ID A0A2U9CJA7_SCOMX Unreviewed; 398 AA.
AC A0A2U9CJA7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=Heparan-sulfate 6-O-sulfotransferase {ECO:0000256|RuleBase:RU364122};
DE EC=2.8.2.- {ECO:0000256|RuleBase:RU364122};
GN ORFNames=SMAX5B_021994 {ECO:0000313|EMBL:AWP16293.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP16293.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP16293.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) 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|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 EMBL; CP026259; AWP16293.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9CJA7; -.
DR STRING; 52904.ENSSMAP00000028664; -.
DR Proteomes; UP000246464; Chromosome 17.
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:SF1; HEPARAN-SULFATE 6-O-SULFOTRANSFERASE 1; 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:UP000246464};
KW Signal-anchor {ECO:0000256|RuleBase:RU364122};
KW Transferase {ECO:0000256|RuleBase:RU364122, ECO:0000313|EMBL:AWP16293.1};
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"
SQ SEQUENCE 398 AA; 45604 MW; BEA2BA56F63256C1 CRC64;
MVERSSKFLL IVVGSVCFML ILYQYVAPGV INFGSPHGYF AEEDEGDIFP TPDPHYVKKY
YFPVRDLERT IDFQIKGEDV IVFLHIQKTG GTTFGRHLVQ NVRLEVPCDC RPGQKKCTCY
RPNRKETWLF SRFSTGWSCG LHADWTELTN CVPGVLDKKE SQQKNLRKFY YITLLRDPVS
RYLSEWRHVQ RGATWKTSLH MCDGRTPTPE ELPSCYEGSD WSGCTLQQFM DCPYNLANNR
QVRMLADLSL VGCYNMSTVP EKKRAQLLLE SAKKNLRDMA FFGLTEYQRK TQFLFERTFR
LRFIRPFMQY NSTRAAGVDL DNTTVQRIEE LNELDMELYD YARDLGNPAL SDCAGSGYNP
LIGGQTGCGS SSPVPCFFPA NKGALALLSL IFSMAFCR
//
