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Database: UniProt
Entry: A0A0N4WKV5_HAEPC
LinkDB: A0A0N4WKV5_HAEPC
Original site: A0A0N4WKV5_HAEPC 
ID   A0A0N4WKV5_HAEPC        Unreviewed;       366 AA.
AC   A0A0N4WKV5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Heparan-sulfate 6-O-sulfotransferase {ECO:0000256|RuleBase:RU364122};
DE            EC=2.8.2.- {ECO:0000256|RuleBase:RU364122};
GN   ORFNames=HPLM_LOCUS11729 {ECO:0000313|EMBL:VDO43675.1};
OS   Haemonchus placei (Barber's pole worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX   NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0001173701-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:HPLM_0001173701-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO43675.1, ECO:0000313|Proteomes:UP000268014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHpl1 {ECO:0000313|EMBL:VDO43675.1,
RC   ECO:0000313|Proteomes:UP000268014};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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|RuleBase:RU364122}; Single-
CC       pass type II membrane protein {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; UZAF01017645; VDO43675.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N4WKV5; -.
DR   STRING; 6290.A0A0N4WKV5; -.
DR   WBParaSite; HPLM_0001173701-mRNA-1; HPLM_0001173701-mRNA-1; HPLM_0001173701.
DR   OMA; HRNYLVE; -.
DR   Proteomes; UP000038042; Unplaced.
DR   Proteomes; UP000268014; Unassembled WGS sequence.
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:SF0; HEPARAN-SULFATE 6-O-SULFOTRANSFERASE; 1.
DR   Pfam; PF03567; Sulfotransfer_2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|RuleBase:RU364122};
KW   Reference proteome {ECO:0000313|Proteomes:UP000268014};
KW   Signal-anchor {ECO:0000256|RuleBase:RU364122};
KW   Transferase {ECO:0000256|RuleBase:RU364122};
KW   Transmembrane {ECO:0000256|RuleBase:RU364122};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU364122}.
FT   TRANSMEM        18..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364122"
SQ   SEQUENCE   366 AA;  43099 MW;  0D6960C8CF2862CF CRC64;
     MLRRQDNRVN ATTFHRKLTV FVLVIFCAPA VYLIIDVTEW DTSFDHLIEN PELGWVWIHC
     YGDCNLSSRN YCRFSIAGND VLVFVHIQKT AGTSFEKFLV RHLDIERPCQ CSKGKKRCSC
     LRPNKRNEVW LFSRYSTGWL CGLHADFTEL YVSGCVDNAL NKKEGARRMR RYFYTTFLRE
     PISRFISEYR HVNRGATWIA SRHICNGRAP TSDELPLCFD PNTGWDDVSL DEFMMCPFNL
     AFNRQTRMLA DLTLVNCYVR NGTDPATRDR VLLESAKRNL NLRLESDHQI YKIYPTWFAF
     SFNRRLSDWS RSKSNDTNVS SEQLKEIRTR NQLDIELYNY ALKLFEHRLA VVQNQSKHRF
     RKTCVC
//
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