CHSTF_NOTSL
ID CHSTF_NOTSL Reviewed; 159 AA.
AC Q8WTN9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 29-SEP-2021, entry version 65.
DE RecName: Full=Carbohydrate sulfotransferase 15;
DE EC=2.8.2.33;
DE AltName: Full=N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase;
DE Short=GalNAc4S-6ST;
DE Flags: Fragments;
GN Name=GALNAC4S6ST;
OS Nototodarus sloanii (Wellington flying squid) (Ommastrephes sloanei).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Decapodiformes; Teuthida; Oegopsina; Ommastrephidae;
OC Nototodarus.
OX NCBI_TaxID=215440;
RN [1]
RP PROTEIN SEQUENCE OF 1-31 AND 149-159, AND NUCLEOTIDE SEQUENCE [MRNA] OF
RP 32-148.
RC TISSUE=Cartilage;
RX PubMed=11572857; DOI=10.1074/jbc.m104922200;
RA Ohtake S., Ito Y., Fukuta M., Habuchi O.;
RT "Human N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase cDNA is related
RT to human B cell recombination activating gene-associated gene.";
RL J. Biol. Chem. 276:43894-43900(2001).
RN [2]
RP COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10871629; DOI=10.1074/jbc.m909633199;
RA Ito Y., Habuchi O.;
RT "Purification and characterization of N-acetylgalactosamine 4-sulfate 6-O-
RT sulfotransferase from the squid cartilage.";
RL J. Biol. Chem. 275:34728-34736(2000).
RN [3]
RP FUNCTION.
RX PubMed=12423630; DOI=10.1016/s0003-2697(02)00277-4;
RA Habuchi O., Moroi R., Ohtake S.;
RT "Enzymatic synthesis of chondroitin sulfate E by N-acetylgalactosamine 4-
RT sulfate 6-O-sulfotransferase purified from squid cartilage.";
RL Anal. Biochem. 310:129-136(2002).
CC -!- FUNCTION: Sulfotransferase that transfers sulfate from 3'-
CC phosphoadenosine 5'-phosphosulfate (PAPS) to the C-6 hydroxyl group of
CC the GalNAc 4-sulfate residue of chondroitin sulfate A and forms
CC chondroitin sulfate E containing GlcA-GalNAc(4,6-SO(4)) repeating
CC units. {ECO:0000269|PubMed:12423630}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=n 3'-phosphoadenylyl sulfate + dermatan 4'-sulfate = n
CC adenosine 3',5'-bisphosphate + dermatan 4',6'-bissulfate + n H(+);
CC Xref=Rhea:RHEA:54304, Rhea:RHEA-COMP:9965, Rhea:RHEA-COMP:13850,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:58465, ChEBI:CHEBI:138121; EC=2.8.2.33;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=n 3'-phosphoadenylyl sulfate + chondroitin 4'-sulfate = n
CC adenosine 3',5'-bisphosphate + chondroitin 4',6'-bissulfate + n H(+);
CC Xref=Rhea:RHEA:54300, Rhea:RHEA-COMP:9829, Rhea:RHEA-COMP:13849,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:58422, ChEBI:CHEBI:138112; EC=2.8.2.33;
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:10871629};
CC -!- COFACTOR:
CC Name=glutathione; Xref=ChEBI:CHEBI:57925;
CC Evidence={ECO:0000269|PubMed:10871629};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 uM for PAPS {ECO:0000269|PubMed:10871629};
CC KM=1.1 uM for chondroitin sulfate A {ECO:0000269|PubMed:10871629};
CC KM=0.13 uM for dermatan sulfate {ECO:0000269|PubMed:10871629};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: In contrast to the human protein, it does not transfer
CC sulfate to the unique non-reducing terminal sequence GalNAc(4SO4)-
CC GlcA(2SO4)-GalNAc(6SO4).
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AB062424; BAB72146.1; -; mRNA.
DR KEGG; ag:BAB72146; -.
DR SABIO-RK; Q8WTN9; -.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050659; F:N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Golgi apparatus; Membrane;
KW Transferase.
FT CHAIN <1..>159
FT /note="Carbohydrate sulfotransferase 15"
FT /id="PRO_0000225626"
FT TOPO_DOM <1..159
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_CONS 10..11
FT /evidence="ECO:0000305"
FT NON_CONS 20..21
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 159
SQ SEQUENCE 159 AA; 19155 MW; DE1C0B5D3C0F9BDF CRC64;
SGTTDFYRRI ITSEASASTL SLENFXHRVT ESINMYEKCF KNETMRKCVY DRSLSLLSGV
RLRIGLYWIY LQDWFSVFPK ENFYIIKTED YAKCLKCTFK KVYRFLGLPQ LNRTNEAFME
SIPKANTRRF KDTKMGKMWK ETYELLEKFY QPHNERLVK
