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   24-JAN-2024, entry version 140.
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   GlyCosmos; Q9QUP4; 4 sites, No reported glycans.
DR   GlyGen; Q9QUP4; 4 sites.
DR   iPTMnet; Q9QUP4; -.
DR   PhosphoSitePlus; Q9QUP4; -.
DR   MaxQB; Q9QUP4; -.
DR   PaxDb; 10090-ENSMUSP00000034430; -.
DR   ProteomicsDB; 281675; -.
DR   DNASU; 56773; -.
DR   Ensembl; ENSMUST00000034430.6; ENSMUSP00000034430.5; ENSMUSG00000031952.6.
DR   GeneID; 56773; -.
DR   KEGG; mmu:56773; -.
DR   UCSC; uc009nmz.1; mouse.
DR   AGR; MGI:1931825; -.
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; TQKPPPF; -.
DR   OrthoDB; 3031241at2759; -.
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 79 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 84 other cell types or tissues.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR016469; Carbohydrate_sulfotransferase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10704; CARBOHYDRATE SULFOTRANSFERASE; 1.
DR   PANTHER; PTHR10704:SF4; CARBOHYDRATE SULFOTRANSFERASE 6; 1.
DR   Pfam; PF13469; Sulfotransfer_3; 1.
DR   PIRSF; PIRSF005883; Carbohydrate_sulfotransferase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   Genevisible; Q9QUP4; MM.
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
//