EXTL1_HUMAN
ID EXTL1_HUMAN Reviewed; 676 AA.
AC Q92935; Q6GSC1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 171.
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; Synonyms=EXTL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-379.
RX PubMed=9037597; DOI=10.1101/gr.7.1.10;
RA Wise C.A., Clines G.A., Massa H., Trask B.J., Lovett M.;
RT "Identification and localization of the gene for EXTL, a third member of
RT the multiple exostoses gene family.";
RL Genome Res. 7:10-16(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASN-379.
RX PubMed=10480354; DOI=10.1007/s004399900058;
RA Xu L., Xia J., Jiang H., Zhou J., Li H., Wang D., Pan Q., Long Z., Fan C.,
RA Deng H.-X.;
RT "Mutation analysis of hereditary multiple exostoses in the Chinese.";
RL Hum. Genet. 105:45-50(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASN-379.
RX PubMed=10575224; DOI=10.1159/000015317;
RA Wuyts W., Spieker N., Van Roy N., De Boulle K., De Paepe A., Willems P.J.,
RA Van Hul W., Versteeg R., Speleman F.;
RT "Refined physical mapping and genomic structure of the EXTL1 gene.";
RL Cytogenet. Cell Genet. 86:267-270(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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).
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 -!- INTERACTION:
CC Q92935; O95484: CLDN9; NbExp=3; IntAct=EBI-1760167, EBI-18341636;
CC Q92935; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-1760167, EBI-781551;
CC Q92935; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-1760167, EBI-12142257;
CC Q92935; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-1760167, EBI-8638294;
CC Q92935; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-1760167, EBI-10982110;
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;
CC Note=Exostosin-like 1;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_529";
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DR EMBL; U67191; AAC51141.1; -; mRNA.
DR EMBL; AF083633; AAD02840.1; -; Genomic_DNA.
DR EMBL; AF083623; AAD02840.1; JOINED; Genomic_DNA.
DR EMBL; AF083624; AAD02840.1; JOINED; Genomic_DNA.
DR EMBL; AF083625; AAD02840.1; JOINED; Genomic_DNA.
DR EMBL; AF083626; AAD02840.1; JOINED; Genomic_DNA.
DR EMBL; AF083627; AAD02840.1; JOINED; Genomic_DNA.
DR EMBL; AF083628; AAD02840.1; JOINED; Genomic_DNA.
DR EMBL; AF083629; AAD02840.1; JOINED; Genomic_DNA.
DR EMBL; AF083630; AAD02840.1; JOINED; Genomic_DNA.
DR EMBL; AF083631; AAD02840.1; JOINED; Genomic_DNA.
DR EMBL; AF083632; AAD02840.1; JOINED; Genomic_DNA.
DR EMBL; AF153980; AAF73172.1; -; Genomic_DNA.
DR EMBL; AF151391; AAF73172.1; JOINED; Genomic_DNA.
DR EMBL; AL391650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC065528; AAH65528.1; -; mRNA.
DR CCDS; CCDS271.1; -.
DR RefSeq; NP_004446.2; NM_004455.2.
DR AlphaFoldDB; Q92935; -.
DR SMR; Q92935; -.
DR BioGRID; 108435; 6.
DR IntAct; Q92935; 7.
DR STRING; 9606.ENSP00000363398; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR CAZy; GT64; Glycosyltransferase Family 64.
DR GlyGen; Q92935; 1 site.
DR iPTMnet; Q92935; -.
DR PhosphoSitePlus; Q92935; -.
DR BioMuta; EXTL1; -.
DR DMDM; 93141259; -.
DR jPOST; Q92935; -.
DR MassIVE; Q92935; -.
DR PaxDb; Q92935; -.
DR PeptideAtlas; Q92935; -.
DR PRIDE; Q92935; -.
DR ProteomicsDB; 75615; -.
DR Antibodypedia; 30538; 123 antibodies from 24 providers.
DR DNASU; 2134; -.
DR Ensembl; ENST00000374280.4; ENSP00000363398.3; ENSG00000158008.10.
DR GeneID; 2134; -.
DR KEGG; hsa:2134; -.
DR MANE-Select; ENST00000374280.4; ENSP00000363398.3; NM_004455.3; NP_004446.2.
DR UCSC; uc001blf.4; human.
DR CTD; 2134; -.
DR DisGeNET; 2134; -.
DR GeneCards; EXTL1; -.
DR HGNC; HGNC:3515; EXTL1.
DR HPA; ENSG00000158008; Group enriched (brain, skeletal muscle, tongue).
DR MIM; 601738; gene.
DR neXtProt; NX_Q92935; -.
DR OpenTargets; ENSG00000158008; -.
DR PharmGKB; PA27927; -.
DR VEuPathDB; HostDB:ENSG00000158008; -.
DR eggNOG; KOG1021; Eukaryota.
DR GeneTree; ENSGT00940000161960; -.
DR HOGENOM; CLU_013906_4_0_1; -.
DR InParanoid; Q92935; -.
DR OMA; WNHFWDE; -.
DR OrthoDB; 789556at2759; -.
DR PhylomeDB; Q92935; -.
DR TreeFam; TF314231; -.
DR BioCyc; MetaCyc:HS08259-MON; -.
DR PathwayCommons; Q92935; -.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR SignaLink; Q92935; -.
DR SIGNOR; Q92935; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 2134; 28 hits in 1066 CRISPR screens.
DR GeneWiki; EXTL1; -.
DR GenomeRNAi; 2134; -.
DR Pharos; Q92935; Tbio.
DR PRO; PR:Q92935; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q92935; protein.
DR Bgee; ENSG00000158008; Expressed in right frontal lobe and 119 other tissues.
DR Genevisible; Q92935; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
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 GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
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 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..676
FT /note="Exostosin-like 1"
FT /id="PRO_0000149653"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..676
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 238..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 584..634
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT VARIANT 163
FT /note="R -> H (in dbSNP:rs34277678)"
FT /id="VAR_049228"
FT VARIANT 379
FT /note="H -> N (in dbSNP:rs2736831)"
FT /evidence="ECO:0000269|PubMed:10480354,
FT ECO:0000269|PubMed:10575224, ECO:0000269|PubMed:9037597"
FT /id="VAR_012830"
SQ SEQUENCE 676 AA; 74697 MW; AAC7E7360E2B2776 CRC64;
MQSWRRRKSL WLALSASWLL LVLLGGFSLL RLALPPRPRP GASQGWPRWL DAELLQSFSQ
PGELPEDAVS PPQAPHGGSC NWESCFDTSK CRGDGLKVFV YPAVGTISET HRRILASIEG
SRFYTFSPAG ACLLLLLSLD AQTGECSSMP LQWNRGRNHL VLRLHPAPCP RTFQLGQAMV
AEASPTVDSF RPGFDVALPF LPEAHPLRGG APGQLRQHSP QPGVALLALE EERGGWRTAD
TGSSACPWDG RCEQDPGPGQ TQRQETLPNA TFCLISGHRP EAASRFLQAL QAGCIPVLLS
PRWELPFSEV IDWTKAAIVA DERLPLQVLA ALQEMSPARV LALRQQTQFL WDAYFSSVEK
VIHTTLEVIQ DRIFGTSAHP SLLWNSPPGA LLALSTFSTS PQDFPFYYLQ QGSRPEGRFS
ALIWVGPPGQ PPLKLIQAVA GSQHCAQILV LWSNERPLPS RWPETAVPLT VIDGHRKVSD
RFYPYSTIRT DAILSLDARS SLSTSEVDFA FLVWQSFPER MVGFLTSSHF WDEAHGGWGY
TAERTNEFSM VLTTAAFYHR YYHTLFTHSL PKALRTLADE APTCVDVLMN FIVAAVTKLP
PIKVPYGKQR QEAAPLAPGG PGPRPKPPAP APDCINQIAA AFGHMPLLSS RLRLDPVLFK
DPVSVQRKKY RSLEKP
