ID A0A3P9N2I5_POERE Unreviewed; 434 AA.
AC A0A3P9N2I5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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 Name=HS6ST3 {ECO:0000313|Ensembl:ENSPREP00000003801.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000003801.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000003801.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000003801.1};
RG Ensembl;
RL Submitted (SEP-2023) 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|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 RefSeq; XP_008398211.1; XM_008399989.2.
DR AlphaFoldDB; A0A3P9N2I5; -.
DR STRING; 8081.ENSPREP00000003801; -.
DR Ensembl; ENSPRET00000003857.1; ENSPREP00000003801.1; ENSPREG00000002663.1.
DR GeneID; 103458872; -.
DR KEGG; pret:103458872; -.
DR CTD; 569353; -.
DR GeneTree; ENSGT00950000183071; -.
DR OMA; RKTQYMF; -.
DR OrthoDB; 2896660at2759; -.
DR Proteomes; UP000242638; 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:SF3; HEPARAN-SULFATE 6-O-SULFOTRANSFERASE 3; 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:UP000242638};
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 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364122"
FT REGION 389..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 434 AA; 50751 MW; C36E2E98A7BDE00D CRC64;
MDERSSKLIL VPILAVLFVM IGYQYICPAG SNSCHFKSEE RFRGVSLLSS PYQDADDFYR
DSDLDDDGPP KLPSKFNFTE RDLDRHVEFN IKGDDVIVFL HIQKTGGTTF GRHLVRNIRL
EQPCDCKPGQ KKCTCHRPGK EESWLFSRFS TGWSCGLHAD WTELTNCVPV VMDKKEAQRN
KRNFYYITML RDPVSRYLSE WKHVQRGATW KTALHMCDGR SPTQDELPTC YSGDDWSGVT
LKEFMNCQSN LANNRQVRML ADLSLVGCYN MSSMNESQRN HILLSSAMSN LKNMAFYGLT
EFQRKTQYLF ERTFSLRFIS AFTQINSTRA ANVDLSEAVR RRIEELNFLD VQLYEYAKDL
FLQRFQYTRQ REHQEVRLKR REERRWLREQ RDQGRPWPSK HKGSGKGDGG VFEKETENDL
PTTTEDYTSQ VARW
//
