STT3B_MOUSE
ID STT3B_MOUSE Reviewed; 823 AA.
AC Q3TDQ1; Q7TT24; Q921E3; Q99LL0; Q9D2V2;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B {ECO:0000305};
DE Short=Oligosaccharyl transferase subunit STT3B;
DE Short=STT3-B;
DE EC=2.4.99.18;
DE AltName: Full=B6dom1 antigen;
DE AltName: Full=Source of immunodominant MHC-associated peptides;
GN Name=Stt3b {ECO:0000312|MGI:MGI:1915542}; Synonyms=Simp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, Czech II, and FVB/N;
RC TISSUE=Brain, Mammary gland, and Mammary tumor;
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 [3]
RP PROTEIN SEQUENCE OF 770-778, AND VARIANT ASP-776.
RC STRAIN=C57BL/6J;
RX PubMed=12439619; DOI=10.1007/s00251-002-0502-4;
RA McBride K., Baron C., Picard S., Martin S., Boismenu D., Bell A.,
RA Bergeron J., Perreault C.;
RT "The model B6dom1 minor histocompatibility antigen is encoded by a mouse
RT homolog of the yeast STT3 gene.";
RL Immunogenetics 54:562-569(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495 AND SER-496, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495 AND SER-496, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-624 AND ASN-638.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-29; SER-495 AND
RP SER-496, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). 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). STT3B is present
CC in a small subset of OST complexes and mediates both cotranslational
CC and post-translational N-glycosylation of target proteins: STT3B-
CC containing complexes are required for efficient post-translational
CC glycosylation and while they are less competent than STT3A-containing
CC complexes for cotranslational glycosylation, they have the ability to
CC mediate glycosylation of some nascent sites that are not accessible for
CC STT3A. STT3B-containing complexes also act post-translationally and
CC mediate modification of skipped glycosylation sites in unfolded
CC proteins. Plays a role in ER-associated degradation (ERAD) pathway that
CC mediates ubiquitin-dependent degradation of misfolded endoplasmic
CC reticulum proteins by mediating N-glycosylation of unfolded proteins,
CC which are then recognized by the ERAD pathway and targeted for
CC degradation (By similarity). {ECO:0000250|UniProtKB:E2RG47,
CC ECO:0000250|UniProtKB:P39007, ECO:0000250|UniProtKB:Q8TCJ2}.
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:0000250|UniProtKB:Q8TCJ2};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:B9KDD4};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q8TCJ2}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex (By
CC similarity). OST exists in two different complex forms which contain
CC common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either
CC STT3A or STT3B as catalytic subunits, and form-specific accessory
CC subunits (By similarity). OST can form stable complexes with the Sec61
CC complex or with both the Sec61 and TRAP complexes (By similarity).
CC {ECO:0000250|UniProtKB:E2RG47, ECO:0000250|UniProtKB:Q8TCJ2}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8TCJ2}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P39007}.
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 -!- POLYMORPHISM: In strains 129, C57BL/10, C57BL/6 and LP Glu-776
CC correlates with a B6dom1-positive phenotype, Asp-776 is found in
CC resistant strains. The B6dom1 minor histocompatibility antigen (MiHA)
CC is used as a model antigen in studying immunodominance.
CC -!- SIMILARITY: Belongs to the STT3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH13054.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK018758; BAB31390.1; -; mRNA.
DR EMBL; AK145674; BAE26582.1; -; mRNA.
DR EMBL; AK154979; BAE32968.1; -; mRNA.
DR EMBL; AK152899; BAE31580.1; -; mRNA.
DR EMBL; AK170079; BAE41550.1; -; mRNA.
DR EMBL; BC003206; AAH03206.1; -; mRNA.
DR EMBL; BC013054; AAH13054.2; ALT_INIT; mRNA.
DR EMBL; BC052433; AAH52433.1; -; mRNA.
DR CCDS; CCDS23599.1; -.
DR RefSeq; NP_077184.2; NM_024222.2.
DR AlphaFoldDB; Q3TDQ1; -.
DR SMR; Q3TDQ1; -.
DR BioGRID; 212788; 4.
DR ComplexPortal; CPX-5822; Oligosaccharyltransferase complex B.
DR STRING; 10090.ENSMUSP00000035010; -.
DR CAZy; GT66; Glycosyltransferase Family 66.
DR GlyConnect; 2265; 3 N-Linked glycans (2 sites).
DR GlyGen; Q3TDQ1; 4 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; Q3TDQ1; -.
DR PhosphoSitePlus; Q3TDQ1; -.
DR SwissPalm; Q3TDQ1; -.
DR EPD; Q3TDQ1; -.
DR jPOST; Q3TDQ1; -.
DR MaxQB; Q3TDQ1; -.
DR PaxDb; Q3TDQ1; -.
DR PeptideAtlas; Q3TDQ1; -.
DR PRIDE; Q3TDQ1; -.
DR ProteomicsDB; 258767; -.
DR DNASU; 68292; -.
DR GeneID; 68292; -.
DR KEGG; mmu:68292; -.
DR UCSC; uc009ryp.1; mouse.
DR CTD; 201595; -.
DR MGI; MGI:1915542; Stt3b.
DR eggNOG; KOG2292; Eukaryota.
DR InParanoid; Q3TDQ1; -.
DR OrthoDB; 187775at2759; -.
DR PhylomeDB; Q3TDQ1; -.
DR TreeFam; TF300822; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 68292; 15 hits in 77 CRISPR screens.
DR ChiTaRS; Stt3b; mouse.
DR PRO; PR:Q3TDQ1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3TDQ1; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
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:0008250; C:oligosaccharyltransferase complex; ISO:MGI.
DR GO; GO:0034998; C:oligosaccharyltransferase I complex; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043686; P:co-translational protein modification; ISS:UniProtKB.
DR GO; GO:0006516; P:glycoprotein catabolic process; ISS:UniProtKB.
DR GO; GO:0043687; P:post-translational protein modification; ISS:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISO:MGI.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISS:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR InterPro; IPR003674; Oligo_trans_STT3.
DR PANTHER; PTHR13872; PTHR13872; 1.
DR Pfam; PF02516; STT3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Endoplasmic reticulum;
KW Glycoprotein; Glycosyltransferase; Magnesium; Manganese; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8TCJ2"
FT CHAIN 2..823
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit STT3B"
FT /id="PRO_0000246002"
FT TOPO_DOM 2..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 42..83
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 84..170
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 171..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..209
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 210..220
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 221..240
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 241..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 243..257
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 258..262
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 263..279
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 280..284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 285..310
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 311..318
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 319..338
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 339..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..407
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 408..430
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 431..436
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 437..453
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 454..457
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 458..479
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 480..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 524..549
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 550..823
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..603
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT MOTIF 98..100
FT /note="DXD motif 1"
FT /evidence="ECO:0000250|UniProtKB:Q5HTX9"
FT MOTIF 218..220
FT /note="DXD motif 2"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT MOTIF 399..402
FT /note="SVSE motif"
FT /evidence="ECO:0000250|UniProtKB:Q5HTX9"
FT MOTIF 601..605
FT /note="WWDYG motif"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT MOTIF 668..675
FT /note="DK motif"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT COMPBIAS 9..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 218
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 220
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 456
FT /ligand="dolichyl diphosphooligosaccharide"
FT /ligand_id="ChEBI:CHEBI:57570"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 606
FT /ligand="dolichyl diphosphooligosaccharide"
FT /ligand_id="ChEBI:CHEBI:57570"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 100
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 211
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 402
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 671
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8TCJ2"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TCJ2"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT CARBOHYD 613
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 624
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT VARIANT 776
FT /note="E -> D (in strain: A.BY, B10.H7 and C3H.SW;
FT correlated with B6dom1-negative phenotype)"
FT /evidence="ECO:0000269|PubMed:12439619"
FT CONFLICT 43
FT /note="S -> R (in Ref. 1; BAE41550 and 2; AAH03206)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="T -> I (in Ref. 1; BAE41550)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="F -> L (in Ref. 1; BAB31390)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 823 AA; 93246 MW; BBC27DB07EE609D1 CRC64;
MAEPSAPESK HKSSLNSSPW SGLMALGNSR HGHHGPGTQS ASSAAAPKPG PPAGLSGGLS
QPAGWQSLLS FTILFLAWLA GFSSRLFAVI RFESIIHEFD PWFNYRSTHH LASHGFYEFL
NWFDERAWYP LGRIVGGTVY PGLMITAGLI HWILNTLNIT VHIRDVCVFL APTFSGLTSI
STFLLTRELW NQGAGLLAAC FIAIVPGYIS RSVAGSFDNE GIAIFALQFT YYLWVKSVKT
GSVFWTMCCC LSYFYMVSAW GGYVFIINLI PLHVFVLLLM QRYSKRVYIA YSTFYIVGLI
LSMQIPFVGF QPIRTSEHMA AAGVFALLQA YAFLQYLRDR LTKQEFQTLF FLGVSLAAGA
VFLSVIYLTY TGYIAPWSGR FYSLWDTGYA KIHIPIIASV SEHQPTTWVS FFFDLHILVC
TFPAGLWFCI KNINDERVFV ALYAISAVYF AGVMVRLMLT LTPVVCMLSA IAFSNVFEHY
LGDDMKRENP PVEDSSDEDD KRNPGNLYDK AGKVRKHVTE QEKPEEGLGP NIKSIVTMLM
LMLLMMFAVH CTWVTSNAYS SPSVVLASYN HDGTRNILDD FREAYFWLRQ NTDEHARVMS
WWDYGYQIAG MANRTTLVDN NTWNNSHIAL VGKAMSSNET AAYKIMRSLD VDYVLVIFGG
VIGYSGDDIN KFLWMVRIAE GEHPKDIREG DYFTQQGEFR VDKAGSPTLL NCLMYKMSYY
RFGEMQLDFR TPPGFDRTRN AEIGNKDIKF KHLEEAFTSE HWLVRIYKVK APDNRETLGH
KPRVTNIVPK QKYLSKKTTK RKRGYVKNKL VFKKGKKTSK KTV
