ID A0A0V0UQE7_9BILA Unreviewed; 633 AA.
AC A0A0V0UQE7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Heparan-sulfate 6-O-sulfotransferase {ECO:0000256|RuleBase:RU364122};
DE EC=2.8.2.- {ECO:0000256|RuleBase:RU364122};
GN Name=hs6st3 {ECO:0000313|EMBL:KRX53572.1};
GN ORFNames=T09_12090 {ECO:0000313|EMBL:KRX53572.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX53572.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX53572.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX53572.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX53572.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDN01000197; KRX53572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0UQE7; -.
DR STRING; 181606.A0A0V0UQE7; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008146; F:sulfotransferase activity; IEA:InterPro.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR010635; Heparan_SO4-6-sulfoTrfase.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000535; MSP_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008962; PapD-like_sf.
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; PF00635; Motile_Sperm; 1.
DR Pfam; PF03567; Sulfotransfer_2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF49354; PapD-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|RuleBase:RU364122};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Signal-anchor {ECO:0000256|RuleBase:RU364122};
KW Transferase {ECO:0000256|RuleBase:RU364122, ECO:0000313|EMBL:KRX53572.1};
KW Transmembrane {ECO:0000256|RuleBase:RU364122};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364122}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364122"
FT DOMAIN 416..504
FT /note="MSP"
FT /evidence="ECO:0000259|Pfam:PF00635"
SQ SEQUENCE 633 AA; 72893 MW; 77849BB400CE67F0 CRC64;
MLDGGCGRYQ TIFIFLCLFG CSFLFYASWY SEVENLSPAD VLPLENFPAE FTAEDESFLD
NLLVETVLDL PKFHEKPSEA QNAMEVGNVS FDKIQSDPTV QRFDLNRSDV IVFLHIQKTG
GTTFERYMVR QIDLISPCVC QARRKRCRCM RPNSYKSPWL FSRFSTGWNC GLHSDWTELV
ASGCVDEYFD NREHRHVARR YFITTFLREP VSRFISEFHH VRRGATWLTS RHLCNGRSPT
AEELPPCFER SQHGWKDVTL DAFLACSSNL AFNRQTRMLA DLRLVHCYNR SAMDMDRRDA
IMLLSAKRNL LKMAFFGLQD EMRRSQYLFE RTFGLHFTKP MVDLKSRTDS IQLTDEQRRQ
VEAVNRLDLD LYRFAKRVFN ERFNHAKQQD ILLLLFIIWI INNMMTTSTE TPLTVVFPDS
LEMSASNRES LSQMLTVCNP YDVPLHYKVL CTAPNMYVVD GASGRLKPRI CSQVHIHRIG
PVTDKNGAPL DPSTDKFRVE VKKMDGVSEV MKTDIIVYIN QNGKRQVGFD QQQQAVKKLT
ACEQRNRCSA TVDSQTTGGN RRSSIRDDDD SALCNFLLTT ISIICLVILL TPVSVDCQAE
GPSWYPEWLR VSLPQKLISA YVLGILTKYL IKP
//
