XYLT1_HUMAN
ID XYLT1_HUMAN Reviewed; 959 AA.
AC Q86Y38; Q9H1B6;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Xylosyltransferase 1;
DE EC=2.4.2.26 {ECO:0000269|PubMed:11087729, ECO:0000269|PubMed:11099377, ECO:0000269|PubMed:15294915, ECO:0000269|PubMed:15461586, ECO:0000269|PubMed:17189265, ECO:0000269|PubMed:23982343, ECO:0000269|PubMed:29681470};
DE AltName: Full=Peptide O-xylosyltransferase 1;
DE AltName: Full=Xylosyltransferase I;
DE Short=XT-I;
DE Short=XylT-I;
GN Name=XYLT1; Synonyms=XT1;
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], FUNCTION, DISULFIDE BONDS, COFACTOR, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF
RP CYS-257; CYS-276; CYS-285; CYS-301; CYS-471; CYS-542; CYS-561; CYS-563;
RP CYS-572; CYS-574; CYS-675; CYS-920; CYS-927 AND CYS-933.
RX PubMed=15461586; DOI=10.1042/bj20041206;
RA Mueller S., Schoettler M., Schoen S., Prante C., Brinkmann T., Kuhn J.,
RA Goetting C., Kleesiek K.;
RT "Human xylosyltransferase I: functional and biochemical characterization of
RT cysteine residues required for enzymic activity.";
RL Biochem. J. 386:227-236(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 133-959, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=11099377; DOI=10.1006/jmbi.2000.4261;
RA Goetting C., Kuhn J., Zahn R., Brinkmann T., Kleesiek K.;
RT "Molecular cloning and expression of human UDP-D-xylose:proteoglycan core
RT protein beta-D-xylosyltransferase and its first isoform XT-II.";
RL J. Mol. Biol. 304:517-528(2000).
RN [3]
RP PROTEIN SEQUENCE OF 159-171; 185-202; 289-296; 444-449; 593-598; 727-748
RP AND 948-959, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=11087729; DOI=10.1074/jbc.m005111200;
RA Kuhn J., Goetting C., Schnoelzer M., Kempf T., Brinkmann T., Kleesiek K.;
RT "First isolation of human UDP-D-xylose: proteoglycan core protein beta-D-
RT xylosyltransferase secreted from cultured JAR choriocarcinoma cells.";
RL J. Biol. Chem. 276:4940-4947(2001).
RN [4]
RP REDUCED ACTIVITY IN SEMINAL PLASMA.
RX PubMed=11814476; DOI=10.1016/s0009-8981(01)00793-8;
RA Goetting C., Kuhn J., Brinkmann T., Kleesiek K.;
RT "Xylosyltransferase activity in seminal plasma of infertile men.";
RL Clin. Chim. Acta 317:199-202(2002).
RN [5]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP MUTAGENESIS OF ASP-314; ASP-316; ASP-745; TRP-746 AND ASP-747.
RX PubMed=15294915; DOI=10.1074/jbc.m401340200;
RA Goetting C., Mueller S., Schoettler M., Schoen S., Prante C., Brinkmann T.,
RA Kuhn J., Kleesiek K.;
RT "Analysis of the DXD motifs in human xylosyltransferase I required for
RT enzyme activity.";
RL J. Biol. Chem. 279:42566-42573(2004).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=17189265; DOI=10.1074/jbc.m611665200;
RA Poenighaus C., Ambrosius M., Casanova J.C., Prante C., Kuhn J., Esko J.D.,
RA Kleesiek K., Goetting C.;
RT "Human xylosyltransferase II is involved in the biosynthesis of the uniform
RT tetrasaccharide linkage region in chondroitin sulfate and heparan sulfate
RT proteoglycans.";
RL J. Biol. Chem. 282:5201-5206(2007).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 232-959 IN COMPLEXES WITH
RP UDP-XYLOSE AND SUBSTRATE PEPTIDES, CATALYTIC ACTIVITY, GLYCOSYLATION AT
RP ASN-777, DISULFIDE BOND, AND MUTAGENESIS OF GLN-462; ASP-494; GLU-529;
RP ARG-557; ARG-598; LYS-599; 562-LYS--CYS-572; LYS-749; GLU-750 AND ARG-754.
RX PubMed=29681470; DOI=10.1016/j.str.2018.03.014;
RA Briggs D.C., Hohenester E.;
RT "Structural Basis for the Initiation of Glycosaminoglycan Biosynthesis by
RT Human Xylosyltransferase 1.";
RL Structure 0:0-0(2018).
RN [8]
RP INVOLVEMENT IN PXE, SUBCELLULAR LOCATION, VARIANT PXE SER-115, AND VARIANTS
RP TRP-406 AND MET-665.
RX PubMed=16571645; DOI=10.1136/jmg.2006.040972;
RA Schon S., Schulz V., Prante C., Hendig D., Szliska C., Kuhn J.,
RA Kleesiek K., Gotting C.;
RT "Polymorphisms in the xylosyltransferase genes cause higher serum XT-I
RT activity in patients with pseudoxanthoma elasticum (PXE) and are involved
RT in a severe disease course.";
RL J. Med. Genet. 43:745-749(2006).
RN [9]
RP VARIANT DBQD2 CYS-598, AND FUNCTION.
RX PubMed=24581741; DOI=10.1016/j.ajhg.2014.01.020;
RA Bui C., Huber C., Tuysuz B., Alanay Y., Bole-Feysot C., Leroy J.G.,
RA Mortier G., Nitschke P., Munnich A., Cormier-Daire V.;
RT "XYLT1 mutations in Desbuquois dysplasia type 2.";
RL Am. J. Hum. Genet. 94:405-414(2014).
RN [10]
RP VARIANT DBQD2 TRP-481, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP AND PATHWAY.
RX PubMed=23982343; DOI=10.1007/s00439-013-1351-y;
RA Schreml J., Durmaz B., Cogulu O., Keupp K., Beleggia F., Pohl E., Milz E.,
RA Coker M., Ucar S.K., Nurnberg G., Nurnberg P., Kuhn J., Ozkinay F.;
RT "The missing 'link': an autosomal recessive short stature syndrome caused
RT by a hypofunctional XYLT1 mutation.";
RL Hum. Genet. 133:29-39(2014).
RN [11]
RP INVOLVEMENT IN DBQD2, CHARACTERIZATION OF VARIANTS DBQD2 TRP-481 AND
RP CYS-598, AND SUBCELLULAR LOCATION.
RX PubMed=28462984; DOI=10.1002/ajmg.a.38244;
RA Al-Jezawi N.K., Ali B.R., Al-Gazali L.;
RT "Endoplasmic reticulum retention of xylosyltransferase 1 (XYLT1) mutants
RT underlying Desbuquois dysplasia type II.";
RL Am. J. Med. Genet. A 173:1773-1781(2017).
CC -!- FUNCTION: Catalyzes the first step in the biosynthesis of chondroitin
CC sulfate and dermatan sulfate proteoglycans, such as DCN. Transfers D-
CC xylose from UDP-D-xylose to specific serine residues of the core
CC protein (PubMed:15461586, PubMed:17189265, PubMed:24581741,
CC PubMed:23982343). Required for normal embryonic and postnatal skeleton
CC development, especially of the long bones (PubMed:24581741,
CC PubMed:23982343). Required for normal maturation of chondrocytes during
CC bone development, and normal onset of ossification (By similarity).
CC {ECO:0000250|UniProtKB:Q811B1, ECO:0000269|PubMed:15461586,
CC ECO:0000269|PubMed:17189265, ECO:0000269|PubMed:23982343,
CC ECO:0000269|PubMed:24581741}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UDP-alpha-D-xylose = 3-O-(beta-D-xylosyl)-
CC L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:50192, Rhea:RHEA-
CC COMP:9863, Rhea:RHEA-COMP:12567, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57632, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:132085; EC=2.4.2.26;
CC Evidence={ECO:0000269|PubMed:11087729, ECO:0000269|PubMed:11099377,
CC ECO:0000269|PubMed:15294915, ECO:0000269|PubMed:15461586,
CC ECO:0000269|PubMed:23982343, ECO:0000269|PubMed:29681470};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:15294915, ECO:0000269|PubMed:15461586};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.9 uM for recombinant bikunin {ECO:0000269|PubMed:15294915,
CC ECO:0000269|PubMed:15461586};
CC Vmax=764 pmol/h/mg enzyme with recombinant bikunin as substrate
CC {ECO:0000269|PubMed:15294915, ECO:0000269|PubMed:15461586};
CC -!- PATHWAY: Glycan metabolism; chondroitin sulfate biosynthesis.
CC {ECO:0000269|PubMed:17189265, ECO:0000269|PubMed:23982343}.
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC {ECO:0000269|PubMed:17189265}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15461586}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:23982343, ECO:0000269|PubMed:28462984}; Single-pass
CC type II membrane protein {ECO:0000305}. Secreted
CC {ECO:0000269|PubMed:11087729, ECO:0000269|PubMed:16571645}.
CC Note=Detected predominantly in the Golgi apparatus.
CC {ECO:0000269|PubMed:28462984}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
CC placenta, kidney and pancreas. Weakly expressed in skeletal muscle.
CC {ECO:0000269|PubMed:11099377}.
CC -!- PTM: Contains 7 disulfide bonds. {ECO:0000305|PubMed:15461586}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11087729}.
CC -!- DISEASE: Desbuquois dysplasia 2 (DBQD2) [MIM:615777]: A
CC chondrodysplasia characterized by severe prenatal and postnatal growth
CC retardation (less than -5 SD), joint laxity, short extremities,
CC progressive scoliosis, round face, midface hypoplasia, prominent
CC bulging eyes. The main radiologic features are short long bones with
CC metaphyseal splay, a 'Swedish key' appearance of the proximal femur
CC (exaggerated trochanter), and advance carpal and tarsal bone age. Two
CC forms of Desbuquois dysplasia are distinguished on the basis of the
CC presence or absence of characteristic hand anomalies: an extra
CC ossification center distal to the second metacarpal, delta phalanx,
CC bifid distal thumb phalanx, and phalangeal dislocations.
CC {ECO:0000269|PubMed:23982343, ECO:0000269|PubMed:24581741,
CC ECO:0000269|PubMed:28462984}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Pseudoxanthoma elasticum (PXE) [MIM:264800]: A multisystem
CC disorder characterized by accumulation of mineralized and fragmented
CC elastic fibers in the skin, vascular walls, and Burch membrane in the
CC eye. Clinically, patients exhibit characteristic lesions of the
CC posterior segment of the eye including peau d'orange, angioid streaks,
CC and choroidal neovascularizations, of the skin including soft, ivory
CC colored papules in a reticular pattern that predominantly affect the
CC neck and large flexor surfaces, and of the cardiovascular system with
CC peripheral and coronary arterial occlusive disease as well as
CC gastrointestinal bleedings. {ECO:0000269|PubMed:16571645}. Note=The
CC gene represented in this entry acts as a disease modifier.
CC -!- MISCELLANEOUS: Activity is strongly reduced in seminal plasma of
CC infertile men. {ECO:0000269|PubMed:11814476}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 14 family. XylT
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ539163; CAD62248.1; -; mRNA.
DR EMBL; AJ277441; CAC16787.1; -; mRNA.
DR CCDS; CCDS10569.1; -.
DR RefSeq; NP_071449.1; NM_022166.3.
DR PDB; 6EJ7; X-ray; 2.00 A; A=232-959.
DR PDB; 6EJ8; X-ray; 2.09 A; A=232-959.
DR PDB; 6EJ9; X-ray; 2.02 A; A=232-959.
DR PDB; 6EJA; X-ray; 1.94 A; A=232-959.
DR PDB; 6EJB; X-ray; 2.56 A; A=232-959.
DR PDB; 6EJC; X-ray; 2.06 A; A=232-959.
DR PDB; 6EJD; X-ray; 2.68 A; A=232-959.
DR PDB; 6EJE; X-ray; 2.43 A; A=232-959.
DR PDB; 6FOA; X-ray; 1.87 A; A=232-959.
DR PDBsum; 6EJ7; -.
DR PDBsum; 6EJ8; -.
DR PDBsum; 6EJ9; -.
DR PDBsum; 6EJA; -.
DR PDBsum; 6EJB; -.
DR PDBsum; 6EJC; -.
DR PDBsum; 6EJD; -.
DR PDBsum; 6EJE; -.
DR PDBsum; 6FOA; -.
DR AlphaFoldDB; Q86Y38; -.
DR SMR; Q86Y38; -.
DR BioGRID; 122080; 14.
DR IntAct; Q86Y38; 3.
DR MINT; Q86Y38; -.
DR STRING; 9606.ENSP00000261381; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR GlyGen; Q86Y38; 4 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q86Y38; -.
DR PhosphoSitePlus; Q86Y38; -.
DR BioMuta; XYLT1; -.
DR DMDM; 71164803; -.
DR EPD; Q86Y38; -.
DR jPOST; Q86Y38; -.
DR MassIVE; Q86Y38; -.
DR MaxQB; Q86Y38; -.
DR PaxDb; Q86Y38; -.
DR PeptideAtlas; Q86Y38; -.
DR PRIDE; Q86Y38; -.
DR ProteomicsDB; 70370; -.
DR Antibodypedia; 2316; 107 antibodies from 23 providers.
DR DNASU; 64131; -.
DR Ensembl; ENST00000261381.7; ENSP00000261381.6; ENSG00000103489.12.
DR GeneID; 64131; -.
DR KEGG; hsa:64131; -.
DR MANE-Select; ENST00000261381.7; ENSP00000261381.6; NM_022166.4; NP_071449.1.
DR UCSC; uc002dfa.4; human.
DR CTD; 64131; -.
DR DisGeNET; 64131; -.
DR GeneCards; XYLT1; -.
DR HGNC; HGNC:15516; XYLT1.
DR HPA; ENSG00000103489; Low tissue specificity.
DR MalaCards; XYLT1; -.
DR MIM; 264800; phenotype.
DR MIM; 608124; gene.
DR MIM; 615777; phenotype.
DR neXtProt; NX_Q86Y38; -.
DR OpenTargets; ENSG00000103489; -.
DR Orphanet; 1425; Desbuquois syndrome.
DR Orphanet; 370930; XYLT1-CDG.
DR PharmGKB; PA37973; -.
DR VEuPathDB; HostDB:ENSG00000103489; -.
DR eggNOG; KOG0799; Eukaryota.
DR GeneTree; ENSGT00940000157381; -.
DR HOGENOM; CLU_012840_0_0_1; -.
DR InParanoid; Q86Y38; -.
DR OMA; QYKGFLV; -.
DR OrthoDB; 564384at2759; -.
DR PhylomeDB; Q86Y38; -.
DR TreeFam; TF315534; -.
DR BioCyc; MetaCyc:HS02509-MON; -.
DR BRENDA; 2.4.2.26; 2681.
DR PathwayCommons; Q86Y38; -.
DR Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR SignaLink; Q86Y38; -.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR BioGRID-ORCS; 64131; 12 hits in 1070 CRISPR screens.
DR ChiTaRS; XYLT1; human.
DR GeneWiki; XYLT1; -.
DR GenomeRNAi; 64131; -.
DR Pharos; Q86Y38; Tbio.
DR PRO; PR:Q86Y38; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q86Y38; protein.
DR Bgee; ENSG00000103489; Expressed in tibia and 194 other tissues.
DR Genevisible; Q86Y38; HS.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0000137; C:Golgi cis cisterna; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030158; F:protein xylosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; IMP:UniProtKB.
DR GO; GO:0048706; P:embryonic skeletal system development; ISS:UniProtKB.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; TAS:UniProtKB.
DR GO; GO:0030203; P:glycosaminoglycan metabolic process; TAS:Reactome.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IMP:UniProtKB.
DR GO; GO:0043931; P:ossification involved in bone maturation; ISS:UniProtKB.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR003406; Glyco_trans_14.
DR InterPro; IPR039864; Xylosyltrans.
DR InterPro; IPR043538; XYLT.
DR InterPro; IPR024448; XylT_C.
DR PANTHER; PTHR46025; PTHR46025; 1.
DR PANTHER; PTHR46025:SF2; PTHR46025:SF2; 1.
DR Pfam; PF02485; Branch; 1.
DR Pfam; PF12529; Xylo_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disease variant; Disulfide bond;
KW Dwarfism; Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Metal-binding; Reference proteome; Secreted; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..959
FT /note="Xylosyltransferase 1"
FT /id="PRO_0000191400"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..959
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 42..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 333
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000269|PubMed:29681470,
FT ECO:0007744|PDB:6EJ7"
FT BINDING 361
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000269|PubMed:29681470,
FT ECO:0007744|PDB:6EJ7"
FT BINDING 390..392
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000269|PubMed:29681470,
FT ECO:0007744|PDB:6EJ7"
FT BINDING 494..495
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000269|PubMed:29681470,
FT ECO:0007744|PDB:6EJ7"
FT BINDING 575
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000269|PubMed:29681470,
FT ECO:0007744|PDB:6EJ7"
FT BINDING 598..599
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000269|PubMed:29681470,
FT ECO:0007744|PDB:6EJ7"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 777
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29681470,
FT ECO:0007744|PDB:6EJ7, ECO:0007744|PDB:6EJ8,
FT ECO:0007744|PDB:6FOA"
FT DISULFID 257..285
FT /evidence="ECO:0000269|PubMed:29681470,
FT ECO:0007744|PDB:6EJ7, ECO:0007744|PDB:6FOA"
FT DISULFID 301..542
FT /evidence="ECO:0000269|PubMed:29681470,
FT ECO:0007744|PDB:6EJ7, ECO:0007744|PDB:6FOA"
FT DISULFID 561..574
FT /evidence="ECO:0000269|PubMed:29681470,
FT ECO:0007744|PDB:6EJ7, ECO:0007744|PDB:6FOA"
FT DISULFID 563..572
FT /evidence="ECO:0000269|PubMed:29681470,
FT ECO:0007744|PDB:6EJ7, ECO:0007744|PDB:6FOA"
FT DISULFID 675..927
FT /evidence="ECO:0000269|PubMed:29681470,
FT ECO:0007744|PDB:6EJ7, ECO:0007744|PDB:6FOA"
FT DISULFID 920..933
FT /evidence="ECO:0000269|PubMed:29681470,
FT ECO:0007744|PDB:6EJ7, ECO:0007744|PDB:6FOA"
FT VARIANT 115
FT /note="A -> S (in PXE; acts as a modifier of disease
FT severity; results in higher serum xylosyltransferase
FT activity; dbSNP:rs61758388)"
FT /evidence="ECO:0000269|PubMed:16571645"
FT /id="VAR_071271"
FT VARIANT 325
FT /note="P -> R (in dbSNP:rs28709752)"
FT /id="VAR_049324"
FT VARIANT 406
FT /note="R -> W (in dbSNP:rs201009902)"
FT /evidence="ECO:0000269|PubMed:16571645"
FT /id="VAR_071272"
FT VARIANT 481
FT /note="R -> W (in DBQD2; causes retention in the
FT endoplasmic reticulum; impairs dermatan sulfate
FT proteoglycan synthesis; dbSNP:rs587777366)"
FT /evidence="ECO:0000269|PubMed:23982343,
FT ECO:0000269|PubMed:28462984"
FT /id="VAR_071273"
FT VARIANT 598
FT /note="R -> C (in DBQD2; causes retention in the
FT endoplasmic reticulum; dbSNP:rs587777367)"
FT /evidence="ECO:0000269|PubMed:24581741,
FT ECO:0000269|PubMed:28462984"
FT /id="VAR_071274"
FT VARIANT 665
FT /note="T -> M (in dbSNP:rs79030430)"
FT /evidence="ECO:0000269|PubMed:16571645"
FT /id="VAR_071275"
FT VARIANT 766
FT /note="P -> A (in dbSNP:rs12325439)"
FT /id="VAR_049325"
FT VARIANT 839
FT /note="V -> I (in dbSNP:rs7200466)"
FT /id="VAR_049326"
FT VARIANT 892
FT /note="R -> Q (in dbSNP:rs35309694)"
FT /id="VAR_049327"
FT MUTAGEN 257
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:15461586"
FT MUTAGEN 276
FT /note="C->A: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:15461586"
FT MUTAGEN 285
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:15461586"
FT MUTAGEN 301
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:15461586"
FT MUTAGEN 314
FT /note="D->G: No effect."
FT /evidence="ECO:0000269|PubMed:15294915"
FT MUTAGEN 316
FT /note="D->G: No effect."
FT /evidence="ECO:0000269|PubMed:15294915"
FT MUTAGEN 462
FT /note="Q->A,W: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:29681470"
FT MUTAGEN 462
FT /note="Q->R: Decreased enzyme activity."
FT /evidence="ECO:0000269|PubMed:29681470"
FT MUTAGEN 471
FT /note="C->A: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:15461586"
FT MUTAGEN 494
FT /note="D->A: Decreased enzyme activity."
FT /evidence="ECO:0000269|PubMed:29681470"
FT MUTAGEN 494
FT /note="D->N: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:29681470"
FT MUTAGEN 529
FT /note="E->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:29681470"
FT MUTAGEN 542
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:15461586"
FT MUTAGEN 557
FT /note="R->N: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:29681470"
FT MUTAGEN 561
FT /note="C->A: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:15461586"
FT MUTAGEN 562..572
FT /note="Missing: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:29681470"
FT MUTAGEN 563
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:15461586"
FT MUTAGEN 572
FT /note="C->A: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:15461586"
FT MUTAGEN 574
FT /note="C->A: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:15461586"
FT MUTAGEN 598
FT /note="R->A: Strongly decreased enzyme activity; when
FT associated with A-599."
FT /evidence="ECO:0000269|PubMed:29681470"
FT MUTAGEN 599
FT /note="K->A: Decreased enzyme activity. Strongly decreased
FT enzyme activity; when associated with A-598."
FT /evidence="ECO:0000269|PubMed:29681470"
FT MUTAGEN 675
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:15461586"
FT MUTAGEN 745
FT /note="D->E: No effect."
FT /evidence="ECO:0000269|PubMed:15294915"
FT MUTAGEN 745
FT /note="D->G: Abolishes enzyme activity but does not affect
FT UDP-binding."
FT /evidence="ECO:0000269|PubMed:15294915"
FT MUTAGEN 746
FT /note="W->D,N,G: Strongly reduced enzyme activity but does
FT not affect UDP-binding."
FT /evidence="ECO:0000269|PubMed:15294915"
FT MUTAGEN 747
FT /note="D->G,E: Reduced enzyme activity but does not affect
FT UDP-binding."
FT /evidence="ECO:0000269|PubMed:15294915"
FT MUTAGEN 749
FT /note="K->A: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:29681470"
FT MUTAGEN 750
FT /note="E->K: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:29681470"
FT MUTAGEN 754
FT /note="R->E: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:29681470"
FT MUTAGEN 920
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:15461586"
FT MUTAGEN 927
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:15461586"
FT MUTAGEN 933
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:15461586"
FT HELIX 262..270
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 274..288
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 328..334
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 339..349
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 365..377
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 396..410
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 417..422
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 432..441
FT /evidence="ECO:0007829|PDB:6FOA"
FT TURN 442..444
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 455..462
FT /evidence="ECO:0007829|PDB:6FOA"
FT TURN 463..465
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 474..480
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 500..508
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 512..520
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 527..529
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 531..538
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 542..544
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 545..547
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 550..553
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 557..560
FT /evidence="ECO:0007829|PDB:6FOA"
FT TURN 564..568
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 581..588
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:6FOA"
FT TURN 602..604
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 607..617
FT /evidence="ECO:0007829|PDB:6FOA"
FT TURN 625..628
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 629..636
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 637..639
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 641..643
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 646..665
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 677..691
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 694..706
FT /evidence="ECO:0007829|PDB:6FOA"
FT TURN 707..710
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 711..721
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 737..747
FT /evidence="ECO:0007829|PDB:6FOA"
FT TURN 748..751
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 752..755
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 767..772
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 774..776
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 778..785
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 791..799
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 805..808
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 818..827
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 830..839
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 843..845
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 852..859
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 865..870
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 873..875
FT /evidence="ECO:0007829|PDB:6FOA"
FT TURN 876..880
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 885..895
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 899..913
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 914..923
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 933..935
FT /evidence="ECO:0007829|PDB:6FOA"
FT STRAND 936..939
FT /evidence="ECO:0007829|PDB:6FOA"
FT HELIX 945..947
FT /evidence="ECO:0007829|PDB:6FOA"
SQ SEQUENCE 959 AA; 107569 MW; 056FC3F66EFD4D81 CRC64;
MVAAPCARRL ARRSHSALLA ALTVLLLQTL VVWNFSSLDS GAGERRGGAA VGGGEQPPPA
PAPRRERRDL PAEPAAARGG GGGGGGGGGG RGPQARARGG GPGEPRGQQP ASRGALPARA
LDPHPSPLIT LETQDGYFSH RPKEKVRTDS NNENSVPKDF ENVDNSNFAP RTQKQKHQPE
LAKKPPSRQK ELLKRKLEQQ EKGKGHTFPG KGPGEVLPPG DRAAANSSHG KDVSRPPHAR
KTGGSSPETK YDQPPKCDIS GKEAISALSR AKSKHCRQEI GETYCRHKLG LLMPEKVTRF
CPLEGKANKN VQWDEDSVEY MPANPVRIAF VLVVHGRASR QLQRMFKAIY HKDHFYYIHV
DKRSNYLHRQ VLQVSRQYSN VRVTPWRMAT IWGGASLLST YLQSMRDLLE MTDWPWDFFI
NLSAADYPIR TNDQLVAFLS RYRDMNFLKS HGRDNARFIR KQGLDRLFLE CDAHMWRLGD
RRIPEGIAVD GGSDWFLLNR RFVEYVTFST DDLVTKMKQF YSYTLLPAES FFHTVLENSP
HCDTMVDNNL RITNWNRKLG CKCQYKHIVD WCGCSPNDFK PQDFHRFQQT ARPTFFARKF
EAVVNQEIIG QLDYYLYGNY PAGTPGLRSY WENVYDEPDG IHSLSDVTLT LYHSFARLGL
RRAETSLHTD GENSCRYYPM GHPASVHLYF LADRFQGFLI KHHATNLAVS KLETLETWVM
PKKVFKIASP PSDFGRLQFS EVGTDWDAKE RLFRNFGGLL GPMDEPVGMQ KWGKGPNVTV
TVIWVDPVNV IAATYDILIE STAEFTHYKP PLNLPLRPGV WTVKILHHWV PVAETKFLVA
PLTFSNRQPI KPEEALKLHN GPLRNAYMEQ SFQSLNPVLS LPINPAQVEQ ARRNAASTGT
ALEGWLDSLV GGMWTAMDIC ATGPTACPVM QTCSQTAWSS FSPDPKSELG AVKPDGRLR
