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Database: UniProt
Entry: A0A183W8U2_TRIRE
LinkDB: A0A183W8U2_TRIRE
Original site: A0A183W8U2_TRIRE 
ID   A0A183W8U2_TRIRE        Unreviewed;       316 AA.
AC   A0A183W8U2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Heparan-sulfate 6-O-sulfotransferase {ECO:0000256|RuleBase:RU364122};
DE            EC=2.8.2.- {ECO:0000256|RuleBase:RU364122};
OS   Trichobilharzia regenti (Nasal bird schistosome).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Trichobilharzia.
OX   NCBI_TaxID=157069 {ECO:0000313|WBParaSite:TRE_0000915801-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TRE_0000915801-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
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|RuleBase:RU364122}; Single-
CC       pass type II membrane protein {ECO:0000256|RuleBase:RU364122}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 6 family.
CC       {ECO:0000256|RuleBase:RU364122}.
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DR   AlphaFoldDB; A0A183W8U2; -.
DR   STRING; 157069.A0A183W8U2; -.
DR   WBParaSite; TRE_0000915801-mRNA-1; TRE_0000915801-mRNA-1; TRE_0000915801.
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   PANTHER; PTHR12812; HEPARAN SULFATE 6-O-SULFOTRANSFERASE 3; 1.
DR   PANTHER; PTHR12812:SF0; HEPARAN-SULFATE 6-O-SULFOTRANSFERASE; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|RuleBase:RU364122};
KW   Signal-anchor {ECO:0000256|RuleBase:RU364122};
KW   Transferase {ECO:0000256|RuleBase:RU364122};
KW   Transmembrane {ECO:0000256|RuleBase:RU364122}.
SQ   SEQUENCE   316 AA;  37275 MW;  4B81DC0E10154800 CRC64;
     LRDPIDRFIS EWQHTRRGAT WISASLRCNR QSPPFKYYKP CSFFIDNNND DDGNINTTDW
     LNISMQSFLN CPYNLAHNRQ TRMLANLSRL ECYKHLTEWS QPVNNTTSLT SISPVQLALL
     NSAKHNLVSV IRCYGLSEYL VYSQYILQKC LCITFKRSFI EFNKLSFIQQ RLMYTHAAIA
     RSNLSSNVLE KIANVNRLDI LLHNFAEKLF TYRLVRYLLF DSSLPMHFKR PLYTLWAYYY
     KYKSDTPLRI LLFSNLIDYD NSNSTANTSR LSSFSYRLNL FLTHLFIRKG SVPVAETVLI
     NENRRWRKKL AYDLKA
//
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