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NDST4_HUMAN
ID   NDST4_HUMAN             Reviewed;         872 AA.
AC   Q9H3R1; Q2KHM8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 4;
DE            EC=2.8.2.8;
DE   AltName: Full=Glucosaminyl N-deacetylase/N-sulfotransferase 4;
DE            Short=NDST-4;
DE   AltName: Full=N-heparan sulfate sulfotransferase 4;
DE            Short=N-HSST 4;
DE   Includes:
DE     RecName: Full=Heparan sulfate N-deacetylase 4;
DE              EC=3.-.-.-;
DE   Includes:
DE     RecName: Full=Heparan sulfate N-sulfotransferase 4;
DE              EC=2.8.2.-;
GN   Name=NDST4; Synonyms=HSST4;
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] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=11087757; DOI=10.1074/jbc.m009606200;
RA   Aikawa J., Grobe K., Tsujimoto M., Esko J.D.;
RT   "Multiple isozymes of heparan sulfate/heparin GlcNAc N-deacetylase/GlcN N-
RT   sulfotransferase. Structure and activity of the fourth member, NDST4.";
RL   J. Biol. Chem. 276:5876-5882(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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: 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       Has low deacetylase activity but high sulfotransferase activity (By
CC       similarity). {ECO:0000250}.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9H3R1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H3R1-2; Sequence=VSP_056256, VSP_056257, VSP_056258;
CC   -!- MISCELLANEOUS: The presence of 4 different heparan sulfate N-
CC       deacetylase/N-sulfotransferase enzymes in mammals, as well as
CC       differences in their enzyme activity suggest that some initiate heparan
CC       sulfate modification/sulfation reactions, whereas other later on fill
CC       in or extend already modified heparan sulfate sequences.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. NDST subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB036429; BAB18535.1; -; mRNA.
DR   EMBL; AC093656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC097519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC109821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC110777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC113075; AAI13076.1; -; mRNA.
DR   CCDS; CCDS3706.1; -. [Q9H3R1-1]
DR   RefSeq; NP_072091.1; NM_022569.2. [Q9H3R1-1]
DR   AlphaFoldDB; Q9H3R1; -.
DR   SMR; Q9H3R1; -.
DR   BioGRID; 122205; 7.
DR   IntAct; Q9H3R1; 1.
DR   STRING; 9606.ENSP00000264363; -.
DR   GlyGen; Q9H3R1; 5 sites.
DR   iPTMnet; Q9H3R1; -.
DR   PhosphoSitePlus; Q9H3R1; -.
DR   BioMuta; NDST4; -.
DR   DMDM; 74718249; -.
DR   jPOST; Q9H3R1; -.
DR   MassIVE; Q9H3R1; -.
DR   MaxQB; Q9H3R1; -.
DR   PaxDb; Q9H3R1; -.
DR   PeptideAtlas; Q9H3R1; -.
DR   PRIDE; Q9H3R1; -.
DR   ProteomicsDB; 80743; -. [Q9H3R1-1]
DR   Antibodypedia; 2469; 106 antibodies from 16 providers.
DR   DNASU; 64579; -.
DR   Ensembl; ENST00000264363.7; ENSP00000264363.2; ENSG00000138653.10. [Q9H3R1-1]
DR   Ensembl; ENST00000504854.1; ENSP00000423218.1; ENSG00000138653.10. [Q9H3R1-2]
DR   Ensembl; ENST00000613194.4; ENSP00000483949.1; ENSG00000138653.10. [Q9H3R1-2]
DR   GeneID; 64579; -.
DR   KEGG; hsa:64579; -.
DR   MANE-Select; ENST00000264363.7; ENSP00000264363.2; NM_022569.3; NP_072091.1.
DR   UCSC; uc003ibu.4; human. [Q9H3R1-1]
DR   CTD; 64579; -.
DR   DisGeNET; 64579; -.
DR   GeneCards; NDST4; -.
DR   HGNC; HGNC:20779; NDST4.
DR   HPA; ENSG00000138653; Tissue enriched (brain).
DR   MIM; 615039; gene.
DR   neXtProt; NX_Q9H3R1; -.
DR   OpenTargets; ENSG00000138653; -.
DR   PharmGKB; PA134875549; -.
DR   VEuPathDB; HostDB:ENSG00000138653; -.
DR   eggNOG; KOG3703; Eukaryota.
DR   GeneTree; ENSGT00940000157168; -.
DR   HOGENOM; CLU_011357_2_0_1; -.
DR   InParanoid; Q9H3R1; -.
DR   OMA; FQYQMVI; -.
DR   PhylomeDB; Q9H3R1; -.
DR   TreeFam; TF313193; -.
DR   BioCyc; MetaCyc:HS06527-MON; -.
DR   BRENDA; 2.8.2.8; 2681.
DR   PathwayCommons; Q9H3R1; -.
DR   Reactome; R-HSA-2022928; HS-GAG biosynthesis.
DR   SignaLink; Q9H3R1; -.
DR   UniPathway; UPA00756; -.
DR   UniPathway; UPA00862; -.
DR   BioGRID-ORCS; 64579; 6 hits in 1057 CRISPR screens.
DR   ChiTaRS; NDST4; human.
DR   GenomeRNAi; 64579; -.
DR   Pharos; Q9H3R1; Tbio.
DR   PRO; PR:Q9H3R1; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q9H3R1; protein.
DR   Bgee; ENSG00000138653; Expressed in palpebral conjunctiva and 50 other tissues.
DR   Genevisible; Q9H3R1; HS.
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   Alternative splicing; Disulfide bond; Glycoprotein; Golgi apparatus;
KW   Hydrolase; Membrane; Multifunctional enzyme; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..872
FT                   /note="Bifunctional heparan sulfate N-deacetylase/N-
FT                   sulfotransferase 4"
FT                   /id="PRO_0000225661"
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..872
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          36..588
FT                   /note="Heparan sulfate N-deacetylase 4"
FT   REGION          589..872
FT                   /note="Heparan sulfate N-sulfotransferase 4"
FT   ACT_SITE        604
FT                   /note="For sulfotransferase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         604..608
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         702
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         823..827
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        226
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        341
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        391
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        657
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        793
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        808..818
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..379
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_056256"
FT   VAR_SEQ         706..748
FT                   /note="HQRSHEDPAALRFNFYEVISTGHWAPSDLKTLQRRCLVPGWYA -> VGVQW
FT                   RDLGSLQPSPPRFMPFSCLSLLSSWDYSTNDHMKIQLL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_056257"
FT   VAR_SEQ         749..872
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_056258"
FT   VARIANT         12
FT                   /note="R -> Q (in dbSNP:rs35181627)"
FT                   /id="VAR_061890"
SQ   SEQUENCE   872 AA;  100716 MW;  9C4E2DD1F98EA859 CRC64;
     MNLIVKLRRS FRTLIVLLAT FCLVSIVISA YFLYSGYKQE MTLIETTAEA ECTDIKILPY
     RSMELKTVKP IDTSKTDPTV LLFVESQYSQ LGQDIIAILE SSRFQYHMVI APGKGDIPPL
     TDNGKGKYTL VIYENILKYV SMDSWNRELL EKYCVEYSVS IIGFHKANEN SLPSTQLKGF
     PLNLFNNLAL KDCFVNPQSP LLHITKAPKV EKGPLPGEDW TIFQYNHSTY QPVLLTELQT
     EKSLSSLSSK TLFATVIQDL GLHDGIQRVL FGNNLNFWLH KLIFIDAISF LSGKRLTLSL
     DRYILVDIDD IFVGKEGTRM NVKDVKALLE TQNLLRTQVA NFTFNLGFSG KFYHTGTEEE
     DEGDDLLLRS VDEFWWFPHM WSHMQPHLFH NESSLVEQMI LNKEFALEHG IPINMGYAVA
     PHHSGVYPVH IQLYAAWKKV WGIQVTSTEE YPHLKPARYR KGFIHNSIMV LPRQTCGLFT
     HTIFYKEYPG GPQELDKSIR GGELFLTILL NPISIFMTHL SNYGNDRLGL YTFVNLVNFV
     QSWTNLKLQT LPPVQLAHQY FELFPEQKDP LWQNPCDDKR HKDIWSREKT CDHLPKFLVI
     GPQKTGTTAL YLFLLMHPSI ISNLPSPKTF EEVQFFNGNN YHKGIDWYMD FFPTPSNTTS
     DFLFEKSANY FHSEEAPRRA ASLVPKAKII TILIDPSDRA YSWYQHQRSH EDPAALRFNF
     YEVISTGHWA PSDLKTLQRR CLVPGWYAVH IERWLTYFAT SQLLIIDGQQ LRSDPATVMD
     EVQKFLGVTP RYNYSEALTF DPQKGFWCQL LEGGKTKCLG KSKGRKYPPM DPESRTFLSN
     YYRDHNVELS KLLHRLGQPL PSWLRQELQK VR
 
 
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