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Database: UniProt
Entry: A0A0M9A1I4_9HYME
LinkDB: A0A0M9A1I4_9HYME
Original site: A0A0M9A1I4_9HYME 
ID   A0A0M9A1I4_9HYME        Unreviewed;       481 AA.
AC   A0A0M9A1I4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   13-SEP-2023, 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   ORFNames=WN51_12174 {ECO:0000313|EMBL:KOX75430.1};
OS   Melipona quadrifasciata.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Melipona.
OX   NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX75430.1, ECO:0000313|Proteomes:UP000053105};
RN   [1] {ECO:0000313|EMBL:KOX75430.1, ECO:0000313|Proteomes:UP000053105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0111107301 {ECO:0000313|EMBL:KOX75430.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KOX75430.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Melipona quadrifasciata.";
RL   Submitted (JUL-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}.
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DR   EMBL; KQ435762; KOX75430.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M9A1I4; -.
DR   STRING; 166423.A0A0M9A1I4; -.
DR   OrthoDB; 2896660at2759; -.
DR   Proteomes; UP000053105; 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.
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:UP000053105};
KW   Signal-anchor {ECO:0000256|RuleBase:RU364122};
KW   Transferase {ECO:0000256|RuleBase:RU364122, ECO:0000313|EMBL:KOX75430.1};
KW   Transmembrane {ECO:0000256|RuleBase:RU364122};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU364122}.
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364122"
SQ   SEQUENCE   481 AA;  55044 MW;  75046D357A9C8463 CRC64;
     MGRRSSEEGV SELSVLVEDD LCERSATMES RARRTRLRSV VGICLFLALT GIIYLGYFCP
     DHVCALTSRE IKESVRLSEG LSAGPGSGLS SVSVEFDKNG LLSVHPAFRL HSIQGSLGYD
     DVFTNDTFQF DINGHDVIVF LHIQKTGGTL FGKHLVRDLD LQRPCSCQRR RKRCFCFRPN
     RNENWLFSRY STGWKCGLHA DWTELTSCVD TELNKIEGDG IKRRYFYITI IRDPVARYLS
     EFRHVQRGAT WRGARHWCGG IQANIPQCYP GSSWQGVSLE QFMACPYNLA SNRQTRMLAD
     LSIVGCYNST LSSLERDRLM LASAKHNLQF MPFFMLTEYQ KVGQYSFEET FGMRFAVAFE
     QHNATLSAAT MATLSAEQLD AVRRLNRLDL ELYDFAKNLA FQRFKRLRDR DPYFVQRFQH
     LGELPSRQSA TEFNWDSVIE DTTDLTTKKI ITKQYANALF SRIFIDCVND PQTSLVFSEN
     A
//
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