EXTL3_MOUSE
ID EXTL3_MOUSE Reviewed; 918 AA.
AC Q9WVL6; E9QKN8;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Exostosin-like 3 {ECO:0000250|UniProtKB:O43909};
DE EC=2.4.1.223 {ECO:0000250|UniProtKB:O43909};
DE AltName: Full=Glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase;
DE AltName: Full=Multiple exostosis-like protein 3 {ECO:0000250|UniProtKB:O43909};
GN Name=Extl3 {ECO:0000312|MGI:MGI:1860765};
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].
RA Sato T.;
RT "Molecular cloning of the mouse homolog of EXT1L.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Glycosyltransferase which regulates the biosynthesis of
CC heparan sulfate (HS). Important for both skeletal development and
CC hematopoiesis, through the formation of HS proteoglycans (HSPGs).
CC Required for the function of REG3A in regulating keratinocyte
CC proliferation and differentiation (By similarity).
CC {ECO:0000250|UniProtKB:O43909}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-Xyl)-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-
CC O-(alpha-D-GlcNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-
CC Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:16221, Rhea:RHEA-COMP:12573, Rhea:RHEA-COMP:12574,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:132093, ChEBI:CHEBI:132104; EC=2.4.1.223;
CC Evidence={ECO:0000250|UniProtKB:O43909};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9ES89};
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC {ECO:0000250|UniProtKB:O43909}.
CC -!- SUBUNIT: Interacts with REG3A. {ECO:0000250|UniProtKB:O43909}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O43909}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:O43909}. Golgi apparatus
CC {ECO:0000250|UniProtKB:O43909}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=EXTL3
CC (Putative GlcNAc Transferase I) [GAG Enzyme];
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_580";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF083550; AAD42040.1; -; mRNA.
DR EMBL; AC155172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q9WVL6; -.
DR SMR; Q9WVL6; -.
DR STRING; 10090.ENSMUSP00000022550; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR CAZy; GT64; Glycosyltransferase Family 64.
DR GlyGen; Q9WVL6; 4 sites.
DR iPTMnet; Q9WVL6; -.
DR PhosphoSitePlus; Q9WVL6; -.
DR SwissPalm; Q9WVL6; -.
DR MaxQB; Q9WVL6; -.
DR PaxDb; Q9WVL6; -.
DR PeptideAtlas; Q9WVL6; -.
DR PRIDE; Q9WVL6; -.
DR ProteomicsDB; 275561; -.
DR MGI; MGI:1860765; Extl3.
DR eggNOG; KOG2264; Eukaryota.
DR InParanoid; Q9WVL6; -.
DR UniPathway; UPA00756; -.
DR ChiTaRS; Extl3; mouse.
DR PRO; PR:Q9WVL6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9WVL6; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0001888; F:glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016757; F:glycosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR004263; Exostosin.
DR InterPro; IPR040911; Exostosin_GT47.
DR InterPro; IPR015338; GT64.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR11062; PTHR11062; 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; Phosphoprotein;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..918
FT /note="Exostosin-like 3"
FT /id="PRO_0000149658"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..918
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 832
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 696
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 722..727
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 743..745
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 745
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 773
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 828..832
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 789
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 830..878
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT CONFLICT 302
FT /note="F -> L (in Ref. 1; AAD42040)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="H -> R (in Ref. 1; AAD42040)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="P -> R (in Ref. 1; AAD42040)"
FT /evidence="ECO:0000305"
FT CONFLICT 758
FT /note="R -> W (in Ref. 1; AAD42040)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 918 AA; 104474 MW; 5A881B9BFCCB8115 CRC64;
MTGYTMLRNG GVGNGGQTCM LRWSNRIRLT WLSFTLFIIL VFFPLIAHYY LTTLDEADEA
GKRIFGPRAG SELCEVKHVL DLCRIRESVS EELLQLEAKR QELNSEIAKL NLKIEACKKS
IENAKQDLLQ LKNVISQTEH SYKELMAQNQ PKLSLPIRLL PEKDDAGLPP PKVTRGCRLH
NCFDYSRCPL TSGFPVYVYD SDQFAFGSYL DPLVKQAFQA TVRANVYVTE NAAIACLYVV
LVGEMQEPTV LRPADLEKQL FSLPHWRTDG HNHVIINLSR KSDTQNLLYN VSTGRHVAQS
TFYAAQYRAG FDLVVSPLVH AMSEPNFMEI PPQVPVKRKY LFTFQGEKIE SLRSSLQEAR
SFEEEMEGDP PADYDDRIIA TLKAVQDSKL DQVLVEFTCK NQPKPSLPTE WALCGEREDR
LELLKLSTFA LIITPGDPHL LISSGCATRL FEALEVGAVP VVLGEQVQLP YHDMLQWNEA
ALVVPKPRVT EVHFLLRSLS DSDLLAMRRQ GRFLWETYFS TADSIFNTVL AMIRTRIQIP
AAPIREEVAA EIPHRSGKAA GTDPNMADNG DLDLGPVETE PPYASPKYLR NFTLTVTDCY
RGWNSAPGPF HLFPHTPFDP VLPSEAKFLG SGTGFRPIGG GAGGSGKEFQ AALGGNVQRE
QFTVVMLTYE REEVLMNSLE RLNGLPYLNK VVVVWNSPKL PSEDLLWPDI GVPIMVVRTE
KNSLNNRFLP WNEIETEAIL SIDDDAHLRH DEIMFGFRVW REARDRIVGF PGRYHAWDIP
HQSWLYNSNY SCELSMVLTG AAFFHKYYAY LYSYVMPQAI RDMVDEYINC EDIAMNFLVS
HITRKPPIKV TSRWTFRCPG CPQALSHDDS HFHERHKCIN FFVKVYGYMP LLYTQFRVDS
VLFKTRLPHD KTKCFKFI
