EXT2_MOUSE
ID EXT2_MOUSE Reviewed; 718 AA.
AC P70428; P70395; Q3TPI7; Q923D6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Exostosin-2;
DE EC=2.4.1.224;
DE EC=2.4.1.225;
DE AltName: Full=Glucuronosyl-N-acetylglucosaminyl-proteoglycan/N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase;
DE AltName: Full=Multiple exostoses protein 2 homolog;
GN Name=Ext2;
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 [MRNA].
RX PubMed=9232192; DOI=10.1006/bmme.1997.2588;
RA Stickens D.J., Evans G.A.;
RT "Isolation and characterization of the murine homolog of the human EXT2
RT multiple exostoses gene.";
RL Biochem. Mol. Med. 61:16-21(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9110175; DOI=10.1101/gr.7.4.359;
RA Clines G.A., Ashley J.A., Shah S., Lovett M.;
RT "The structure of the human multiple exostoses 2 gene and characterization
RT of homologs in mouse and Caenorhabditis elegans.";
RL Genome Res. 7:359-367(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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 [7]
RP CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=10639137; DOI=10.1073/pnas.97.2.668;
RA McCormick C., Duncan G., Goutsos K.T., Tufaro F.;
RT "The putative tumor suppressors EXT1 and EXT2 form a stable complex that
RT accumulates in the Golgi apparatus and catalyzes the synthesis of heparan
RT sulfate.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:668-673(2000).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=18337501; DOI=10.1073/pnas.0705807105;
RA Presto J., Thuveson M., Carlsson P., Busse M., Wilen M., Eriksson I.,
RA Kusche-Gullberg M., Kjellen L.;
RT "Heparan sulfate biosynthesis enzymes EXT1 and EXT2 affect NDST1 expression
RT and heparan sulfate sulfation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:4751-4756(2008).
CC -!- FUNCTION: Glycosyltransferase required for the biosynthesis of heparan-
CC sulfate. The EXT1/EXT2 complex possesses substantially higher
CC glycosyltransferase activity than EXT1 or EXT2 alone. Appears to be a
CC tumor suppressor. Required for the exosomal release of SDCBP, CD63 and
CC syndecan. {ECO:0000250|UniProtKB:Q93063}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-{[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n)-(1->4)-
CC beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-
CC seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-{alpha-D-
CC GlcNAc-[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n)-(1->4)-beta-D-
CC GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl-
CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:16213, Rhea:RHEA-COMP:12621,
CC Rhea:RHEA-COMP:12623, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:132415, ChEBI:CHEBI:132416;
CC EC=2.4.1.224;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-{alpha-D-GlcNAc-[(1->4)-beta-D-GlcA-(1->4)-alpha-D-
CC GlcNAc](n)-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-
CC (1->4)-beta-D-Xyl}-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-
CC O-{[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n+1)-(1->4)-beta-D-
CC GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl-
CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:20908, Rhea:RHEA-COMP:12623,
CC Rhea:RHEA-COMP:14295, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:132415, ChEBI:CHEBI:132416;
CC EC=2.4.1.225;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9ES89};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Forms a homo/heterooligomeric complex with EXT1. Interacts
CC with GALNT5. Interacts with NDST1. {ECO:0000250|UniProtKB:Q93063}.
CC -!- INTERACTION:
CC P70428; Q3UHN9: Ndst1; NbExp=2; IntAct=EBI-15693102, EBI-15693148;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q93063}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q93063}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:10639137}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:10639137}. Golgi apparatus, cis-Golgi network
CC membrane {ECO:0000250|UniProtKB:Q93063}; Single-pass type II membrane
CC protein {ECO:0000255}. Note=The EXT1/EXT2 complex is localized in the
CC Golgi apparatus. {ECO:0000269|PubMed:10639137}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung, liver,
CC skeletal muscle and testis. Heart shows a high expression.
CC {ECO:0000269|PubMed:18337501, ECO:0000269|PubMed:9232192}.
CC -!- DEVELOPMENTAL STAGE: Expressed in early stages of embryonic
CC development.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000305}.
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DR EMBL; U72141; AAB17006.1; -; mRNA.
DR EMBL; U67837; AAC53143.1; -; mRNA.
DR EMBL; AK164342; BAE37749.1; -; mRNA.
DR EMBL; AL732472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL732493; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL27629.1; -; Genomic_DNA.
DR EMBL; BC006597; AAH06597.1; -; mRNA.
DR CCDS; CCDS16456.1; -.
DR RefSeq; NP_034293.2; NM_010163.3.
DR RefSeq; XP_006498796.1; XM_006498733.3.
DR AlphaFoldDB; P70428; -.
DR SMR; P70428; -.
DR BioGRID; 199557; 5.
DR DIP; DIP-29858N; -.
DR IntAct; P70428; 1.
DR STRING; 10090.ENSMUSP00000028623; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR CAZy; GT64; Glycosyltransferase Family 64.
DR GlyGen; P70428; 2 sites.
DR iPTMnet; P70428; -.
DR PhosphoSitePlus; P70428; -.
DR CPTAC; non-CPTAC-4033; -.
DR EPD; P70428; -.
DR MaxQB; P70428; -.
DR PaxDb; P70428; -.
DR PeptideAtlas; P70428; -.
DR PRIDE; P70428; -.
DR ProteomicsDB; 275806; -.
DR Antibodypedia; 26103; 241 antibodies from 29 providers.
DR DNASU; 14043; -.
DR Ensembl; ENSMUST00000028623; ENSMUSP00000028623; ENSMUSG00000027198.
DR GeneID; 14043; -.
DR KEGG; mmu:14043; -.
DR UCSC; uc008lgf.2; mouse.
DR CTD; 2132; -.
DR MGI; MGI:108050; Ext2.
DR VEuPathDB; HostDB:ENSMUSG00000027198; -.
DR eggNOG; KOG1022; Eukaryota.
DR GeneTree; ENSGT00940000156620; -.
DR HOGENOM; CLU_013906_4_1_1; -.
DR InParanoid; P70428; -.
DR OMA; NCTFWDC; -.
DR OrthoDB; 789556at2759; -.
DR PhylomeDB; P70428; -.
DR TreeFam; TF314231; -.
DR BRENDA; 2.4.1.224; 3474.
DR Reactome; R-MMU-2022928; HS-GAG biosynthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 14043; 7 hits in 74 CRISPR screens.
DR ChiTaRS; Ext2; mouse.
DR PRO; PR:P70428; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P70428; protein.
DR Bgee; ENSMUSG00000027198; Expressed in embryonic post-anal tail and 253 other tissues.
DR ExpressionAtlas; P70428; baseline and differential.
DR Genevisible; P70428; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:BHF-UCL.
DR GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
DR GO; GO:0000139; C:Golgi membrane; IC:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043541; C:UDP-N-acetylglucosamine transferase complex; ISO:MGI.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0050508; F:glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity; IC:BHF-UCL.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0016757; F:glycosyltransferase activity; ISO:MGI.
DR GO; GO:0042328; F:heparan sulfate N-acetylglucosaminyltransferase activity; IC:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050509; F:N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
DR GO; GO:0033692; P:cellular polysaccharide biosynthetic process; ISO:MGI.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IMP:MGI.
DR GO; GO:0002062; P:chondrocyte differentiation; IMP:MGI.
DR GO; GO:0060350; P:endochondral bone morphogenesis; IGI:MGI.
DR GO; GO:0042044; P:fluid transport; IGI:MGI.
DR GO; GO:0010467; P:gene expression; IDA:MGI.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; ISO:MGI.
DR GO; GO:0060047; P:heart contraction; IGI:MGI.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IMP:MGI.
DR GO; GO:0015014; P:heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; ISO:MGI.
DR GO; GO:0030210; P:heparin biosynthetic process; IGI:MGI.
DR GO; GO:0001707; P:mesoderm formation; IMP:MGI.
DR GO; GO:0050891; P:multicellular organismal water homeostasis; IGI:MGI.
DR GO; GO:0001503; P:ossification; ISO:MGI.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; IGI:MGI.
DR GO; GO:0055078; P:sodium ion homeostasis; IGI:MGI.
DR GO; GO:0051923; P:sulfation; IDA:MGI.
DR GO; GO:0042311; P:vasodilation; IGI:MGI.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR004263; Exostosin.
DR InterPro; IPR027673; Exostosin-2.
DR InterPro; IPR040911; Exostosin_GT47.
DR InterPro; IPR015338; GT64.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR11062; PTHR11062; 1.
DR PANTHER; PTHR11062:SF128; PTHR11062:SF128; 1.
DR Pfam; PF03016; Exostosin; 1.
DR Pfam; PF09258; Glyco_transf_64; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Manganese; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..718
FT /note="Exostosin-2"
FT /id="PRO_0000149652"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..718
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 628
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 490
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 517..522
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 538..540
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 540
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 569
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 624..628
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 662..673
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 637
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 626..676
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT CONFLICT 62
FT /note="S -> T (in Ref. 2; AAC53143)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="L -> V (in Ref. 2; AAC53143)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="G -> R (in Ref. 2; AAC53143)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="V -> I (in Ref. 2; AAC53143)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="R -> K (in Ref. 2; AAC53143)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="Q -> H (in Ref. 2; AAC53143)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="T -> A (in Ref. 2; AAC53143)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 718 AA; 82064 MW; 45D947BF6678378B CRC64;
MCASVKSNIR GPALIPRMKT KHRIYYVTLF SIVLLGLIAT GMFQFWPHSI ESSSDGGVEK
RSIREVPVVR LPTDSPIPER GDLSCRMHTC FDVYRCGFNP KNKIKVYIYP LKKYVDDAGV
PVSSAISREY NELLTAISDS DYYTDDINRA CLFVPSIDVL NQNPLRIKET AQALAQLSRW
DRGTNHLLFN MLPGAPPDYN TALDVPRDRA LLAGGGFSTW TYRQGYDVSI PVFSPLSAEM
ALPEKAPGPR RYFLLSSQMA IHPEYREELE ALQAKHQESV LVLDKCTNLS EGVLSVRKRC
HQHQVFDYPQ VLQEATFCTV LRGARLGQAV LSDVLQAGCV PVVIADSYIL PFSEVLDWKR
ASVVVPEEKM SDVYSILQNI PQRQIEEMQR QARWFWEAYF QSIKAIALAT LQIINDRIYP
YAAISYEEWN DPPAVKWASV SNPLFLPLIP PQSQGFTAIV LTYDRVESLF RVITEVSKVP
SLSKLLVVWN NQNKNPPEES LWPKIRVPLK VVRTAENKLS NRFFPYDEIE TEAVLAIDDD
IIMLTSDELQ FGYEVWREFP DRLVGYPGRL HLWDHEMNKW KYESEWTNEV SMVLTGAAFY
HKYFNYLYTY KMPGDIKNWV DTHMNCEDIA MNFLVANVTG KAVIKVTPRK KFKCPECTAI
DGLSLDQTHM VERSECINKF ASVFGTMPLK VVEHRADPVL YKDDFPEKLK SFPNIGSL
