CHST5_HUMAN
ID CHST5_HUMAN Reviewed; 411 AA.
AC Q9GZS9; B2RV23; Q7LCN3; Q9UBY3;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Carbohydrate sulfotransferase 5;
DE EC=2.8.2.-;
DE AltName: Full=Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 4-alpha;
DE Short=GST4-alpha;
DE AltName: Full=Intestinal N-acetylglucosamine-6-O-sulfotransferase;
DE Short=I-GlcNAc6ST;
DE Short=Intestinal GlcNAc-6-sulfotransferase;
DE Short=hIGn6ST;
DE AltName: Full=N-acetylglucosamine 6-O-sulfotransferase 3;
DE Short=GlcNAc6ST-3;
DE Short=Gn6st-3;
GN Name=CHST5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND
RP TISSUE SPECIFICITY.
RC 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RX PubMed=11017086; DOI=10.1038/79987;
RA Akama T.O., Nishida K., Nakayama J., Watanabe H., Ozaki K., Nakamura T.,
RA Dota A., Kawasaki S., Inoue Y., Maeda N., Yamamoto S., Fujiwara T.,
RA Thonar E.J.-M.A., Shimomura Y., Kinoshita S., Tanigami A., Fukuda M.N.;
RT "Macular corneal dystrophy type I and type II are caused by distinct
RT mutations in a new sulphotransferase gene.";
RL Nat. Genet. 26:237-241(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11352640; DOI=10.1006/bbrc.2001.4668;
RA Bartes A., Bhakta S., Hemmerich S.;
RT "Sulfation of endothelial mucin by corneal keratan N-acetylglucosamine 6-O-
RT sulfotransferase (GST-4beta).";
RL Biochem. Biophys. Res. Commun. 282:928-933(2001).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=12107080; DOI=10.1093/glycob/12.6.379;
RA Seko A., Nagata K., Yonezawa S., Yamashita K.;
RT "Ectopic expression of a GlcNAc 6-O-sulfotransferase, GlcNAc6ST-2, in
RT colonic mucinous adenocarcinoma.";
RL Glycobiology 12:379-388(2002).
RN [7]
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).
RN [8]
RP SUBSTRATE SPECIFICITY, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12626414; DOI=10.1093/glycob/cwg018;
RA Lee J.K., Bistrup A., van Zante A., Rosen S.D.;
RT "Activities and expression pattern of the carbohydrate sulfotransferase
RT GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.";
RL Glycobiology 13:245-254(2003).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=12855678; DOI=10.1074/jbc.m304928200;
RA de Graffenried C.L., Bertozzi C.R.;
RT "Golgi localization of carbohydrate sulfotransferases is a determinant of
RT L-selectin ligand biosynthesis.";
RL J. Biol. Chem. 278:40282-40295(2003).
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 and O-
CC linked sugars of mucin-type acceptors. Acts on the non-reducing
CC terminal GlcNAc of short carbohydrate substrates. However, it does not
CC transfer sulfate to longer carbohydrate substrates that have poly-N-
CC acetyllactosamine structures. Has no activity toward keratan. Not
CC involved in generating HEV-expressed ligands for SELL. Its substrate
CC specificity may be influenced by its subcellular location.
CC {ECO:0000269|PubMed:10491328, ECO:0000269|PubMed:11352640,
CC ECO:0000269|PubMed:12218059, ECO:0000269|PubMed:12626414}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:12855678}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:12855678}. Note=Golgi membrane, early secretory
CC pathway.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9GZS9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9GZS9-2; Sequence=VSP_037526;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in small and large
CC intestines and colon. Weakly expressed in lymphocytes. Not expressed in
CC other tissues. Down-regulated in colonic adenocarcinomas.
CC {ECO:0000269|PubMed:10491328, ECO:0000269|PubMed:11017086,
CC ECO:0000269|PubMed:11352640, ECO:0000269|PubMed:12107080,
CC ECO:0000269|PubMed:12626414}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD56000.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAD56001.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF176838; AAD56000.1; ALT_INIT; mRNA.
DR EMBL; AF176839; AAD56001.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF246718; AAG28023.1; -; mRNA.
DR EMBL; AF219991; AAG26326.1; -; Genomic_DNA.
DR EMBL; CH471114; EAW95635.1; -; Genomic_DNA.
DR EMBL; BC147002; AAI47003.1; -; mRNA.
DR EMBL; BC147007; AAI47008.1; -; mRNA.
DR CCDS; CCDS10919.1; -. [Q9GZS9-1]
DR RefSeq; NP_078809.2; NM_024533.4. [Q9GZS9-1]
DR AlphaFoldDB; Q9GZS9; -.
DR BioGRID; 117106; 45.
DR STRING; 9606.ENSP00000338783; -.
DR GlyGen; Q9GZS9; 3 sites.
DR iPTMnet; Q9GZS9; -.
DR PhosphoSitePlus; Q9GZS9; -.
DR BioMuta; CHST5; -.
DR DMDM; 239938912; -.
DR jPOST; Q9GZS9; -.
DR MassIVE; Q9GZS9; -.
DR PaxDb; Q9GZS9; -.
DR PeptideAtlas; Q9GZS9; -.
DR PRIDE; Q9GZS9; -.
DR ProteomicsDB; 80127; -. [Q9GZS9-1]
DR ProteomicsDB; 80128; -. [Q9GZS9-2]
DR Antibodypedia; 30316; 97 antibodies from 19 providers.
DR DNASU; 23563; -.
DR Ensembl; ENST00000336257.8; ENSP00000338783.3; ENSG00000135702.15. [Q9GZS9-1]
DR GeneID; 23563; -.
DR KEGG; hsa:23563; -.
DR MANE-Select; ENST00000336257.8; ENSP00000338783.3; NM_024533.5; NP_078809.2.
DR UCSC; uc002fei.4; human. [Q9GZS9-1]
DR CTD; 23563; -.
DR DisGeNET; 23563; -.
DR GeneCards; CHST5; -.
DR HGNC; HGNC:1973; CHST5.
DR HPA; ENSG00000135702; Tissue enriched (intestine).
DR MIM; 604817; gene.
DR neXtProt; NX_Q9GZS9; -.
DR OpenTargets; ENSG00000135702; -.
DR PharmGKB; PA26505; -.
DR VEuPathDB; HostDB:ENSG00000135702; -.
DR eggNOG; ENOG502QQMD; Eukaryota.
DR GeneTree; ENSGT00940000162788; -.
DR HOGENOM; CLU_028381_3_1_1; -.
DR InParanoid; Q9GZS9; -.
DR OMA; YLMVRFE; -.
DR OrthoDB; 1246608at2759; -.
DR PhylomeDB; Q9GZS9; -.
DR TreeFam; TF342871; -.
DR PathwayCommons; Q9GZS9; -.
DR Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
DR SABIO-RK; Q9GZS9; -.
DR BioGRID-ORCS; 23563; 6 hits in 1064 CRISPR screens.
DR GeneWiki; CHST5; -.
DR GenomeRNAi; 23563; -.
DR Pharos; Q9GZS9; Tbio.
DR PRO; PR:Q9GZS9; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9GZS9; protein.
DR Bgee; ENSG00000135702; Expressed in duodenum and 86 other tissues.
DR ExpressionAtlas; Q9GZS9; baseline and differential.
DR Genevisible; Q9GZS9; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0031228; C:intrinsic component of Golgi membrane; NAS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0001517; F:N-acetylglucosamine 6-O-sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; TAS:ProtInc.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0018146; P:keratan sulfate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IDA:UniProtKB.
DR GO; GO:0006477; P:protein sulfation; TAS:ProtInc.
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 Alternative splicing; Carbohydrate metabolism; Glycoprotein;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..411
FT /note="Carbohydrate sulfotransferase 5"
FT /id="PRO_0000085195"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..48
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..411
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 71..77
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 224..232
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..16
FT /note="MGMRARVPKVAHSTRR -> MSRHLPWICDQRCSSPSSPGRW (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:10491328"
FT /id="VSP_037526"
FT VARIANT 311
FT /note="A -> T (in dbSNP:rs7206332)"
FT /id="VAR_057993"
FT VARIANT 318
FT /note="T -> M (in dbSNP:rs3826107)"
FT /id="VAR_021416"
SQ SEQUENCE 411 AA; 46161 MW; 97642D54BE926E06 CRC64;
MGMRARVPKV AHSTRRPPAA RMWLPRFSSK TVTVLLLAQT TCLLLFIISR PGPSSPAGGE
DRVHVLVLSS WRSGSSFLGQ LFSQHPDVFY LMEPAWHVWT TLSQGSAATL HMAVRDLMRS
IFLCDMDVFD AYMPQSRNLS AFFNWATSRA LCSPPACSAF PRGTISKQDV CKTLCTRQPF
SLAREACRSY SHVVLKEVRF FNLQVLYPLL SDPALNLRIV HLVRDPRAVL RSREAAGPIL
ARDNGIVLGT NGKWVEADPH LRLIREVCRS HVRIAEAATL KPPPFLRGRY RLVRFEDLAR
EPLAEIRALY AFTGLTLTPQ LEAWIHNITH GSGIGKPIEA FHTSSRNARN VSQAWRHALP
FTKILRVQEV CAGALQLLGY RPVYSADQQR DLTLDLVLPR GPDHFSWASP D
