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Database: UniProt
Entry: E3LE34_CAERE
LinkDB: E3LE34_CAERE
Original site: E3LE34_CAERE 
ID   E3LE34_CAERE            Unreviewed;       295 AA.
AC   E3LE34;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Heparan-sulfate 6-O-sulfotransferase {ECO:0000256|RuleBase:RU364122};
DE            EC=2.8.2.- {ECO:0000256|RuleBase:RU364122};
GN   Name=Cre-hst-6 {ECO:0000313|EMBL:EFO82261.1};
GN   ORFNames=CRE_00741 {ECO:0000313|EMBL:EFO82261.1};
OS   Caenorhabditis remanei (Caenorhabditis vulgaris).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN   [1] {ECO:0000313|Proteomes:UP000008281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG   Caenorhabditis remanei Sequencing Consortium;
RA   Wilson R.K.;
RT   "PCAP assembly of the Caenorhabditis remanei genome.";
RL   Submitted (JUL-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|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; DS268407; EFO82261.1; -; Genomic_DNA.
DR   RefSeq; XP_003117663.1; XM_003117615.1.
DR   AlphaFoldDB; E3LE34; -.
DR   STRING; 31234.E3LE34; -.
DR   EnsemblMetazoa; CRE00741.1; CRE00741.1; WBGene00051704.
DR   eggNOG; KOG3955; Eukaryota.
DR   HOGENOM; CLU_027877_2_0_1; -.
DR   InParanoid; E3LE34; -.
DR   OrthoDB; 2896660at2759; -.
DR   Proteomes; UP000008281; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008146; F:sulfotransferase activity; IEA:InterPro.
DR   GO; GO:0015015; P:heparan sulfate proteoglycan biosynthetic process, enzymatic modification; IEA:EnsemblMetazoa.
DR   GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:EnsemblMetazoa.
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.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|RuleBase:RU364122};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008281};
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        20..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364122"
SQ   SEQUENCE   295 AA;  34531 MW;  1B440E32868243EC CRC64;
     MKKMGMCSLR GWKGVLGRKL FVFATILFVA SIVYFYIDFP LKISNRILEN GYHQHEDDVY
     NYEEIIQKEE GQAISFNKSS NDVIVFVHIQ KTAGTTFEKF LVRYQQSLPC KCQAHKKRCN
     CGRNASNETW LFSRYSTGWV CGLHADFTEL VVNSCVQRVL DKQAGHKKRR NYFYTTFLRN
     PTDRFISEFR HVQRGATWIS SKHVCDGKPA SINDLPTCFD PRIGWEGVSL EEFISCPYNL
     AFNRQTRMLS NLSLVGCYEH LRKPSYEQDK IMMESAKQNL RQVFYSDYYT QVKKR
//
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