by STT3A (PubMed:19167329).
{ECO:0000250|UniProtKB:P39007, ECO:0000269|PubMed:19167329}.
-!- CATALYTIC ACTIVITY: Dolichyl diphosphooligosaccharide + [protein]-
L-asparagine = dolichyl diphosphate + a glycoprotein with the
oligosaccharide chain attached by N-beta-D-glycosyl linkage to a
protein L-asparagine. {ECO:0000250|UniProtKB:P39007}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:B9KDD4};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:B9KDD4};
-!- PATHWAY: Protein modification; protein glycosylation.
{ECO:0000250|UniProtKB:P39007}.
-!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
OST exists in two different complex forms which contain common
core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either
STT3A or STT3B as catalytic subunits, and form-specific accessory
subunits. OST can form stable complexes with the Sec61 complex or
with both the Sec61 and TRAP complexes.
{ECO:0000250|UniProtKB:F1PJP5, ECO:0000269|PubMed:23606741,
ECO:0000269|PubMed:25135935, ECO:0000305}.
-!- INTERACTION:
O43187:IRAK2; NbExp=2; IntAct=EBI-719212, EBI-447733;
Q6PDS3:Sarm1 (xeno); NbExp=2; IntAct=EBI-719212, EBI-6117196;
Q86WV6:TMEM173; NbExp=2; IntAct=EBI-719212, EBI-2800345;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum
{ECO:0000269|PubMed:12887896}. Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P46978}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P46978}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P46977-1; Sequence=Displayed;
Name=2;
IsoId=P46977-2; Sequence=VSP_055106;
-!- TISSUE SPECIFICITY: Expressed at high levels in placenta, liver,
muscle and pancreas, and at very low levels in brain, lung and
kidney. Expressed in skin fibroblasts (at protein level).
{ECO:0000269|PubMed:12887896}.
-!- DOMAIN: Despite low primary sequence conservation between
eukaryotic catalytic subunits and bacterial and archaeal single
subunit OSTs (ssOST), structural comparison revealed several
common motifs at spatially equivalent positions, like the DXD
motif 1 on the external loop 1 and the DXD motif 2 on the external
loop 2 involved in binding of the metal ion cofactor and the
carboxamide group of the acceptor asparagine, the conserved Glu
residue of the TIXE/SVSE motif on the external loop 5 involved in
catalysis, as well as the WWDYG and the DK/MI motifs in the
globular domain that define the binding pocket for the +2 Ser/Thr
of the acceptor sequon. In bacterial ssOSTs, an Arg residue was
found to interact with a negatively charged side chain at the -2
position of the sequon. This Arg is conserved in bacterial enzymes
and correlates with an extended sequon requirement (Asp-X-Asn-X-
Ser/Thr) for bacterial N-glycosylation.
{ECO:0000250|UniProtKB:P39007}.
-!- DISEASE: Congenital disorder of glycosylation 1W (CDG1W)
[MIM:615596]: A form of congenital disorder of glycosylation, a
multisystem disorder caused by a defect in glycoprotein
biosynthesis and characterized by under-glycosylated serum
glycoproteins. Congenital disorders of glycosylation result in a
wide variety of clinical features, such as defects in the nervous
system development, psychomotor retardation, dysmorphic features,
hypotonia, coagulation disorders, and immunodeficiency. The broad
spectrum of features reflects the critical role of N-glycoproteins
during embryonic development, differentiation, and maintenance of
cell functions. {ECO:0000269|PubMed:23842455}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the STT3 family. {ECO:0000305}.
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EMBL; L38961; AAB05994.1; -; mRNA.
EMBL; L47337; AAL77539.1; -; mRNA.
EMBL; AK290040; BAF82729.1; -; mRNA.
EMBL; AK290657; BAF83346.1; -; mRNA.
EMBL; AK295892; BAG58686.1; -; mRNA.
EMBL; BT007100; AAP35764.1; -; mRNA.
EMBL; AP001132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471065; EAW67647.1; -; Genomic_DNA.
EMBL; BC020965; AAH20965.1; -; mRNA.
EMBL; BC048348; AAH48348.2; -; mRNA.
CCDS; CCDS60998.1; -. [P46977-2]
CCDS; CCDS8458.1; -. [P46977-1]
PIR; S70029; S70029.
RefSeq; NP_001265432.1; NM_001278503.1. [P46977-1]
RefSeq; NP_001265433.1; NM_001278504.1. [P46977-2]
RefSeq; NP_689926.1; NM_152713.4. [P46977-1]
RefSeq; XP_011541109.1; XM_011542807.2. [P46977-1]
UniGene; Hs.504237; -.
UniGene; Hs.659244; -.
ProteinModelPortal; P46977; -.
BioGrid; 109908; 26.
CORUM; P46977; -.
IntAct; P46977; 48.
MINT; P46977; -.
STRING; 9606.ENSP00000376472; -.
CAZy; GT66; Glycosyltransferase Family 66.
TCDB; 9.B.142.3.4; the integral membrane glycosyltransferase family 39 (gt39) family.
GlyConnect; 1188; -.
iPTMnet; P46977; -.
PhosphoSitePlus; P46977; -.
SwissPalm; P46977; -.
DMDM; 182676409; -.
EPD; P46977; -.
MaxQB; P46977; -.
PaxDb; P46977; -.
PeptideAtlas; P46977; -.
PRIDE; P46977; -.
ProteomicsDB; 55782; -.
DNASU; 3703; -.
Ensembl; ENST00000392708; ENSP00000376472; ENSG00000134910. [P46977-1]
Ensembl; ENST00000529196; ENSP00000436962; ENSG00000134910. [P46977-1]
Ensembl; ENST00000531491; ENSP00000432820; ENSG00000134910. [P46977-2]
GeneID; 3703; -.
KEGG; hsa:3703; -.
UCSC; uc001qcd.4; human. [P46977-1]
CTD; 3703; -.
DisGeNET; 3703; -.
EuPathDB; HostDB:ENSG00000134910.12; -.
GeneCards; STT3A; -.
HGNC; HGNC:6172; STT3A.
HPA; HPA030735; -.
MalaCards; STT3A; -.
MIM; 601134; gene.
MIM; 615596; phenotype.
neXtProt; NX_P46977; -.
OpenTargets; ENSG00000134910; -.
Orphanet; 370921; STT3A-CDG.
PharmGKB; PA29969; -.
eggNOG; KOG2292; Eukaryota.
eggNOG; COG1287; LUCA.
GeneTree; ENSGT00390000015238; -.
HOGENOM; HOG000157471; -.
HOVERGEN; HBG010606; -.
InParanoid; P46977; -.
KO; K07151; -.
OMA; SWSSFYF; -.
OrthoDB; EOG091G02DB; -.
PhylomeDB; P46977; -.
TreeFam; TF300822; -.
Reactome; R-HSA-446203; Asparagine N-linked glycosylation.
SignaLink; P46977; -.
UniPathway; UPA00378; -.
ChiTaRS; STT3A; human.
GenomeRNAi; 3703; -.
PRO; PR:P46977; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000134910; Expressed in 209 organ(s), highest expression level in body of pancreas.
CleanEx; HS_STT3A; -.
ExpressionAtlas; P46977; baseline and differential.
Genevisible; P46977; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0008250; C:oligosaccharyltransferase complex; ISS:UniProtKB.
GO; GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IMP:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043686; P:co-translational protein modification; IMP:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; IBA:GO_Central.
GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IMP:UniProtKB.
InterPro; IPR003674; Oligo_trans_STT3.
Pfam; PF02516; STT3; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome;
Congenital disorder of glycosylation; Disease mutation;
Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Magnesium;
Membrane; Metal-binding; Reference proteome; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 705 Dolichyl-diphosphooligosaccharide--
protein glycosyltransferase subunit
STT3A.
/FTId=PRO_0000072290.
TOPO_DOM 1 17 Cytoplasmic. {ECO:0000305}.
TRANSMEM 18 38 Helical. {ECO:0000255}.
TOPO_DOM 39 119 Lumenal. {ECO:0000305}.
TRANSMEM 120 138 Helical. {ECO:0000250|UniProtKB:P39007}.
TOPO_DOM 139 140 Cytoplasmic. {ECO:0000305}.
TRANSMEM 141 158 Helical. {ECO:0000250|UniProtKB:P39007}.
TOPO_DOM 159 169 Lumenal. {ECO:0000305}.
TRANSMEM 170 189 Helical. {ECO:0000250|UniProtKB:P39007}.
TOPO_DOM 190 191 Cytoplasmic. {ECO:0000305}.
TRANSMEM 192 206 Helical. {ECO:0000250|UniProtKB:P39007}.
TOPO_DOM 207 211 Lumenal. {ECO:0000305}.
TRANSMEM 212 228 Helical. {ECO:0000250|UniProtKB:P39007}.
TOPO_DOM 229 233 Cytoplasmic. {ECO:0000305}.
TRANSMEM 234 259 Helical. {ECO:0000250|UniProtKB:P39007}.
TOPO_DOM 260 267 Lumenal. {ECO:0000305}.
TRANSMEM 268 287 Helical. {ECO:0000250|UniProtKB:P39007}.
TOPO_DOM 288 300 Cytoplasmic. {ECO:0000305}.
TRANSMEM 301 321 Helical. {ECO:0000255}.
TOPO_DOM 322 356 Lumenal. {ECO:0000305}.
TRANSMEM 357 379 Helical. {ECO:0000250|UniProtKB:P39007}.
TOPO_DOM 380 385 Cytoplasmic. {ECO:0000305}.
TRANSMEM 386 402 Helical. {ECO:0000250|UniProtKB:P39007}.
TOPO_DOM 403 406 Lumenal. {ECO:0000305}.
TRANSMEM 407 428 Helical. {ECO:0000250|UniProtKB:P39007}.
TOPO_DOM 429 453 Cytoplasmic. {ECO:0000305}.
TRANSMEM 454 473 Helical. {ECO:0000250|UniProtKB:P39007}.
TOPO_DOM 474 705 Lumenal. {ECO:0000305}.
REGION 525 527 Target acceptor peptide binding.
{ECO:0000250|UniProtKB:B9KDD4}.
MOTIF 47 49 DXD motif 1.
{ECO:0000250|UniProtKB:Q5HTX9}.
MOTIF 167 169 DXD motif 2.
{ECO:0000250|UniProtKB:P39007}.
MOTIF 348 351 SVSE motif.
{ECO:0000250|UniProtKB:Q5HTX9}.
MOTIF 525 529 WWDYG motif.
{ECO:0000250|UniProtKB:P39007}.
MOTIF 592 599 DK motif. {ECO:0000250|UniProtKB:P39007}.
METAL 49 49 Manganese.
{ECO:0000250|UniProtKB:B9KDD4}.
METAL 167 167 Manganese.
{ECO:0000250|UniProtKB:B9KDD4}.
METAL 169 169 Manganese.
{ECO:0000250|UniProtKB:B9KDD4}.
BINDING 49 49 Target acceptor peptide.
{ECO:0000250|UniProtKB:B9KDD4}.
BINDING 351 351 Target acceptor peptide.
{ECO:0000250|UniProtKB:B9KDD4}.
BINDING 405 405 Lipid-linked oligosaccharide.
{ECO:0000250|UniProtKB:B9KDD4}.
BINDING 530 530 Lipid-linked oligosaccharide.
{ECO:0000250|UniProtKB:B9KDD4}.
BINDING 595 595 Target acceptor peptide.
{ECO:0000250|UniProtKB:B9KDD4}.
SITE 160 160 Important for catalytic activity.
{ECO:0000250|UniProtKB:B9KDD4}.
CARBOHYD 537 537 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 544 544 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 548 548 N-linked (GlcNAc...) (high mannose)
asparagine.
{ECO:0000269|PubMed:19159218}.
VAR_SEQ 1 92 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055106.
VARIANT 626 626 V -> A (in CDG1W; affects activity
resulting in hypoglycosylation of STT3A-
specific substrates; dbSNP:rs587777216).
{ECO:0000269|PubMed:23842455}.
/FTId=VAR_070944.
CONFLICT 61 61 A -> S (in Ref. 2; AAL77539).
{ECO:0000305}.
CONFLICT 117 117 V -> M (in Ref. 3; BAG58686).
{ECO:0000305}.
CONFLICT 128 128 T -> S (in Ref. 1; AAB05994).
{ECO:0000305}.
CONFLICT 133 133 H -> L (in Ref. 1; AAB05994).
{ECO:0000305}.
CONFLICT 252 252 M -> R (in Ref. 1; AAB05994).
{ECO:0000305}.
CONFLICT 270 270 A -> G (in Ref. 1; AAB05994).
{ECO:0000305}.
CONFLICT 415 415 C -> S (in Ref. 1; AAB05994).
{ECO:0000305}.
CONFLICT 454 454 N -> I (in Ref. 1; AAB05994).
{ECO:0000305}.
CONFLICT 494 494 G -> D (in Ref. 2; AAL77539).
{ECO:0000305}.
CONFLICT 681 681 A -> G (in Ref. 1; AAB05994).
{ECO:0000305}.
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


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