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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
 
 
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