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Database: UniProt
Entry: A0A3S0ZB56_ELYCH
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ID   A0A3S0ZB56_ELYCH        Unreviewed;       407 AA.
AC   A0A3S0ZB56;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   03-MAY-2023, entry version 16.
DE   RecName: Full=Heparan-sulfate 6-O-sulfotransferase {ECO:0000256|RuleBase:RU364122};
DE            EC=2.8.2.- {ECO:0000256|RuleBase:RU364122};
GN   ORFNames=EGW08_018546 {ECO:0000313|EMBL:RUS73684.1};
OS   Elysia chlorotica (Eastern emerald elysia) (Sea slug).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Sacoglossa; Placobranchoidea;
OC   Plakobranchidae; Elysia.
OX   NCBI_TaxID=188477 {ECO:0000313|EMBL:RUS73684.1, ECO:0000313|Proteomes:UP000271974};
RN   [1] {ECO:0000313|EMBL:RUS73684.1, ECO:0000313|Proteomes:UP000271974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC2010 {ECO:0000313|EMBL:RUS73684.1};
RC   TISSUE=Whole organism of an adult {ECO:0000313|EMBL:RUS73684.1};
RA   Cai H., Li Q., Fang X., Li J., Curtis N.E., Altenburger A., Shibata T.,
RA   Feng M., Maeda T., Schwartz J.A., Shigenobu S., Lundholm N., Nishiyama T.,
RA   Yang H., Hasebe M., Li S., Pierce S.K., Wang J.;
RT   "A draft genome assembly of the solar-powered sea slug Elysia chlorotica.";
RL   Submitted (JAN-2019) 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:RUS73684.1}.
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DR   EMBL; RQTK01000910; RUS73684.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S0ZB56; -.
DR   STRING; 188477.A0A3S0ZB56; -.
DR   Proteomes; UP000271974; 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:UP000271974};
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        18..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364122"
FT   REGION          363..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..388
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..407
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   407 AA;  47469 MW;  95D171E0A22F08FC CRC64;
     MNKTIKSLSS RNLNRTRFVV FSFVATIVVF FILFAIYSCA GTVCFQSQLV KHSFTSHDLD
     RVRTLNLEGN DVLVHLHIQK TGGSRFGRHL SFNLDVDPPC KCRDAKHCTC FTRKNLIWLF
     NHESVGSICG LHADWTDLQN CVDPWFQRID SGVRNYRRYH YITMLRDPVE RFFSEWQHVH
     RGATWAGARL HCNGREATLE EVPFCFQGED WAGVSFPEFV GCKSNLAFNR MTRMLSNLSK
     VNCYNRTGLD EGFVFRTMVE SAKENLLDFA FFGILEEQAK SQFLFEHTLG IRFIKSLDQR
     EDTHVAKLNM TKEMVDLVRR TNQQDIELYR FARELFHQRV VDMERRLGYT VEEYFDVYRD
     AQNELGTQDE QHGEEEEEEE EEEDDSGMLH GTGDERKLTH YPGEGGK
//
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