MGT4A_MOUSE
ID MGT4A_MOUSE Reviewed; 535 AA.
AC Q812G0; Q3TQT1; Q80UI0;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A {ECO:0000305};
DE EC=2.4.1.145 {ECO:0000269|PubMed:16377570};
DE AltName: Full=N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVa;
DE Short=GlcNAc-T IVa;
DE Short=GnT-IVa;
DE Short=N-acetylglucosaminyltransferase IVa;
DE AltName: Full=UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVa;
DE Contains:
DE RecName: Full=Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A soluble form;
GN Name=Mgat4a {ECO:0000312|MGI:MGI:2662992};
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 [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, DISRUPTION
RP PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=129/SvJ;
RX PubMed=16377570; DOI=10.1016/j.cell.2005.09.041;
RA Ohtsubo K., Takamatsu S., Minowa M.T., Yoshida A., Takeuchi M., Marth J.D.;
RT "Dietary and genetic control of glucose transporter 2 glycosylation
RT promotes insulin secretion in suppressing diabetes.";
RL Cell 123:1307-1321(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Egg;
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).
CC -!- FUNCTION: Glycosyltransferase that catalyze the transfer of GlcNAc from
CC UDP-GlcNAc to the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of
CC N-linked glycans through a beta1-4 linkage and participates in the
CC production of tri- and tetra-antennary N-linked sugar chains
CC (PubMed:16377570). Involved in glucose transport by mediating
CC SLC2A2/GLUT2 glycosylation, thereby controlling cell-surface expression
CC of SLC2A2 in pancreatic beta cells (PubMed:16377570).
CC {ECO:0000269|PubMed:16377570}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-
CC (1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-
CC glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-
CC (1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-
CC beta-D-Man-(1->4)-beta-D-GlcNAcl-(1->4)-beta-D-GlcNAc}-L-asparaginyl-
CC [protein] + UDP; Xref=Rhea:RHEA:16057, Rhea:RHEA-COMP:13526,
CC Rhea:RHEA-COMP:14374, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:60651, ChEBI:CHEBI:139507;
CC EC=2.4.1.145; Evidence={ECO:0000269|PubMed:16377570};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16058;
CC Evidence={ECO:0000305|PubMed:16377570};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-
CC asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) +
CC N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-
CC GlcNAc}-L-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:69615,
CC Rhea:RHEA-COMP:14369, Rhea:RHEA-COMP:17732, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60615,
CC ChEBI:CHEBI:187873; Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69616;
CC Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-
CC (1->2)-{beta-D-GlcNAc-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP-N-
CC acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-
CC D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-{beta-D-
CC GlcNAc-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC (1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:69619, Rhea:RHEA-COMP:17733, Rhea:RHEA-COMP:17734,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:187874, ChEBI:CHEBI:187875;
CC Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69620;
CC Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-D-Fuc-(1->6)]-
CC beta-D-GlcNAc}-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-
CC glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-
CC (1->4)]-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-[alpha-D-Fuc-(1->6)]-beta-D-GlcNAc}-asparaginyl-
CC [protein] + UDP; Xref=Rhea:RHEA:69623, Rhea:RHEA-COMP:17735,
CC Rhea:RHEA-COMP:17736, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:187876, ChEBI:CHEBI:187877;
CC Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69624;
CC Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man-
CC (1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP-N-
CC acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-Gal-(1->4)-beta-D-
CC GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-
CC GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC (1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:69627, Rhea:RHEA-COMP:17737, Rhea:RHEA-COMP:17738,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:187878, ChEBI:CHEBI:187879;
CC Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69628;
CC Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->3)-{alpha-D-Man-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP-N-
CC acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-
CC D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-{alpha-D-Man-
CC (1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC beta-D-GlcNAc}-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:69631,
CC Rhea:RHEA-COMP:17739, Rhea:RHEA-COMP:17740, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:187880,
CC ChEBI:CHEBI:187881; Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69632;
CC Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-beta-D-Man-
CC (1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] +
CC UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-
CC [beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-
CC GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:69635, Rhea:RHEA-COMP:17741, Rhea:RHEA-COMP:17742,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:187882, ChEBI:CHEBI:187883;
CC Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69636;
CC Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:O77836};
CC -!- ACTIVITY REGULATION: Inhibited by UDP. {ECO:0000250|UniProtKB:O77836}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:16377570}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9D4R2}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q9D4R2}.
CC -!- SUBCELLULAR LOCATION: [Alpha-1,3-mannosyl-glycoprotein 4-beta-N-
CC acetylglucosaminyltransferase A soluble form]: Secreted
CC {ECO:0000250|UniProtKB:O77836}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q812G0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q812G0-2; Sequence=VSP_025715;
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:O77836}.
CC -!- DISRUPTION PHENOTYPE: Mice display impaired beta cell glucose transport
CC and insulin secretion causing type 2 diabete. This is due to defects in
CC SLC2A2/Glut-2 glycosylation, provoking SLC2A2/Glut-2 endocytosis with
CC redistribution into endosomes and lysosomes.
CC {ECO:0000269|PubMed:16377570}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 54 family.
CC {ECO:0000305}.
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DR EMBL; AB053217; BAC55018.1; -; mRNA.
DR EMBL; AB053225; BAC55085.1; -; Genomic_DNA.
DR EMBL; AK163327; BAE37301.1; -; mRNA.
DR CCDS; CCDS14893.1; -. [Q812G0-1]
DR CCDS; CCDS69882.1; -. [Q812G0-2]
DR RefSeq; NP_001277730.1; NM_001290801.1. [Q812G0-2]
DR RefSeq; NP_776295.1; NM_173870.3. [Q812G0-1]
DR RefSeq; XP_006496085.1; XM_006496022.3. [Q812G0-1]
DR RefSeq; XP_011236828.1; XM_011238526.2. [Q812G0-2]
DR AlphaFoldDB; Q812G0; -.
DR STRING; 10090.ENSMUSP00000114175; -.
DR CAZy; GT54; Glycosyltransferase Family 54.
DR GlyGen; Q812G0; 2 sites.
DR PhosphoSitePlus; Q812G0; -.
DR EPD; Q812G0; -.
DR MaxQB; Q812G0; -.
DR PaxDb; Q812G0; -.
DR PRIDE; Q812G0; -.
DR ProteomicsDB; 295659; -. [Q812G0-1]
DR ProteomicsDB; 295660; -. [Q812G0-2]
DR Antibodypedia; 32749; 91 antibodies from 23 providers.
DR DNASU; 269181; -.
DR Ensembl; ENSMUST00000042161; ENSMUSP00000038894; ENSMUSG00000026110. [Q812G0-1]
DR Ensembl; ENSMUST00000151952; ENSMUSP00000114175; ENSMUSG00000026110. [Q812G0-1]
DR Ensembl; ENSMUST00000154819; ENSMUSP00000121181; ENSMUSG00000026110. [Q812G0-2]
DR GeneID; 269181; -.
DR KEGG; mmu:269181; -.
DR UCSC; uc007arr.2; mouse. [Q812G0-1]
DR UCSC; uc007aru.2; mouse. [Q812G0-2]
DR CTD; 11320; -.
DR MGI; MGI:2662992; Mgat4a.
DR VEuPathDB; HostDB:ENSMUSG00000026110; -.
DR eggNOG; ENOG502QPQJ; Eukaryota.
DR GeneTree; ENSGT00940000159177; -.
DR InParanoid; Q812G0; -.
DR OMA; ERIRWRT; -.
DR OrthoDB; 593094at2759; -.
DR PhylomeDB; Q812G0; -.
DR TreeFam; TF324570; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR Reactome; R-MMU-975577; N-Glycan antennae elongation.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 269181; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Mgat4a; mouse.
DR PRO; PR:Q812G0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q812G0; protein.
DR Bgee; ENSMUSG00000026110; Expressed in left colon and 205 other tissues.
DR ExpressionAtlas; Q812G0; baseline and differential.
DR Genevisible; Q812G0; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IDA:MGI.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; ISS:UniProtKB.
DR GO; GO:0008454; F:alpha-1,3-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0046487; P:glyoxylate metabolic process; ISS:UniProtKB.
DR GO; GO:0006491; P:N-glycan processing; IDA:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IGI:MGI.
DR InterPro; IPR006759; Glyco_transf_54.
DR PANTHER; PTHR12062; PTHR12062; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Secreted; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..535
FT /note="Alpha-1,3-mannosyl-glycoprotein 4-beta-N-
FT acetylglucosaminyltransferase A"
FT /id="PRO_0000288585"
FT CHAIN 93..535
FT /note="Alpha-1,3-mannosyl-glycoprotein 4-beta-N-
FT acetylglucosaminyltransferase A soluble form"
FT /evidence="ECO:0000250|UniProtKB:O77836"
FT /id="PRO_0000288586"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..535
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT COILED 28..63
FT /evidence="ECO:0000255"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UM21"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 79..88
FT /note="SKTALSTISD -> N (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025715"
FT CONFLICT 487
FT /note="F -> S (in Ref. 2; BAE37301)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="G -> A (in Ref. 2; BAE37301)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="W -> R (in Ref. 2; BAE37301)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 61480 MW; D6E0CA37825795C2 CRC64;
MRLRNGTVAT ALVFVTSFLT LSWYTTWQNG KEKLIAYQRE FLALKERLRV AEHRISQRSS
ELNTIVQQFR RAGAETNGSK TALSTISDNT IKLLKELTSK KSLRVPSIYY HLPHLLQNER
SLQPAVQIGS GRTGVSIVMG IPTVKREVKS YLVETLHSLI DNLYPEEKLD CVIVVFIGET
DLDYVHSVVA NLEKEFSREI SSGLLEIISP PESYYPDLTN LKETFGDSKE RVRWRTKQNL
DYCFLMMYAQ EKGIYYIQLE DDIIVKQNYF NTIKNFALQL SSEEWMILEF SQLGFIGKMF
QAPDLALVVE FILMFYKEKP IDWLLDHILW VKVCNPEKDA KHCDRQKANL RIRFRPSLFQ
HVGLHSSLSG KIQKLTDKDY MKPLLLKVHV NPPAEVSTSL KVYQGHTLEK TYMGEDFFWA
ITPTAGDYIL FKFDKPVNVE SYLFHSGNQE HPGDILLNTT VDVLPLKSDS LEISKETKDK
RLEDGYFRIG KFEYGVAEGI VDPGLNPISA FRLSVIQNSA VWAILNEIHI KKVTS
