ID   B7Z2U5_HUMAN            Unreviewed;       486 AA.
AC   B7Z2U5;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Heparan-sulfate 6-O-sulfotransferase {ECO:0000256|RuleBase:RU364122};
DE            EC=2.8.2.- {ECO:0000256|RuleBase:RU364122};
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 {ECO:0000313|EMBL:BAH11981.1};
RN   [1] {ECO:0000313|EMBL:BAH11981.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:BAH11981.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA   Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA   Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA   Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: 6-O-sulfation enzyme which catalyzes the transfer of sulfate
CC       from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the
CC       N-sulfoglucosamine residue (GlcNS) of heparan sulfate.
CC       {ECO:0000256|RuleBase:RU364122}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan
CC         sulfate](n) = 6-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) +
CC         adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:56604, Rhea:RHEA-
CC         COMP:9830, Rhea:RHEA-COMP:14621, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:58388,
CC         ChEBI:CHEBI:140604; Evidence={ECO:0000256|RuleBase:RU364122};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606,
CC       ECO:0000256|RuleBase:RU364122}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606, ECO:0000256|RuleBase:RU364122}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 6 family.
CC       {ECO:0000256|ARBA:ARBA00010109, ECO:0000256|RuleBase:RU364122}.
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DR   EMBL; AK295118; BAH11981.1; -; mRNA.
DR   AlphaFoldDB; B7Z2U5; -.
DR   PeptideAtlas; B7Z2U5; -.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProt.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008146; F:sulfotransferase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR010635; Heparan_SO4-6-sulfoTrfase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005331; Sulfotransferase.
DR   PANTHER; PTHR12812; HEPARAN SULFATE 6-O-SULFOTRANSFERASE 3; 1.
DR   PANTHER; PTHR12812:SF6; HEPARAN-SULFATE 6-O-SULFOTRANSFERASE 2; 1.
DR   Pfam; PF03567; Sulfotransfer_2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   2: Evidence at transcript level;
KW   Membrane {ECO:0000256|RuleBase:RU364122}; Signal {ECO:0000256|SAM:SignalP};
KW   Signal-anchor {ECO:0000256|RuleBase:RU364122};
KW   Transferase {ECO:0000256|RuleBase:RU364122, ECO:0000313|EMBL:BAH11981.1};
KW   Transmembrane {ECO:0000256|RuleBase:RU364122}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..486
FT                   /note="Heparan-sulfate 6-O-sulfotransferase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002866146"
FT   REGION          169..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..479
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   486 AA;  56241 MW;  F790D30CF96779D4 CRC64;
     MLFLFAVIVL QYVCPGTECQ LLRLQAFSSP VPDPYRSEDE SSARFVPRYN FTRGDLLRKV
     DFDIKGDDLI VFLHIQKTGG TTFGRHLVRN IQLEQPCECR VGQKKCTCHR PGKRETWLFS
     RFSTGWSCGL HADWTELTSC VPSVVDGKRD ARLRPSRWRI FQILDAASKD KRGSPNTNAG
     ANSPSSTKTR NTSKSGKNFH YITILRDPVS RYLSEWRHVQ RGATWKASLH VCDGRPPTSE
     ELPSCYTGDD WSGCPLKEFM DCPYNLANNR QVRMLSDLTL VGCYNLSVMP EKQRNKVLLE
     SAKSNLKHMA FFGLTEFQRK TQYLFEKTFN MNFISPFTQY NTTRASSVEI NEEIQKRIEG
     LNFLDMELYS YAKDLFLQRY QFMRQKEHQE ARRKRQEQRK FLKGRLLQTH FQSQGQGQSQ
     NPNQNQSQNP NPNANQNLTQ NLMQNLTQSL SQKENRESPK QNSGKEQNDN TSNGTNDYIG
     SVEKWR
//