EXTL3_HUMAN
ID EXTL3_HUMAN Reviewed; 919 AA.
AC O43909; D3DST8; O00225; Q53XT3;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Exostosin-like 3 {ECO:0000303|PubMed:9479495};
DE EC=2.4.1.223 {ECO:0000305|PubMed:28132690, ECO:0000305|PubMed:28148688};
DE AltName: Full=EXT-related protein 1 {ECO:0000303|PubMed:9473480};
DE AltName: Full=Glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase;
DE AltName: Full=Hereditary multiple exostoses gene isolog {ECO:0000303|Ref.9};
DE AltName: Full=Multiple exostosis-like protein 3 {ECO:0000303|Ref.6};
DE AltName: Full=Putative tumor suppressor protein EXTL3 {ECO:0000303|PubMed:9479495};
GN Name=EXTL3 {ECO:0000303|PubMed:28397838, ECO:0000312|HGNC:HGNC:3518};
GN Synonyms=EXTL1L, EXTR1, KIAA0519;
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].
RX PubMed=9479495; DOI=10.1006/geno.1997.5101;
RA van Hul W., Wuyts W., Hendrickx J., Speleman F., Wauters J., de Boulle K.,
RA van Roy N., Bossuyt P., Willems P.J.;
RT "Identification of a third EXT-like gene (EXTL3) belonging to the EXT gene
RT family.";
RL Genomics 47:230-237(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetus, and Testis;
RX PubMed=9473480; DOI=10.1006/bbrc.1997.8062;
RA Saito T., Seki N., Yamauchi M., Tsuji S., Hayashi A., Kozuma S.,
RA Hori T.-A.;
RT "Structure, chromosomal location, and expression profile of EXTR1 and
RT EXTR2, new members of the multiple exostoses gene family.";
RL Biochem. Biophys. Res. Commun. 243:61-66(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Deng H.-X., Xu L., Xia J.-H., Fan C., Pan Q., Liu C.-Y., Ruan Q.-G.;
RT "Molecular cloning of a candidate gene for multiple exostoses.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sato T.;
RT "The human EXTL1L/EXTR1/EXTL3 gene at 8p11-p12, the third breast cancer
RT susceptibility gene locus, is not mutated in breast and various cancers.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 470-919.
RA Adams M.D.;
RT "Human chromosome 8 BAC clone CIT987SK-2A8 complete sequence.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP 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 [11]
RP FUNCTION, INTERACTION WITH REG3A, AND TISSUE SPECIFICITY.
RX PubMed=22727489; DOI=10.1016/j.immuni.2012.04.010;
RA Lai Y., Li D., Li C., Muehleisen B., Radek K.A., Park H.J., Jiang Z.,
RA Li Z., Lei H., Quan Y., Zhang T., Wu Y., Kotol P., Morizane S., Hata T.R.,
RA Iwatsuki K., Tang C., Gallo R.L.;
RT "The antimicrobial protein REG3A regulates keratinocyte proliferation and
RT differentiation after skin injury.";
RL Immunity 37:74-84(2012).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, INVOLVEMENT IN
RP ISDNA, VARIANTS ISDNA LEU-461; CYS-513; SER-657 AND ASP-670,
RP CHARACTERIZATION OF VARIANTS ISDNA LEU-461; CYS-513; SER-657 AND ASP-670,
RP AND VARIANT LEU-442.
RX PubMed=28132690; DOI=10.1016/j.ajhg.2017.01.013;
RA Oud M.M., Tuijnenburg P., Hempel M., van Vlies N., Ren Z.,
RA Ferdinandusse S., Jansen M.H., Santer R., Johannsen J., Bacchelli C.,
RA Alders M., Li R., Davies R., Dupuis L., Cale C.M., Wanders R.J., Pals S.T.,
RA Ocaka L., James C., Mueller I., Lehmberg K., Strom T., Engels H.,
RA Williams H.J., Beales P., Roepman R., Dias P., Brunner H.G., Cobben J.M.,
RA Hall C., Hartley T., Le Quesne Stabej P., Mendoza-Londono R., Davies E.G.,
RA de Sousa S.B., Lessel D., Arts H.H., Kuijpers T.W.;
RT "Mutations in EXTL3 cause neuro-immuno-skeletal dysplasia syndrome.";
RL Am. J. Hum. Genet. 100:281-296(2017).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, VARIANTS ISDNA TRP-339 AND LEU-461,
RP AND CHARACTERIZATION OF VARIANTS ISDNA TRP-339 AND LEU-461.
RX PubMed=28148688; DOI=10.1084/jem.20161525;
RA Volpi S., Yamazaki Y., Brauer P.M., van Rooijen E., Hayashida A.,
RA Slavotinek A., Sun Kuehn H., Di Rocco M., Rivolta C., Bortolomai I., Du L.,
RA Felgentreff K., Ott de Bruin L., Hayashida K., Freedman G.,
RA Marcovecchio G.E., Capuder K., Rath P., Luche N., Hagedorn E.J.,
RA Buoncompagni A., Royer-Bertrand B., Giliani S., Poliani P.L., Imberti L.,
RA Dobbs K., Poulain F.E., Martini A., Manis J., Linhardt R.J., Bosticardo M.,
RA Rosenzweig S.D., Lee H., Puck J.M., Zuniga-Pfluecker J.C., Zon L.,
RA Park P.W., Superti-Furga A., Notarangelo L.D.;
RT "EXTL3 mutations cause skeletal dysplasia, immune deficiency, and
RT developmental delay.";
RL J. Exp. Med. 214:623-637(2017).
RN [14]
RP VARIANT CYS-646.
RX PubMed=28397838; DOI=10.1038/mp.2017.60;
RA Harripaul R., Vasli N., Mikhailov A., Rafiq M.A., Mittal K.,
RA Windpassinger C., Sheikh T.I., Noor A., Mahmood H., Downey S., Johnson M.,
RA Vleuten K., Bell L., Ilyas M., Khan F.S., Khan V., Moradi M., Ayaz M.,
RA Naeem F., Heidari A., Ahmed I., Ghadami S., Agha Z., Zeinali S., Qamar R.,
RA Mozhdehipanah H., John P., Mir A., Ansar M., French L., Ayub M.,
RA Vincent J.B.;
RT "Mapping autosomal recessive intellectual disability: combined microarray
RT and exome sequencing identifies 26 novel candidate genes in 192
RT consanguineous families.";
RL Mol. Psychiatry 23:973-984(2018).
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 (PubMed:28132690, PubMed:28148688). Required for the function of REG3A
CC in regulating keratinocyte proliferation and differentiation
CC (PubMed:22727489). {ECO:0000269|PubMed:22727489,
CC ECO:0000269|PubMed:28132690, ECO:0000269|PubMed:28148688}.
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:0000305|PubMed:28132690, ECO:0000305|PubMed:28148688};
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:0000269|PubMed:28132690, ECO:0000269|PubMed:28148688}.
CC -!- SUBUNIT: Interacts with REG3A. {ECO:0000269|PubMed:22727489}.
CC -!- INTERACTION:
CC O43909; P54253: ATXN1; NbExp=3; IntAct=EBI-1754679, EBI-930964;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10639137}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:10639137}. Golgi apparatus
CC {ECO:0000269|PubMed:28132690}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in keratinocytes.
CC {ECO:0000269|PubMed:22727489}.
CC -!- DISEASE: Immunoskeletal dysplasia with neurodevelopmental abnormalities
CC (ISDNA) [MIM:617425]: An autosomal recessive disorder characterized by
CC variable skeletal abnormalities and neurodevelopmental defects.
CC Neurologic manifestations include intellectual disability and motor
CC delay. Some patients manifest hypotonia and seizures. Skeletal features
CC include disproportionate short stature, cervical malformations,
CC epiphyseal and metaphyseal dysplasia, and rarely premature
CC craniosynostosis with progressive microcephaly. Severe combined
CC immunodeficiency with a complete absence of T cells is observed in some
CC patients. {ECO:0000269|PubMed:28132690, ECO:0000269|PubMed:28148688}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1, Met-6 or Met-20 is the
CC initiator. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25445.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Exostosin-like 3;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_531";
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; AF001690; AAC39598.1; -; mRNA.
DR EMBL; U76188; AAB93670.1; -; mRNA.
DR EMBL; AB007042; BAA24080.1; -; mRNA.
DR EMBL; AB011091; BAA25445.2; ALT_INIT; mRNA.
DR EMBL; AF029231; AAD01877.1; -; mRNA.
DR EMBL; AF083551; AAD42041.1; -; mRNA.
DR EMBL; BT007353; AAP36017.1; -; mRNA.
DR EMBL; CH471080; EAW63507.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63508.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63509.1; -; Genomic_DNA.
DR EMBL; BC006363; AAH06363.1; -; mRNA.
DR EMBL; U96629; AAB67602.1; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS6070.1; -.
DR PIR; JC5934; JC5934.
DR RefSeq; NP_001431.1; NM_001440.3.
DR RefSeq; XP_011542742.1; XM_011544440.2.
DR AlphaFoldDB; O43909; -.
DR SMR; O43909; -.
DR BioGRID; 108438; 130.
DR IntAct; O43909; 27.
DR MINT; O43909; -.
DR STRING; 9606.ENSP00000220562; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR CAZy; GT64; Glycosyltransferase Family 64.
DR GlyGen; O43909; 5 sites, 1 O-linked glycan (1 site).
DR iPTMnet; O43909; -.
DR PhosphoSitePlus; O43909; -.
DR BioMuta; EXTL3; -.
DR EPD; O43909; -.
DR jPOST; O43909; -.
DR MassIVE; O43909; -.
DR MaxQB; O43909; -.
DR PaxDb; O43909; -.
DR PeptideAtlas; O43909; -.
DR PRIDE; O43909; -.
DR ProteomicsDB; 49226; -.
DR Antibodypedia; 23127; 282 antibodies from 29 providers.
DR DNASU; 2137; -.
DR Ensembl; ENST00000220562.9; ENSP00000220562.4; ENSG00000012232.9.
DR GeneID; 2137; -.
DR KEGG; hsa:2137; -.
DR MANE-Select; ENST00000220562.9; ENSP00000220562.4; NM_001440.4; NP_001431.1.
DR UCSC; uc003xgz.3; human.
DR CTD; 2137; -.
DR DisGeNET; 2137; -.
DR GeneCards; EXTL3; -.
DR HGNC; HGNC:3518; EXTL3.
DR HPA; ENSG00000012232; Low tissue specificity.
DR MalaCards; EXTL3; -.
DR MIM; 605744; gene.
DR MIM; 617425; phenotype.
DR neXtProt; NX_O43909; -.
DR OpenTargets; ENSG00000012232; -.
DR Orphanet; 508533; Skeletal dysplasia-T-cell immunodeficiency-developmental delay syndrome.
DR PharmGKB; PA27930; -.
DR VEuPathDB; HostDB:ENSG00000012232; -.
DR eggNOG; KOG2264; Eukaryota.
DR GeneTree; ENSGT00940000156692; -.
DR HOGENOM; CLU_013906_3_0_1; -.
DR InParanoid; O43909; -.
DR OMA; AKFMGSH; -.
DR OrthoDB; 789556at2759; -.
DR PhylomeDB; O43909; -.
DR TreeFam; TF314231; -.
DR BioCyc; MetaCyc:HS00333-MON; -.
DR BRENDA; 2.4.1.223; 2681.
DR PathwayCommons; O43909; -.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR SignaLink; O43909; -.
DR UniPathway; UPA00756; -.
DR BioGRID-ORCS; 2137; 100 hits in 1082 CRISPR screens.
DR ChiTaRS; EXTL3; human.
DR GeneWiki; EXTL3; -.
DR GenomeRNAi; 2137; -.
DR Pharos; O43909; Tbio.
DR PRO; PR:O43909; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; O43909; protein.
DR Bgee; ENSG00000012232; Expressed in stromal cell of endometrium and 139 other tissues.
DR ExpressionAtlas; O43909; baseline and differential.
DR Genevisible; O43909; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0001888; F:glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016757; F:glycosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IDA:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
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 Disease variant; Disulfide bond; Dwarfism; Endoplasmic reticulum;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Intellectual disability; Manganese; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..919
FT /note="Exostosin-like 3"
FT /id="PRO_0000149657"
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..919
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 833
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 697
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 723..728
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 744..746
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 746
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 774
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 829..833
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVL6"
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 592
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 790
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 831..879
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT VARIANT 339
FT /note="R -> W (in ISDNA; changed glycosaminoglycan
FT synthesis; dbSNP:rs747676107)"
FT /evidence="ECO:0000269|PubMed:28148688"
FT /id="VAR_079089"
FT VARIANT 442
FT /note="V -> L (in dbSNP:rs116659770)"
FT /evidence="ECO:0000269|PubMed:28132690"
FT /id="VAR_079090"
FT VARIANT 461
FT /note="P -> L (in ISDNA; changed glycosaminoglycan
FT synthesis; dbSNP:rs554294508)"
FT /evidence="ECO:0000269|PubMed:28132690,
FT ECO:0000269|PubMed:28148688"
FT /id="VAR_079091"
FT VARIANT 513
FT /note="R -> C (in ISDNA; changed glycosaminoglycan
FT synthesis; no localization to Golgi apparatus in patient
FT fibroblasts; dbSNP:rs1332006145)"
FT /evidence="ECO:0000269|PubMed:28132690"
FT /id="VAR_079092"
FT VARIANT 550
FT /note="A -> V (in dbSNP:rs35781576)"
FT /id="VAR_061194"
FT VARIANT 646
FT /note="S -> C (found in a small consanguineous family with
FT intellectual disability; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28397838"
FT /id="VAR_080762"
FT VARIANT 657
FT /note="N -> S (in ISDNA; changed glycosaminoglycan
FT synthesis; dbSNP:rs770842408)"
FT /evidence="ECO:0000269|PubMed:28132690"
FT /id="VAR_079093"
FT VARIANT 670
FT /note="Y -> D (in ISDNA; changed glycosaminoglycan
FT synthesis)"
FT /evidence="ECO:0000269|PubMed:28132690"
FT /id="VAR_079094"
FT VARIANT 706
FT /note="L -> P (in dbSNP:rs2269452)"
FT /id="VAR_049229"
SQ SEQUENCE 919 AA; 104749 MW; 200ADD4DAB4A39FD CRC64;
MTGYTMLRNG GAGNGGQTCM LRWSNRIRLT WLSFTLFVIL VFFPLIAHYY LTTLDEADEA
GKRIFGPRVG NELCEVKHVL DLCRIRESVS EELLQLEAKR QELNSEIAKL NLKIEACKKS
IENAKQDLLQ LKNVISQTEH SYKELMAQNQ PKLSLPIRLL PEKDDAGLPP PKATRGCRLH
NCFDYSRCPL TSGFPVYVYD SDQFVFGSYL DPLVKQAFQA TARANVYVTE NADIACLYVI
LVGEMQEPVV LRPAELEKQL YSLPHWRTDG HNHVIINLSR KSDTQNLLYN VSTGRAMVAQ
STFYTVQYRP GFDLVVSPLV HAMSEPNFME IPPQVPVKRK YLFTFQGEKI ESLRSSLQEA
RSFEEEMEGD PPADYDDRII ATLKAVQDSK LDQVLVEFTC KNQPKPSLPT EWALCGERED
RLELLKLSTF ALIITPGDPR LVISSGCATR LFEALEVGAV PVVLGEQVQL PYQDMLQWNE
AALVVPKPRV TEVHFLLRSL SDSDLLAMRR QGRFLWETYF STADSIFNTV LAMIRTRIQI
PAAPIREEAA AEIPHRSGKA AGTDPNMADN GDLDLGPVET EPPYASPRYL RNFTLTVTDF
YRSWNCAPGP FHLFPHTPFD PVLPSEAKFL GSGTGFRPIG GGAGGSGKEF QAALGGNVPR
EQFTVVMLTY EREEVLMNSL ERLNGLPYLN KVVVVWNSPK LPSEDLLWPD IGVPIMVVRT
EKNSLNNRFL PWNEIETEAI LSIDDDAHLR HDEIMFGFRV WREARDRIVG FPGRYHAWDI
PHQSWLYNSN YSCELSMVLT GAAFFHKYYA YLYSYVMPQA IRDMVDEYIN CEDIAMNFLV
SHITRKPPIK VTSRWTFRCP GCPQALSHDD SHFHERHKCI NFFVKVYGYM PLLYTQFRVD
SVLFKTRLPH DKTKCFKFI
