CHSTC_XENLA
ID CHSTC_XENLA Reviewed; 420 AA.
AC Q5XHM7; Q5HZM5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Carbohydrate sulfotransferase 12;
DE EC=2.8.2.5;
DE AltName: Full=Chondroitin 4-O-sulfotransferase 2;
DE AltName: Full=Chondroitin 4-sulfotransferase 2;
DE Short=C4ST-2;
DE Short=C4ST2;
GN Name=chst12;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of sulfate to position 4 of the N-
CC acetylgalactosamine (GalNAc) residue of chondroitin and desulfated
CC dermatan sulfate. Chondroitin sulfate constitutes the predominant
CC proteoglycan present in cartilage and is distributed on the surfaces of
CC many cells and extracellular matrices (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=n 3'-phosphoadenylyl sulfate + chondroitin beta-D-glucuronate
CC = n adenosine 3',5'-bisphosphate + chondroitin 4'-sulfate + n H(+);
CC Xref=Rhea:RHEA:16101, Rhea:RHEA-COMP:9827, Rhea:RHEA-COMP:9829,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57652, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:58422; EC=2.8.2.5;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 2 family. {ECO:0000305}.
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DR EMBL; BC088957; AAH88957.1; -; mRNA.
DR RefSeq; NP_001088975.1; NM_001095506.1.
DR AlphaFoldDB; Q5XHM7; -.
DR DNASU; 496355; -.
DR GeneID; 496355; -.
DR KEGG; xla:496355; -.
DR CTD; 496355; -.
DR Xenbase; XB-GENE-1014622; chst12.L.
DR OMA; REWFANI; -.
DR OrthoDB; 1330889at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 496355; Expressed in egg cell and 19 other tissues.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047756; F:chondroitin 4-sulfotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR InterPro; IPR018011; Carb_sulfotrans_8-10.
DR InterPro; IPR005331; Sulfotransferase.
DR PANTHER; PTHR12137; PTHR12137; 1.
DR Pfam; PF03567; Sulfotransfer_2; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..420
FT /note="Carbohydrate sulfotransferase 12"
FT /id="PRO_0000189670"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..420
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 176..182
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 251..259
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 420 AA; 49238 MW; 21E08CC6471CF687 CRC64;
MAKSRLFCLL VALGSVFMIL FIIVYWDNVG TANLNLHTSF SKSLPFQSSE ELSTAVTATR
NRFVSDVDVF LNSFLNLSTR RSELQSTKAE KMPLRGSSSL EENARGYDWS TKEKLEDAIL
DQEMIQQERK LNLLQFCGNS SFGFPTKERS FDDIPNRELD HLIVDDRHGI IYCYVPKVAC
TNWKRVMIVL SESLLDKKGV PYQDPLLIPR EDVHNTSSHL TFNKFWRRYG KFSRHMMKIK
LKKYTKFLFV RDPFVRLISA FRSKFELENE DFYRSFAVPI LTRFSNTTRV PDTVGEAFSS
GTMPSFSQFI QYLLDPQTEE QKPFNEHWRQ VYRLCHPCQI EYDFIGKLET LGEDTALLLR
QLNLDTLFQF PPSYRNRTAS SWEEDWYSKL PIAWRKKLYK LFEADFVLFG YPKPDDLLSV