CHST1_DANRE
ID CHST1_DANRE Reviewed; 420 AA.
AC Q6DBY9; Q4QRG8;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Carbohydrate sulfotransferase 1;
DE EC=2.8.2.21;
DE AltName: Full=Keratan sulfate Gal-6 sulfotransferase;
DE Short=KS6ST;
DE Short=KSGal6ST;
DE Short=KSST;
GN Name=chst1; ORFNames=zgc:100904;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the transfer of sulfate to
CC position 6 of galactose (Gal) residues of keratan. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + keratan = adenosine 3',5'-
CC bisphosphate + keratan 6'-sulfate.; EC=2.8.2.21;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc
CC subfamily. {ECO:0000305}.
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DR EMBL; BC078309; AAH78309.1; -; mRNA.
DR EMBL; BC096983; AAH96983.1; -; mRNA.
DR RefSeq; NP_001003518.1; NM_001003518.2.
DR AlphaFoldDB; Q6DBY9; -.
DR STRING; 7955.ENSDARP00000108405; -.
DR PaxDb; Q6DBY9; -.
DR GeneID; 445124; -.
DR KEGG; dre:445124; -.
DR CTD; 8534; -.
DR ZFIN; ZDB-GENE-040801-21; chst1.
DR eggNOG; ENOG502S17I; Eukaryota.
DR InParanoid; Q6DBY9; -.
DR OrthoDB; 1246608at2759; -.
DR PhylomeDB; Q6DBY9; -.
DR Reactome; R-DRE-2022854; Keratan sulfate biosynthesis.
DR PRO; PR:Q6DBY9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0045130; F:keratan sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0001517; F:N-acetylglucosamine 6-O-sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042339; P:keratan sulfate metabolic process; IBA:GO_Central.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IBA:GO_Central.
DR GO; GO:0006790; P:sulfur compound metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR016469; Carbohydrate_sulfotransferase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR PIRSF; PIRSF005883; Carbohydrate_sulfotransferase; 1.
DR SUPFAM; SSF52540; SSF52540; 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 1"
FT /id="PRO_0000085185"
FT TOPO_DOM 1
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..420
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 77..83
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 242..250
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 166
FT /note="K -> N (in Ref. 1; AAH78309)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="S -> T (in Ref. 1; AAH78309)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="G -> S (in Ref. 1; AAH78309)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="L -> S (in Ref. 1; AAH78309)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 48212 MW; 2BDED25FFCADCB00 CRC64;
MQCSWKAVIL LALVSIAIQY TAIRTFTAKP FHICPVPNPL NCGLGQDVES FDRMCDEYPY
FNYNSSRKTH ILILATTRSG SSFVGQLFNQ HSDVFYLFEP LYHVQTTLIP HLSPSRYAVE
RRVMLGASRD LLRSLYNCDL YFLESYIKPQ PANHTTDKLF RRGASKALCS MPVCDAFSPN
DGNIEEGDCV RKCASLNLTL ATESCRERRH VAIKTVRIPE VNDLKALIED PRLNLKVIQL
VRDPRGILSS RIETFRDTYR LWRIWRATGR KPYNLDLTQL TTVCDDFLNS VSTGLSRPPW
LRGRYMLVRY EDLARNPLQK TKEVYEFLGL SLEKGVVDWI HNNTRGNNDV SAKHKYGTLR
DSAANAESWR LKLSHDIVDY TQTVCQHILD ELGYKAVNSP EELKNMSISL IEDKTFIPFL
