CHST5_MOUSE
ID CHST5_MOUSE Reviewed; 395 AA.
AC Q9QUP4;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Carbohydrate sulfotransferase 5;
DE EC=2.8.2.-;
DE AltName: Full=Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 4;
DE Short=GST4;
DE AltName: Full=Intestinal N-acetylglucosamine-6-O-sulfotransferase;
DE Short=I-GlcNAc6ST;
DE Short=Intestinal GlcNAc-6-sulfotransferase;
DE Short=mIGn6ST;
DE AltName: Full=N-acetylglucosamine 6-O-sulfotransferase 3;
DE Short=GlcNAc6ST-3;
DE Short=Gn6st-3;
GN Name=Chst5; Synonyms=Gst4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=C57BL/6J; TISSUE=Intestine;
RX PubMed=10491328; DOI=10.1006/bbrc.1999.1324;
RA Lee J.K., Bhakta S., Rosen S.D., Hemmerich S.;
RT "Cloning and characterization of a mammalian N-acetylglucosamine-6-
RT sulfotransferase that is highly restricted to intestinal tissue.";
RL Biochem. Biophys. Res. Commun. 263:543-549(1999).
RN [2]
RP TISSUE SPECIFICITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=11278593; DOI=10.1074/jbc.m009995200;
RA Akama T.O., Nakayama J., Nishida K., Hiraoka N., Suzuki M., McAuliffe J.,
RA Hindsgaul O., Fukuda M., Fukuda M.N.;
RT "Human corneal GlcNAc 6-O-sulfotransferase and mouse intestinal GlcNAc 6-O-
RT sulfotransferase both produce keratan sulfate.";
RL J. Biol. Chem. 276:16271-16278(2001).
RN [3]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=12218059; DOI=10.1074/jbc.m207412200;
RA Akama T.O., Misra A.K., Hindsgaul O., Fukuda M.N.;
RT "Enzymatic synthesis in vitro of the disulfated disaccharide unit of
RT corneal keratan sulfate.";
RL J. Biol. Chem. 277:42505-42513(2002).
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 non-reducing N-acetylglucosamine (GlcNAc) residues of
CC keratan. Mediates sulfation of keratan in cornea. Keratan sulfate plays
CC a central role in maintaining corneal transparency. Acts on the non-
CC reducing terminal GlcNAc of short and long carbohydrate substrates that
CC have poly-N-acetyllactosamine structures. May also have activity toward
CC O-linked sugars of mucin-type acceptors. {ECO:0000269|PubMed:12218059}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}. Note=Golgi membrane, early
CC secretory pathway. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in cornea. {ECO:0000269|PubMed:11278593}.
CC -!- MISCELLANEOUS: In human, there are 2 related proteins, CHST5 and CHST6,
CC the latter mediating sulfation of keratan in cornea. In mouse however,
CC there is no CHST6 protein, CHST5 functioning as a corneal keratan
CC sulfotransferase and mediates such function.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc
CC subfamily. {ECO:0000305}.
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DR EMBL; AF176840; AAD56002.1; -; mRNA.
DR EMBL; AF176841; AAD56003.1; -; Genomic_DNA.
DR CCDS; CCDS22682.1; -.
DR RefSeq; NP_064334.1; NM_019950.2.
DR AlphaFoldDB; Q9QUP4; -.
DR STRING; 10090.ENSMUSP00000034430; -.
DR GlyGen; Q9QUP4; 4 sites.
DR iPTMnet; Q9QUP4; -.
DR PhosphoSitePlus; Q9QUP4; -.
DR MaxQB; Q9QUP4; -.
DR PaxDb; Q9QUP4; -.
DR PRIDE; Q9QUP4; -.
DR ProteomicsDB; 281675; -.
DR DNASU; 56773; -.
DR Ensembl; ENSMUST00000034430; ENSMUSP00000034430; ENSMUSG00000031952.
DR GeneID; 56773; -.
DR KEGG; mmu:56773; -.
DR UCSC; uc009nmz.1; mouse.
DR CTD; 23563; -.
DR MGI; MGI:1931825; Chst5.
DR VEuPathDB; HostDB:ENSMUSG00000031952; -.
DR eggNOG; ENOG502QQMD; Eukaryota.
DR GeneTree; ENSGT00940000162986; -.
DR HOGENOM; CLU_028381_3_1_1; -.
DR InParanoid; Q9QUP4; -.
DR OMA; FKWASST; -.
DR OrthoDB; 1246608at2759; -.
DR PhylomeDB; Q9QUP4; -.
DR TreeFam; TF342871; -.
DR BRENDA; 2.8.2.21; 3474.
DR Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
DR BioGRID-ORCS; 56773; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Chst5; mouse.
DR PRO; PR:Q9QUP4; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9QUP4; protein.
DR Bgee; ENSMUSG00000031952; Expressed in vestibular epithelium and 83 other tissues.
DR Genevisible; Q9QUP4; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0001517; F:N-acetylglucosamine 6-O-sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0018146; P:keratan sulfate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IDA:UniProtKB.
DR GO; GO:0006790; P:sulfur compound metabolic process; IDA:UniProtKB.
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..395
FT /note="Carbohydrate sulfotransferase 5"
FT /id="PRO_0000085196"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..395
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 49..55
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 202..210
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 395 AA; 44537 MW; 3FDF71E43ED383BE CRC64;
MRLPRFSSTV MLSLLMVQTG ILVFLVSRQV PSSPAGLGER VHVLVLSSWR SGSSFVGQLF
SQHPDVFYLM EPAWHVWDTL SQGSAPALHM AVRDLIRSVF LCDMDVFDAY LPWRRNISDL
FQWAVSRALC SPPVCEAFAR GNISSEEVCK PLCATRPFGL AQEACSSYSH VVLKEVRFFN
LQVLYPLLSD PALNLRIVHL VRDPRAVLRS REQTAKALAR DNGIVLGTNG TWVEADPRLR
VVNEVCRSHV RIAEAALHKP PPFLQDRYRL VRYEDLARDP LTVIRELYAF TGLGLTPQLQ
TWIHNITHGS GPGARREAFK TTSRDALSVS QAWRHTLPFA KIRRVQELCG GALQLLGYRS
VHSELEQRDL SLDLLLPRGM DSFKWASSTE KQPES
