GenomeNet

Database: UniProt
Entry: G3SW88_LOXAF
LinkDB: G3SW88_LOXAF
Original site: G3SW88_LOXAF 
ID   G3SW88_LOXAF            Unreviewed;       367 AA.
AC   G3SW88;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Sulfotransferase {ECO:0000256|RuleBase:RU361155};
DE            EC=2.8.2.- {ECO:0000256|RuleBase:RU361155};
GN   Name=HS3ST2 {ECO:0000313|Ensembl:ENSLAFP00000004567.2};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000004567.2, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000004567.2, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000004567.2,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000004567.2}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000004567.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family.
CC       {ECO:0000256|RuleBase:RU361155}.
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DR   RefSeq; XP_003418863.1; XM_003418815.2.
DR   AlphaFoldDB; G3SW88; -.
DR   STRING; 9785.ENSLAFP00000004567; -.
DR   Ensembl; ENSLAFT00000005448.2; ENSLAFP00000004567.2; ENSLAFG00000005452.2.
DR   GeneID; 100670647; -.
DR   KEGG; lav:100670647; -.
DR   CTD; 9956; -.
DR   eggNOG; KOG3704; Eukaryota.
DR   GeneTree; ENSGT00940000160498; -.
DR   HOGENOM; CLU_017703_0_0_1; -.
DR   InParanoid; G3SW88; -.
DR   OMA; NIIFYRG; -.
DR   OrthoDB; 10019at2759; -.
DR   TreeFam; TF350755; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008467; F:[heparan sulfate]-glucosamine 3-sulfotransferase 1 activity; IEA:Ensembl.
DR   GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IEA:Ensembl.
DR   GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IEA:Ensembl.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR037359; NST/OST.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000863; Sulfotransferase_dom.
DR   PANTHER; PTHR10605:SF10; HEPARAN SULFATE GLUCOSAMINE 3-O-SULFOTRANSFERASE 2; 1.
DR   PANTHER; PTHR10605; HEPARAN SULFATE SULFOTRANSFERASE; 1.
DR   Pfam; PF00685; Sulfotransfer_1; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR637359-3};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW   Transferase {ECO:0000256|RuleBase:RU361155};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          115..350
FT                   /note="Sulfotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00685"
FT   REGION          58..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..90
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        124
FT                   /note="For sulfotransferase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT   BINDING         124..128
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         205
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         213
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         330..334
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   DISULFID        313..325
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
SQ   SEQUENCE   367 AA;  41431 MW;  F01B149D51B60BD9 CRC64;
     MAYRVLGRAG PPQPRRARRL LFAFTLSLSC TYLCYSLLCC CDDLRQSRLI GAPSCLRGPS
     TGGQKLLQKS RPCDPPGPTP SEPGAPSAPA AAVPAPRLSG SNHSGSPKPG TKRLPQALIV
     GVKKGGTRAV LEFIRVHPDV RALGTEPHFF DRNYGRGLDW YRSLMPRTLE SQITLEKTPS
     YFVTQEAPRR IFNMSRDTKL IVVVRNPVTR AISDYTQTLS KKPDIPTFEG LSFRNRTLGL
     VDVSWNAIRI GMYALHLESW LQYFPLAQIH FVSGERLITD PAGEMGRVQD FLGIKRFITD
     KHFYFNKTKG FPCLKKPESS LLPRCLGKSK GRTHVQIDPE VIDQLREFYR PYNIKFYETV
     GQDFRWE
//
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