Q9ES89 (EXTL2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	330 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Manganese Metal-binding
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intrinsic to endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro
Molecular function	glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 330

330

Exostosin-like 2

PRO_0000149656

Regions

Topological domain

1 – 21

21

Cytoplasmic Potential

Transmembrane

22 – 42

21

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

43 – 330

288

Lumenal Potential

Sites

Metal binding

153

1

Manganese; catalytic

Amino acid modifications

Glycosylation

75

1

N-linked (GlcNAc...) Potential

Disulfide bond

244 ↔ 296

Ref.4

Experimental info

Sequence conflict

191

1

Y → D in BAB31683. Ref.2

Secondary structure

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330

Helix Strand Turn

Details...

Beta strand

67 – 73

7

Helix

77 – 87

11

Beta strand

93 – 101

9

Helix

109 – 114

6

Beta strand

122 – 127

6

Helix

129 – 132

4

Beta strand

144 – 151

8

Helix

158 – 170

13

Beta strand

174 – 178

5

Beta strand

180 – 187

8

Beta strand

190 – 194

5

Beta strand

202 – 206

5

Beta strand

209 – 212

4

Beta strand

217 – 220

4

Helix

222 – 228

7

Helix

232 – 240

9

Beta strand

241 – 243

3

Helix

245 – 257

13

Beta strand

261 – 265

5

Beta strand

268 – 271

4

Helix

290 – 304

15

Beta strand

314 – 318

5

Turn

323 – 326

4

Sequences

	Sequence		Length	Mass (Da)
	Q9ES89 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 51F88BE5D3E5EADF	FASTA	330	37,391
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

IPI

IPI00112900.

RefSeq

NP_001156986.1. NM_001163514.1.
NP_067363.3. NM_021388.4.

UniGene

Mm.41739.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OMX	X-ray	2.40	A/B	38-330	[»]
1OMZ	X-ray	2.10	A/B	38-330	[»]
1ON6	X-ray	2.30	A/B	38-330	[»]
1ON8	X-ray	2.70	A/B	38-330	[»]

ProteinModelPortal

Q9ES89.

SMR

Q9ES89. Positions 63-327.

DisProt

DP00397.

ModBase

Search...

Protein-protein interaction databases

STRING

Q9ES89.

Protein family/group databases

CAZy

GT64. Glycosyltransferase Family 64.

Proteomic databases

PRIDE

Q9ES89.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000029575; ENSMUSP00000029575; ENSMUSG00000027963.
ENSMUST00000106502; ENSMUSP00000102111; ENSMUSG00000027963.

GeneID

58193.

KEGG

mmu:58193.

UCSC

uc008rbu.2. mouse.

Organism-specific databases

CTD

2135.

MGI

MGI:1889574. Extl2.

Phylogenomic databases

GeneTree

ENSGT00550000074496.

HOGENOM

HBG713996.

HOVERGEN

HBG051525.

InParanoid

Q9ES89.

OMA

NHYQAVP.

OrthoDB

EOG4RNB91.

PhylomeDB

Q9ES89.

Gene expression databases

ArrayExpress

Q9ES89.

Bgee

Q9ES89.

CleanEx

MM_EXTL2.

Genevestigator

Q9ES89.

GermOnline

ENSMUSG00000027963. Mus musculus.

Family and domain databases

InterPro

IPR015338. HexNAc_Trfase_a.
[Graphical view]

KO

K02369.

Pfam

PF09258. Glyco_transf_64. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

SOURCE

Search...

Entry information

Entry name

EXTL2_MOUSE

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program