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Protein

Glycosyltransferase-like protein LARGE2

Gene

Gyltl1b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Bifunctional glycosyltransferase with both xylosyltransferase and beta-1,3-glucuronyltransferase activities involved in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1). Phosphorylated O-mannosyl trisaccharid is required for binding laminin G-like domain-containing extracellular proteins with high affinity. Elongates the glucuronyl-beta-1,4-xylose-beta disaccharide primer structure by adding repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-] to produce a heteropolysaccharide. Has a higher activity toward alpha-dystroglycan than LARGE (PubMed:15958417).4 Publications

Cofactori

Mn2+By similarityNote: Binds 2 Mn2+ ions per subunit. The xylosyltransferase part binds one Mn2+ and the beta-1,3-glucuronyltransferase part binds one Mn2+.By similarity

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.2 Publications
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi172 – 1721Manganese 1By similarity
Metal bindingi174 – 1741Manganese 1By similarity
Metal bindingi492 – 4921Manganese 2By similarity
Metal bindingi494 – 4941Manganese 2By similarity

GO - Molecular functioni

  • dystroglycan binding Source: MGI
  • glucuronosyltransferase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • transferase activity, transferring glycosyl groups Source: MGI
  • xylosyltransferase activity Source: UniProtKB

GO - Biological processi

  • protein O-linked mannosylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-5173105. O-linked glycosylation.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT49. Glycosyltransferase Family 49.
GT8. Glycosyltransferase Family 8.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycosyltransferase-like protein LARGE2 (EC:2.4.-.-)
Alternative name(s):
Glycosyltransferase-like 1B
Including the following 2 domains:
Xylosyltransferase LARGE2Curated (EC:2.4.2.-2 Publications)
Beta-1,3-glucuronyltransferase LARGE2Curated (EC:2.4.1.-2 Publications)
Gene namesi
Name:Gyltl1b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:2443769. Gyltl1b.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88CytoplasmicSequence analysis
Transmembranei9 – 2921Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini30 – 690661LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 690690Glycosyltransferase-like protein LARGE2PRO_0000226812Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi51 – 511N-linked (GlcNAc...)Sequence analysis
Glycosylationi78 – 781N-linked (GlcNAc...)Sequence analysis
Glycosylationi202 – 2021N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ5XPT3.
PaxDbiQ5XPT3.
PRIDEiQ5XPT3.

PTM databases

iPTMnetiQ5XPT3.
PhosphoSiteiQ5XPT3.

Expressioni

Tissue specificityi

Highly expressed in the testis and kidney, but weakly expressed in the heart and brain. Expressed during embryogenesis from 7 dpc.1 Publication

Gene expression databases

BgeeiQ5XPT3.
CleanExiMM_GYLTL1B.
ExpressionAtlasiQ5XPT3. baseline and differential.
GenevisibleiQ5XPT3. MM.

Interactioni

Subunit structurei

Interacts with B3GNT1/B4GAT1.By similarity

GO - Molecular functioni

  • dystroglycan binding Source: MGI

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000064128.

Structurei

3D structure databases

ProteinModelPortaliQ5XPT3.
SMRiQ5XPT3. Positions 67-316.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni68 – 343276Xylosyltransferase activityBy similarityAdd
BLAST
Regioni344 – 686343Glucuronyltransferase activityBy similarityAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the glycosyltransferase 49 family.Curated
In the N-terminal section; belongs to the glycosyltransferase 8 family.Curated
Belongs to the glycosyltransferase 8 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3765. Eukaryota.
ENOG410XRNY. LUCA.
GeneTreeiENSGT00530000063165.
HOGENOMiHOG000231467.
HOVERGENiHBG052308.
InParanoidiQ5XPT3.
KOiK09668.
TreeFamiTF319168.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR002495. Glyco_trans_8.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF01501. Glyco_transf_8. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5XPT3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLPRGRPRAM GAAVLLLLLL LVVGFFLFGR DPDYGLGTTA TLDEDPYRSR
60 70 80 90 100
NLSASSPQLL LPPKCEMLHV AIVCAGYNSS REIITLTKSL LFYRKNPLHL
110 120 130 140 150
HLITDAVARN ILETLFRTWM VPAVVVSFYD AEELKPLVSW IPNKHYSGLY
160 170 180 190 200
GLMKLVLPSI LPPSLARVIV LDTDVTFSSD IVELWALFDH FSDKQVVGLV
210 220 230 240 250
ENQSDWYLGN LWKNHRPWPA LGRGFNTGVI LLWLDRLQQT GWEQMWKVTA
260 270 280 290 300
KRELLTLMAT SLADQDIFNA VIKEHPHLVH PLPCVWNVQL SDHTRAERCY
310 320 330 340 350
LEAADLKVIH WNSPKKLRVK NKHAEFFRNL HLTFLGYDGK LLRRELFGCP
360 370 380 390 400
NQFPPGAEQL QQALTQLDEE EPCFEFRQQQ LTVHRVHITF LPHQPPPPQP
410 420 430 440 450
HDVTLVAQLS MDRLQMLEAL CRHWPGPMSL ALYLTDEEAQ QFLHFVETSP
460 470 480 490 500
VLSMRKDVAY HVVYRDGPLY PVNQLRNVAL AQALTPYVFL SDIDFLPAYS
510 520 530 540 550
LYDYLRASIE QLELDSRRKT ALVVPAFETL HYRFSFPNSK AELLTLLDAG
560 570 580 590 600
SLHTFRYHEW PQGHSSTDYS RWREAQAPYS VQWSADYEPY VVVPRDCPRY
610 620 630 640 650
DPRFVGFGWN KVAHIIELDA QEYEFLVLPE AFSIHLPHAP SLDISRFRSS
660 670 680 690
PTYRNCLQAL KEEFHQDLSR RYGSAALKYL TALQQARSRA
Length:690
Mass (Da):79,514
Last modified:November 23, 2004 - v1
Checksum:i76AE2A4E8B87930E
GO
Isoform 2 (identifier: Q5XPT3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     193-227: Missing.

Show »
Length:655
Mass (Da):75,436
Checksum:i8C73CC720C73B69B
GO
Isoform 3 (identifier: Q5XPT3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     67-76: MLHVAIVCAG → EKSAAPPPDN
     77-690: Missing.

Note: No experimental confirmation available. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:76
Mass (Da):8,209
Checksum:iAB9633F7594B02F7
GO

Sequence cautioni

The sequence BAC36913.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti144 – 1441K → N in BAC36913 (PubMed:16141072).Curated
Sequence conflicti580 – 5801S → R in AAH33922 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei67 – 7610MLHVAIVCAG → EKSAAPPPDN in isoform 3. 1 PublicationVSP_041607
Alternative sequencei77 – 690614Missing in isoform 3. 1 PublicationVSP_041608Add
BLAST
Alternative sequencei193 – 22735Missing in isoform 2. 1 PublicationVSP_017489Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY742914 mRNA. Translation: AAU95213.1.
AY742915 mRNA. Translation: AAU95214.1.
AK077630 mRNA. Translation: BAC36913.1. Sequence problems.
AL731709 Genomic DNA. Translation: CAM20620.1.
BC033922 mRNA. Translation: AAH33922.1.
BC096655 mRNA. Translation: AAH96655.1.
CCDSiCCDS16443.2. [Q5XPT3-1]
CCDS50646.1. [Q5XPT3-2]
RefSeqiNP_001160105.1. NM_001166633.2. [Q5XPT3-2]
NP_001277702.1. NM_001290773.1.
NP_001277703.1. NM_001290774.1.
NP_001277704.1. NM_001290775.1.
NP_766258.2. NM_172670.3. [Q5XPT3-1]
UniGeneiMm.31158.

Genome annotation databases

EnsembliENSMUST00000068586; ENSMUSP00000064128; ENSMUSG00000040434. [Q5XPT3-1]
ENSMUST00000090582; ENSMUSP00000088070; ENSMUSG00000040434. [Q5XPT3-2]
ENSMUST00000176289; ENSMUSP00000135118; ENSMUSG00000040434. [Q5XPT3-3]
GeneIDi228366.
KEGGimmu:228366.
UCSCiuc008kxn.3. mouse. [Q5XPT3-1]
uc008kxp.3. mouse. [Q5XPT3-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY742914 mRNA. Translation: AAU95213.1.
AY742915 mRNA. Translation: AAU95214.1.
AK077630 mRNA. Translation: BAC36913.1. Sequence problems.
AL731709 Genomic DNA. Translation: CAM20620.1.
BC033922 mRNA. Translation: AAH33922.1.
BC096655 mRNA. Translation: AAH96655.1.
CCDSiCCDS16443.2. [Q5XPT3-1]
CCDS50646.1. [Q5XPT3-2]
RefSeqiNP_001160105.1. NM_001166633.2. [Q5XPT3-2]
NP_001277702.1. NM_001290773.1.
NP_001277703.1. NM_001290774.1.
NP_001277704.1. NM_001290775.1.
NP_766258.2. NM_172670.3. [Q5XPT3-1]
UniGeneiMm.31158.

3D structure databases

ProteinModelPortaliQ5XPT3.
SMRiQ5XPT3. Positions 67-316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000064128.

Protein family/group databases

CAZyiGT49. Glycosyltransferase Family 49.
GT8. Glycosyltransferase Family 8.

PTM databases

iPTMnetiQ5XPT3.
PhosphoSiteiQ5XPT3.

Proteomic databases

MaxQBiQ5XPT3.
PaxDbiQ5XPT3.
PRIDEiQ5XPT3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000068586; ENSMUSP00000064128; ENSMUSG00000040434. [Q5XPT3-1]
ENSMUST00000090582; ENSMUSP00000088070; ENSMUSG00000040434. [Q5XPT3-2]
ENSMUST00000176289; ENSMUSP00000135118; ENSMUSG00000040434. [Q5XPT3-3]
GeneIDi228366.
KEGGimmu:228366.
UCSCiuc008kxn.3. mouse. [Q5XPT3-1]
uc008kxp.3. mouse. [Q5XPT3-2]

Organism-specific databases

CTDi120071.
MGIiMGI:2443769. Gyltl1b.

Phylogenomic databases

eggNOGiKOG3765. Eukaryota.
ENOG410XRNY. LUCA.
GeneTreeiENSGT00530000063165.
HOGENOMiHOG000231467.
HOVERGENiHBG052308.
InParanoidiQ5XPT3.
KOiK09668.
TreeFamiTF319168.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiR-MMU-5173105. O-linked glycosylation.

Miscellaneous databases

ChiTaRSiGyltl1b. mouse.
PROiQ5XPT3.
SOURCEiSearch...

Gene expression databases

BgeeiQ5XPT3.
CleanExiMM_GYLTL1B.
ExpressionAtlasiQ5XPT3. baseline and differential.
GenevisibleiQ5XPT3. MM.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR002495. Glyco_trans_8.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF01501. Glyco_transf_8. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the LARGE family of putative glycosyltransferases associated with dystroglycanopathies."
    Grewal P.K., McLaughlan J.M., Moore C.J., Browning C.A., Hewitt J.E.
    Glycobiology 15:912-923(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: C57BL/6J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Strain: C57BL/6J.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: Czech II.
    Tissue: Lung and Mammary tumor.
  5. "Xylosyl- and glucuronyltransferase functions of LARGE in alpha-dystroglycan modification are conserved in LARGE2."
    Inamori K., Hara Y., Willer T., Anderson M.E., Zhu Z., Yoshida-Moriguchi T., Campbell K.P.
    Glycobiology 23:295-302(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PATHWAY.
  6. "LARGE2 generates the same xylose- and glucuronic acid-containing glycan structures as LARGE."
    Ashikov A., Buettner F.F., Tiemann B., Gerardy-Schahn R., Bakker H.
    Glycobiology 23:303-309(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PATHWAY.
  7. "Endogenous glucuronyltransferase activity of LARGE or LARGE2 required for functional modification of alpha-dystroglycan in cells and tissues."
    Inamori K., Willer T., Hara Y., Venzke D., Anderson M.E., Clarke N.F., Guicheney P., Bonnemann C.G., Moore S.A., Campbell K.P.
    J. Biol. Chem. 289:28138-28148(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiLARG2_MOUSE
AccessioniPrimary (citable) accession number: Q5XPT3
Secondary accession number(s): A2AHG9
, Q5XPT2, Q8BJZ8, Q8K253
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: November 23, 2004
Last modified: June 8, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.