EXTL1_MOUSE
ID EXTL1_MOUSE Reviewed; 669 AA.
AC Q9JKV7; E9QKA3;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Exostosin-like 1;
DE EC=2.4.1.224;
DE AltName: Full=Exostosin-L;
DE AltName: Full=Glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase;
DE AltName: Full=Multiple exostosis-like protein;
GN Name=Extl1;
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].
RC TISSUE=Fetal brain;
RX PubMed=10878610;
RX DOI=10.1002/1097-0177(200007)218:3<452::aid-dvdy1000>3.0.co;2-p;
RA Stickens D., Brown D., Evans G.A.;
RT "EXT genes are differentially expressed in bone and cartilage during mouse
RT embryogenesis.";
RL Dev. Dyn. 218:452-464(2000).
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).
CC -!- FUNCTION: Probable glycosyltransferase. {ECO:0000250}.
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 -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=EXTL1
CC (putative HS transferase) [GAG Enzyme];
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_578";
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; AF224461; AAF61913.1; -; mRNA.
DR EMBL; AL669982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS18770.1; -.
DR RefSeq; NP_062524.2; NM_019578.2.
DR AlphaFoldDB; Q9JKV7; -.
DR SMR; Q9JKV7; -.
DR STRING; 10090.ENSMUSP00000030643; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR CAZy; GT64; Glycosyltransferase Family 64.
DR GlyGen; Q9JKV7; 2 sites.
DR PhosphoSitePlus; Q9JKV7; -.
DR PaxDb; Q9JKV7; -.
DR PRIDE; Q9JKV7; -.
DR ProteomicsDB; 267677; -.
DR Antibodypedia; 30538; 123 antibodies from 24 providers.
DR DNASU; 56219; -.
DR Ensembl; ENSMUST00000030643; ENSMUSP00000030643; ENSMUSG00000028838.
DR GeneID; 56219; -.
DR KEGG; mmu:56219; -.
DR UCSC; uc012dmu.1; mouse.
DR CTD; 2134; -.
DR MGI; MGI:1888742; Extl1.
DR VEuPathDB; HostDB:ENSMUSG00000028838; -.
DR eggNOG; KOG1021; Eukaryota.
DR GeneTree; ENSGT00940000161960; -.
DR HOGENOM; CLU_013906_4_0_1; -.
DR InParanoid; Q9JKV7; -.
DR OMA; WNHFWDE; -.
DR OrthoDB; 789556at2759; -.
DR PhylomeDB; Q9JKV7; -.
DR TreeFam; TF314231; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 56219; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Extl1; mouse.
DR PRO; PR:Q9JKV7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9JKV7; protein.
DR Bgee; ENSMUSG00000028838; Expressed in hindlimb stylopod muscle and 167 other tissues.
DR Genevisible; Q9JKV7; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0050508; F:glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IBA:GO_Central.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR004263; Exostosin.
DR InterPro; IPR027675; Exostosin-like_1.
DR InterPro; IPR040911; Exostosin_GT47.
DR InterPro; IPR015338; GT64.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR11062; PTHR11062; 1.
DR PANTHER; PTHR11062:SF8; PTHR11062:SF8; 1.
DR Pfam; PF03016; Exostosin; 1.
DR Pfam; PF09258; Glyco_transf_64; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..669
FT /note="Exostosin-like 1"
FT /id="PRO_0000149654"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..669
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 601..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 577..627
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT CONFLICT 32
FT /note="L -> S (in Ref. 1; AAF61913)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="L -> I (in Ref. 1; AAF61913)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="I -> V (in Ref. 1; AAF61913)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="L -> P (in Ref. 1; AAF61913)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="E -> D (in Ref. 1; AAF61913)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 669 AA; 74079 MW; 79629222B6CA3821 CRC64;
MLWRRKSFWL ALSAFWLLLV LLGVFPLRLA VLPGPLPGRS QGWPRWLDAA FLQSFSQSET
NPEDVAQLPR VSRGSSCTWG ACFDTSKCRG KVLKIFVHSP AGPTSEAQRR ILDSLEGSRY
SALSPADACL LLFLPSQDRR GACGPLPPNW NGGRNHLVLS LYPAPCTRLG QAMVAEASPS
SDIFRPGFDL ALPYLPEAHP LRGGAPGKLQ QHSPQPGATL LAVAEEKGRW RITSTHASAC
LWDRHCEQDP GPQQTYPGET LPNATFCLIP GHRSATSCFL QALQAGCIPV LLSPRWELPF
SEVIDWTKAA IIADERLPLQ VLAALREMLP SRVLALRQQT QFLWTAYFSS VEKVIHTTLE
IIQDRIWGAS GHPSLMWNSP PGALLALPTF STSLQDFPFY HLQLGSGPGS SFSAVIWVGA
SGESLLKLIQ EVAGSRHCAQ ILILWNSEKL PPDRWPETAV PLTVIKGHRK VSNRFFPYSN
ISTNVILSLD AQSTLSTSEV DFAFVVWQSF PERMVGFLSG SHFWDEAQGG WGYRTGMTNE
FSMVLTTAAF YHRYYHTLFT HSLPKALRTI ADETPTCVDV LMNFLVATVT KLPPIKVPYG
RQHPEAVPMD SGDPRPVPEP QPLDQDCINR LAAGFGHMPL VSSQVRLDPV LFKDPVSVQR
KKYRSLEKP
