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Q9ES89 (EXTL2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Exostosin-like 2

EC=2.4.1.223
Alternative name(s):
Alpha-1,4-N-acetylhexosaminyltransferase EXTL2
Alpha-GalNAcT EXTL2
EXT-related protein 2
Glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase
Gene names
Name:Extl2
Synonyms:Extr2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Glycosyltransferase required for the biosynthesis of heparan-sulfate and responsible for the alternating addition of beta-1-4-linked glucuronic acid (GlcA) and alpha-1-4-linked N-acetylglucosamine (GlcNAc) units to nascent heparan sulfate chains By similarity.

Catalytic activity

UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl-proteoglycan = UDP + alpha-N-acetyl-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl-proteoglycan.

Pathway

Glycan metabolism; heparan sulfate biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Single-pass type II membrane protein By similarity.

Sequence similarities

Belongs to the glycosyltransferase 47 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 330330Exostosin-like 2
PRO_0000149656

Regions

Topological domain1 – 2121Cytoplasmic Potential
Transmembrane22 – 4221Helical; Signal-anchor for type II membrane protein; Potential
Topological domain43 – 330288Lumenal Potential

Sites

Metal binding1531Manganese; catalytic

Amino acid modifications

Glycosylation751N-linked (GlcNAc...) Potential
Disulfide bond244 ↔ 296 Ref.4

Experimental info

Sequence conflict1911Y → D in BAB31683. Ref.2

Secondary structure

.............................................. 330
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9ES89 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 51F88BE5D3E5EADF

FASTA33037,391
        10         20         30         40         50         60 
MMRGCHICKL PGRVMGIRVL RFSLVVILVL LLVAGALTNL LPNIKEDKML TLRREIKSPS 

        70         80         90        100        110        120 
KSALDSFTLI MQTYNRTDLL LRLLNHYQAV PSLHKVIVVW NNVGEKGPEE LWNSLGPHPI 

       130        140        150        160        170        180 
PVIFKPQTAN KMRNRLQVFP EVETNAVLMV DDDTLISAQD LVFAFSIWQQ FPDQIIGFVP 

       190        200        210        220        230        240 
RKHVSTSSGI YSYGGFELQT PGPGNGDQYS MVLIGASFFN SKYLELFQKQ PAAVHALIDE 

       250        260        270        280        290        300 
TQNCDDIAMN FLVTRHTGKP SGIFVKPINM VNLEKETNGY SGMWHRAEHF LQRSYCINKL 

       310        320        330 
VNIYDGMPLK YSNIMISQFG FPYANHKSKM 

« Hide

References

« Hide 'large scale' references
[1]"Characterization and genomic localization of the mouse Extl2 gene."
Wuyts W., Van Hul W.
Cytogenet. Cell Genet. 89:185-188(2000) [PubMed: 10965119] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryonic head.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Eye and Mammary gland.
[4]"Crystal structure of an alpha 1,4-N-acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis."
Pedersen L.C., Dong J., Taniguchi F., Kitagawa H., Krahn J.M., Pedersen L.G., Sugahara K., Negishi M.
J. Biol. Chem. 278:14420-14428(2003) [PubMed: 12562774] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 38-330, METAL-BINDING, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF200973 mRNA. Translation: AAG17542.1.
AK019370 mRNA. Translation: BAB31683.2.
BC031438 mRNA. Translation: AAH31438.1.
BC094444 mRNA. Translation: AAH94444.1.
IPIIPI00112900.
RefSeqNP_001156986.1. NM_001163514.1.
NP_067363.3. NM_021388.4.
UniGeneMm.41739.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OMXX-ray2.40A/B38-330[»]
1OMZX-ray2.10A/B38-330[»]
1ON6X-ray2.30A/B38-330[»]
1ON8X-ray2.70A/B38-330[»]
ProteinModelPortalQ9ES89.
SMRQ9ES89. Positions 63-327.
DisProtDP00397.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9ES89.

Protein family/group databases

CAZyGT64. Glycosyltransferase Family 64.

Proteomic databases

PRIDEQ9ES89.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029575; ENSMUSP00000029575; ENSMUSG00000027963.
ENSMUST00000106502; ENSMUSP00000102111; ENSMUSG00000027963.
GeneID58193.
KEGGmmu:58193.
UCSCuc008rbu.2. mouse.

Organism-specific databases

CTD2135.
MGIMGI:1889574. Extl2.

Phylogenomic databases

GeneTreeENSGT00550000074496.
HOGENOMHBG713996.
HOVERGENHBG051525.
InParanoidQ9ES89.
OMANHYQAVP.
OrthoDBEOG4RNB91.
PhylomeDBQ9ES89.

Gene expression databases

ArrayExpressQ9ES89.
BgeeQ9ES89.
CleanExMM_EXTL2.
GenevestigatorQ9ES89.
GermOnlineENSMUSG00000027963. Mus musculus.

Family and domain databases

InterProIPR015338. HexNAc_Trfase_a.
[Graphical view]
KOK02369.
PfamPF09258. Glyco_transf_64. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

SOURCESearch...

Entry information

Entry nameEXTL2_MOUSE
AccessionPrimary (citable) accession number: Q9ES89
Secondary accession number(s): Q505Q8, Q9CX90
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: March 1, 2001
Last modified: November 16, 2011
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families