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NDST_CAEEL
ID   NDST_CAEEL              Reviewed;         852 AA.
AC   Q966W3; Q19197; Q966W4; Q966W5; Q966W6;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1;
DE            EC=2.8.2.8;
DE   AltName: Full=Glucosaminyl N-deacetylase/N-sulfotransferase 1;
DE   Includes:
DE     RecName: Full=Heparan sulfate N-deacetylase 1;
DE              EC=3.-.-.-;
DE   Includes:
DE     RecName: Full=Heparan sulfate N-sulfotransferase 1;
DE              EC=2.8.2.-;
GN   Name=hst-1; ORFNames=F08B4.6;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Aikawa J.;
RT   "Molecular characterization of N-deacetylase/N-sulfotransferase in worm.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RA   Aikawa J.;
RT   "Structure and function of heparan sulfate/heparin N-deacetylase/ N-
RT   sulfotransferase in worm.";
RL   (In) Proceedings of the 14th international C. elegans meeting, pp.345-345,
RL   Los Angeles (2003).
CC   -!- FUNCTION: Essential bifunctional enzyme that catalyzes both the N-
CC       deacetylation and the N-sulfation of glucosamine (GlcNAc) of the
CC       glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA
CC       disaccharide repeating sugar backbone to make N-sulfated heparosan, a
CC       prerequisite substrate for later modifications in heparin biosynthesis
CC       (Probable). {ECO:0000305|Ref.3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan
CC         sulfate](n) = adenosine 3',5'-bisphosphate + 2 H(+) + N-sulfo-alpha-
CC         D-glucosaminyl-[heparan sulfate](n); Xref=Rhea:RHEA:21980, Rhea:RHEA-
CC         COMP:9830, Rhea:RHEA-COMP:14602, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:58388,
CC         ChEBI:CHEBI:140572; EC=2.8.2.8;
CC   -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC   -!- PATHWAY: Glycan metabolism; heparin biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Present in some specific neurons in head and tail
CC       regions and muscles. {ECO:0000269|Ref.3}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. NDST subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB037941; BAB61756.1; -; mRNA.
DR   EMBL; AB037942; BAB61757.1; -; mRNA.
DR   EMBL; AB037943; BAB61758.1; -; mRNA.
DR   EMBL; AB038044; BAB62394.1; -; mRNA.
DR   EMBL; FO080903; CCD67652.2; -; Genomic_DNA.
DR   PIR; T29486; T29486.
DR   RefSeq; NP_501491.4; NM_069090.4.
DR   AlphaFoldDB; Q966W3; -.
DR   SMR; Q966W3; -.
DR   STRING; 6239.F08B4.6; -.
DR   EPD; Q966W3; -.
DR   PaxDb; Q966W3; -.
DR   EnsemblMetazoa; F08B4.6.1; F08B4.6.1; WBGene00002028.
DR   GeneID; 177675; -.
DR   KEGG; cel:CELE_F08B4.6; -.
DR   UCSC; F08B4.6; c. elegans.
DR   CTD; 177675; -.
DR   WormBase; F08B4.6; CE46914; WBGene00002028; hst-1.
DR   eggNOG; KOG3703; Eukaryota.
DR   GeneTree; ENSGT00940000168016; -.
DR   HOGENOM; CLU_011357_2_0_1; -.
DR   InParanoid; Q966W3; -.
DR   OMA; EMHLNYA; -.
DR   OrthoDB; 388292at2759; -.
DR   PhylomeDB; Q966W3; -.
DR   Reactome; R-CEL-2022928; HS-GAG biosynthesis.
DR   UniPathway; UPA00756; -.
DR   UniPathway; UPA00862; -.
DR   PRO; PR:Q966W3; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00002028; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015016; F:[heparan sulfate]-glucosamine N-sulfotransferase activity; IBA:GO_Central.
DR   GO; GO:0019213; F:deacetylase activity; IBA:GO_Central.
DR   GO; GO:0015014; P:heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; IBA:GO_Central.
DR   GO; GO:0030210; P:heparin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR021930; Heparan_SO4_deacetylase.
DR   InterPro; IPR037359; NST/OST.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000863; Sulfotransferase_dom.
DR   PANTHER; PTHR10605; PTHR10605; 1.
DR   Pfam; PF12062; HSNSD; 1.
DR   Pfam; PF00685; Sulfotransfer_1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Golgi apparatus; Hydrolase; Membrane;
KW   Multifunctional enzyme; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..852
FT                   /note="Bifunctional heparan sulfate N-deacetylase/N-
FT                   sulfotransferase 1"
FT                   /id="PRO_0000225664"
FT   TOPO_DOM        1..13
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        14..34
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..852
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          34..574
FT                   /note="Heparan sulfate N-deacetylase 1"
FT   REGION          575..852
FT                   /note="Heparan sulfate N-sulfotransferase 1"
FT   ACT_SITE        592
FT                   /note="For sulfotransferase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         592..596
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         686
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         803..807
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        261
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        328
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        377
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        428
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        576
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        607
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        712
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        789..798
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   852 AA;  99061 MW;  1DD390CCDA5EDE21 CRC64;
     MIITPYLNRK ITRPLKWILA LIFLYLIYIC LFSNNSKPPK PRKKPKLVEN YTCPFARTEG
     TASENLFFHT NNGTDARILV ILDSLFSRHG KTIIQILNSQ KLQFKAEAVS KNLPVLTTSR
     RGRYSLIIIE NYYKYLNMAQ WNRQLLDKYC KEYRVPMFSF MSSKPNDQLK RIKIKGSSLW
     MWQNQRIQRL AVTPSIIHRI SKIGNYRQFS SSDPADWILF ETSEKFESVL SGTVKSGYER
     AVVVRDKGLE DGVERIIFGR NLTDFQVKIT FLDALWWAMG NQKSFTLDRF VQVDIDDVFV
     GAQGTRIVEE DVRKLISTQK EFRNYVQNFT FMLGFSGSYF RNGDDLEDRG DEFLVENAEK
     FVWFPHMWRH NHAHEHNFTY LEAIMAQNKL FAQNMHLPVD YPYAIAPQHD GVFPVHEQLF
     RAWRKVWNVS VTATEEYPHF KPATARKGFI HAGIHVLPRQ TCGLYTHTQL FDEYPEGFDK
     VQKSIEGGDL FFTILLNPIS IFMTHQQNYA YDRLALYTFE NLFRFIKCWT NIKLKWQDPL
     TSSQLYFQKF PDERTPLWTN PCTDPRHHAI LPPSINCTKK SLPDLLIIGP QKTGSTALAS
     FLSLHPNTSQ NTPVPGSFEE VQFFGGQNYL KGVEWYMSNF PSSSTVTFEK SATYFDNPSA
     PKQAASLVPH AKIVIILQNP AQRAYSWFQH ILAHEDPVAI TAGSLEVILD SNSTSSKKVR
     QRCISGGRYV HHLTKWLEHF SLQQMIFVDS DELKMKPPTV LNSLSKWLDL PEFPFETYIR
     YSPSKGFHCR LLDGKTKCLG ESKGRKYPEM PENLRRKLDK IFSLDNSALY KFLRKNRLKI
     PTWLEESVRI RA
 
 
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