ID H3A5G8_LATCH Unreviewed; 876 AA.
AC H3A5G8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=[heparan sulfate]-glucosamine N-sulfotransferase {ECO:0000256|ARBA:ARBA00012979};
DE EC=2.8.2.8 {ECO:0000256|ARBA:ARBA00012979};
GN Name=LOC102347296 {ECO:0000313|Ensembl:ENSLACP00000004889.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000004889.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000004889.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005093}.
CC -!- PATHWAY: Glycan metabolism; heparin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004841}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. NDST subfamily.
CC {ECO:0000256|ARBA:ARBA00010420}.
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DR EMBL; AFYH01202237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01202238; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01202239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01202240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01202241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01202242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01202243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01202244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01202245; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01202246; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3A5G8; -.
DR STRING; 7897.ENSLACP00000004889; -.
DR Ensembl; ENSLACT00000004932.1; ENSLACP00000004889.1; ENSLACG00000004348.1.
DR eggNOG; KOG3703; Eukaryota.
DR GeneTree; ENSGT00940000157168; -.
DR HOGENOM; CLU_011357_2_0_1; -.
DR InParanoid; H3A5G8; -.
DR OMA; FCHTYSH; -.
DR TreeFam; TF313193; -.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0015016; F:[heparan sulfate]-glucosamine N-sulfotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0019213; F:deacetylase activity; IEA:UniProt.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0030210; P:heparin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR021930; Heparan_SO4_deacetylase.
DR InterPro; IPR037359; NST/OST.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR PANTHER; PTHR10605:SF45; BIFUNCTIONAL HEPARAN SULFATE N-DEACETYLASE_N-SULFOTRANSFERASE 4; 1.
DR PANTHER; PTHR10605; HEPARAN SULFATE SULFOTRANSFERASE; 1.
DR Pfam; PF12062; HSNSD; 1.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR637359-3};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 18..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 79..509
FT /note="Heparan sulphate-N-deacetylase"
FT /evidence="ECO:0000259|Pfam:PF12062"
FT DOMAIN 599..849
FT /note="Sulfotransferase"
FT /evidence="ECO:0000259|Pfam:PF00685"
FT ACT_SITE 608
FT /note="For sulfotransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT BINDING 706
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 811
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 827..831
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT DISULFID 812..822
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
SQ SEQUENCE 876 AA; 101050 MW; 7BBEC2EE25AD7204 CRC64;
QYNMVFVMKL NRHFRRTVIL LATFCTVSIV ISAYYLYTGH KRDTDLSEMP TGMECGDLKL
LPYRILDVKN AKPIHWSRTE AVVLVFVESQ YSQLGQDIVA ILESSRIQFH TEIAPGKGDI
PVLTDKGRGR YALIIYENIL KYVNMDSWNR ALLDNYCIEH SVGIIGFHKA TENSLLSPQL
KGFPLKVYTK LGLKDYCVNP HSPLLHITKA SEGDKGSLSG EDWAVFQFNH STYQPVLLAK
LSSSENIPQA LSKDTLHATV VQDLGLHDGI QRVLFGNNLN FWLHKLIFVD AISFLSGKKF
SLSLERYILV DIDDIFVGKE GTRMNANDVK ALLDTQNLLR TQIANFTFNL GFSGKFYHTG
AEEEDDGDDL LLKYIDEFWW FPHMWNHMQP HLFHNESTLV DQMILNKKFA LEHGIPTDMG
YAVSPHHSGV YPVHVQLYEA WKKVWGIKVT STEEYPHLKP ARYRRGFIHK GIMVLPRQTC
GLFTHTIFYK EYPGGPKELD KSIRGGELFL TVLLNPISIF MTHLSNYGND RLGLYTFVNL
ARFVERWTNL KLRTLPPVQL AHKYFQLFPQ HKEPLWQSPC DDKRHKDIWS KEKTCDRLPK
FLVIGPQKTG TTALYLFLLM HPSIICNLPS PKTFEEVQFF NGNNYHKGID WYMDFFPIPS
NVTSDFLFEK SANYFPSEEA PKRVVALLPK AKIITILIDP SDRAYSWYQH QRAHEDPTAL
KFSFYEVITA GHQAPVELRT LQKRCLVPGW YSTHIERWLA YFQAAQLLII DGQQLRNDPA
AVMDEVQKFL GVSPHYNYSE ALMFDSRKGF WCQLLEGGKT KCLGKSKGRK YPPMDSESRA
FLSNYYREHN VELSKLLHRL GQALPSWLRQ ELQNVR
//
