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XYLT1_RAT
ID   XYLT1_RAT               Reviewed;         821 AA.
AC   Q9EPI1;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Xylosyltransferase 1;
DE            EC=2.4.2.26 {ECO:0000250|UniProtKB:Q86Y38};
DE   AltName: Full=Peptide O-xylosyltransferase 1;
DE   AltName: Full=Xylosyltransferase I;
DE   Flags: Fragment;
GN   Name=Xylt1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
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).
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. Required for normal maturation of chondrocytes during bone
CC       development, normal onset of ossification and normal embryonic and
CC       postnatal skeleton development, especially of the long bones.
CC       {ECO:0000250|UniProtKB:Q811B1}.
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:0000250|UniProtKB:Q86Y38};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:Q86Y38};
CC   -!- PATHWAY: Glycan metabolism; chondroitin sulfate biosynthesis.
CC       {ECO:0000250|UniProtKB:Q86Y38}.
CC   -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC       {ECO:0000250|UniProtKB:Q86Y38}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q86Y38}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q86Y38}; Single-pass type II membrane protein
CC       {ECO:0000250}.
CC   -!- PTM: Contains 7 disulfide bonds. {ECO:0000250|UniProtKB:Q86Y38}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q86Y38}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 14 family. XylT
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AJ295748; CAC16797.1; -; mRNA.
DR   AlphaFoldDB; Q9EPI1; -.
DR   SMR; Q9EPI1; -.
DR   STRING; 10116.ENSRNOP00000025008; -.
DR   CAZy; GT14; Glycosyltransferase Family 14.
DR   GlyGen; Q9EPI1; 3 sites.
DR   PaxDb; Q9EPI1; -.
DR   PRIDE; Q9EPI1; -.
DR   UCSC; RGD:620093; rat.
DR   RGD; 620093; Xylt1.
DR   eggNOG; KOG0799; Eukaryota.
DR   InParanoid; Q9EPI1; -.
DR   PhylomeDB; Q9EPI1; -.
DR   Reactome; R-RNO-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR   UniPathway; UPA00755; -.
DR   UniPathway; UPA00756; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0000137; C:Golgi cis cisterna; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030158; F:protein xylosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0034605; P:cellular response to heat; ISO:RGD.
DR   GO; GO:0030206; P:chondroitin sulfate biosynthetic process; ISO:RGD.
DR   GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0048706; P:embryonic skeletal system development; ISS:UniProtKB.
DR   GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0048681; P:negative regulation of axon regeneration; IMP:RGD.
DR   GO; GO:0043931; P:ossification involved in bone maturation; ISS:UniProtKB.
DR   GO; GO:0030166; P:proteoglycan biosynthetic process; IMP:RGD.
DR   GO; GO:0070555; P:response to interleukin-1; IEP:RGD.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW   Membrane; Metal-binding; Reference proteome; Transferase.
FT   CHAIN           <1..821
FT                   /note="Xylosyltransferase 1"
FT                   /id="PRO_0000191403"
FT   TOPO_DOM        <1..821
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          1..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          801..821
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         198
FT                   /ligand="UDP-alpha-D-xylose"
FT                   /ligand_id="ChEBI:CHEBI:57632"
FT                   /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT   BINDING         226
FT                   /ligand="UDP-alpha-D-xylose"
FT                   /ligand_id="ChEBI:CHEBI:57632"
FT                   /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT   BINDING         255..257
FT                   /ligand="UDP-alpha-D-xylose"
FT                   /ligand_id="ChEBI:CHEBI:57632"
FT                   /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT   BINDING         359..360
FT                   /ligand="UDP-alpha-D-xylose"
FT                   /ligand_id="ChEBI:CHEBI:57632"
FT                   /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT   BINDING         440
FT                   /ligand="UDP-alpha-D-xylose"
FT                   /ligand_id="ChEBI:CHEBI:57632"
FT                   /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT   BINDING         463..464
FT                   /ligand="UDP-alpha-D-xylose"
FT                   /ligand_id="ChEBI:CHEBI:57632"
FT                   /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        286
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        642
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        122..150
FT                   /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT   DISULFID        166..407
FT                   /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT   DISULFID        426..439
FT                   /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT   DISULFID        428..437
FT                   /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT   DISULFID        540..789
FT                   /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT   DISULFID        782..795
FT                   /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT   NON_TER         1
SQ   SEQUENCE   821 AA;  93859 MW;  75186697AD3428A3 CRC64;
     YFSHRPKEKV RTDSNNENSV PKDFENVDNS NFAPRTQKQK HQPELAKKPL SRQKERLQRK
     LGAQDKGQGQ SVLGKGPKEV LPPREKAPGN SSQGKDLSRH SHSRKSGGGG SPETKSDQVP
     KCDISGKEAI SALTRAKSKH CRQEIAETYC RHKLGLLMPE KVARFCPLEG KANKNVQWDE
     DAVEYMPPNP VRIAFVLVVH GRASRQLQRM FKAIYHKDHF YYIHVDKRSN YLHRQVLQFS
     RQYDNVRVTS WRMATIWGGA SLLSTYLQSM RDLLEMTDWP WDFFINLSAA DYPIRTNDQL
     VAFLSRYRDM NFLKSHGRDN ARFIRKQDLD RLFLECDTHM WRLGDRRIPE GIAVDGGSDW
     FLLNRKFVEY VAFSTDDLVT KMKQFYSYTL LPAESFFHTV LENSPHCDTM VDNNLRITNW
     NRKLGCKCQY KHIVDWCGCS PNDFKPQDFH RFQQTARPTF FARKFEAIVN QEIIGQLDSY
     LYGNYPAGTP GLRSYWENVY DEPDGIQSLS DVALTMYHSF IRLGLRRAES SLHTDGENSC
     RYYPMGHPAS VHLYFLADRF QGFLIKHHVT NLAVSKLETL ETWMMPKKVF KVASPPSDFG
     RLQFSEVGTD WDAKERLFRN FGGLLGPMDE PVGMQKWGKG PNVTVTVIWV DPVNVIAATY
     DILIESTAEF THYKPPLNLP LRPGVWTVKI LHHWVPVAET KFLVAPLTFS NKQPIKPEEA
     LKLHNGPPRS AYMEQSFQSL NPVLSLHINP AQVEQARKNA AFTGTALEAW LVGGTWTAMD
     VCATGPTACP VMQTCSQTAW SSFSPDPKSE LGAVKPDGRL R
 
 
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