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   27-MAR-2024, entry version 143.
DE   RecName: Full=Exostosin-like 1;
DE            EC=2.4.1.224 {ECO:0000250|UniProtKB:Q92935};
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: Glycosyltransferase required for the biosynthesis of heparan-
CC       sulfate (HS). Transfers N-acetyl-alpha-D-glucosamine to the nascent HS
CC       chain (GlcNAcT-II activity). Appears to lack GlcNAcT I and GlcAT-II
CC       activities. {ECO:0000250|UniProtKB:Q92935}.
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; Evidence={ECO:0000250|UniProtKB:Q92935};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:Q92935}.
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";
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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   GlyCosmos; Q9JKV7; 2 sites, No reported glycans.
DR   GlyGen; Q9JKV7; 3 sites, 1 O-linked glycan (1 site).
DR   PhosphoSitePlus; Q9JKV7; -.
DR   PaxDb; 10090-ENSMUSP00000030643; -.
DR   Antibodypedia; 30538; 129 antibodies from 24 providers.
DR   DNASU; 56219; -.
DR   Ensembl; ENSMUST00000030643.3; ENSMUSP00000030643.3; ENSMUSG00000028838.12.
DR   GeneID; 56219; -.
DR   KEGG; mmu:56219; -.
DR   UCSC; uc012dmu.1; mouse.
DR   AGR; MGI:1888742; -.
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; QWNGGKN; -.
DR   OrthoDB; 1220028at2759; -.
DR   PhylomeDB; Q9JKV7; -.
DR   TreeFam; TF314231; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 56219; 3 hits in 77 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 169 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0008375; F:acetylglucosaminyltransferase activity; IBA:GO_Central.
DR   GO; GO:0050508; F:glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0015020; F:glucuronosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR004263; Exostosin.
DR   InterPro; IPR040911; Exostosin_GT47.
DR   InterPro; IPR015338; GT64.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR48261; ACETYLGLUCOSAMINYLTRANSFERASE; 1.
DR   PANTHER; PTHR48261:SF2; EXOSTOSIN-1-LIKE; 1.
DR   Pfam; PF03016; Exostosin; 1.
DR   Pfam; PF09258; Glyco_transf_64; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   Genevisible; Q9JKV7; MM.
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
//