CHST1_MOUSE
ID CHST1_MOUSE Reviewed; 411 AA.
AC Q9EQC0; Q9D0K5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Carbohydrate sulfotransferase 1;
DE AltName: Full=Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 1;
DE Short=GST-1;
DE AltName: Full=Keratan sulfate Gal-6 sulfotransferase;
DE Short=KS6ST;
DE Short=KSGal6ST;
DE Short=KSST;
DE EC=2.8.2.21 {ECO:0000269|PubMed:24152993};
GN Name=Chst1; Synonyms=Gst1;
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 [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=11181564; DOI=10.1093/glycob/11.1.75;
RA Hemmerich S., Lee J.K., Bhakta S., Bistrup A., Ruddle N.R., Rosen S.D.;
RT "Chromosomal localization and genomic organization for the galactose/ N-
RT acetylgalactosamine/N-acetylglucosamine 6-O-sulfotransferase gene family.";
RL Glycobiology 11:75-87(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 292-411.
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=23254996; DOI=10.1093/glycob/cws166;
RA Patnode M.L., Yu S.Y., Cheng C.W., Ho M.Y., Tegesjoe L., Sakuma K.,
RA Uchimura K., Khoo K.H., Kannagi R., Rosen S.D.;
RT "KSGal6ST generates galactose-6-O-sulfate in high endothelial venules but
RT does not contribute to L-selectin-dependent lymphocyte homing.";
RL Glycobiology 23:381-394(2013).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=24152993; DOI=10.1369/0022155413511619;
RA Hoshino H., Foyez T., Ohtake-Niimi S., Takeda-Uchimura Y., Michikawa M.,
RA Kadomatsu K., Uchimura K.;
RT "KSGal6ST is essential for the 6-sulfation of galactose within keratan
RT sulfate in early postnatal brain.";
RL J. Histochem. Cytochem. 62:145-156(2014).
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 internal galactose (Gal) residues of keratan. Cooperates
CC with B4GALT4 and B3GNT7 glycosyltransferases and CHST6 sulfotransferase
CC to construct and elongate disulfated disaccharide unit [->3(6-
CC sulfoGalbeta)1->4(6-sulfoGlcNAcbeta)1->] within keratan sulfate
CC polymer. Has a preference for sulfating keratan sulfate, but it also
CC transfers sulfate to the unsulfated polymer (By similarity). Involved
CC in biosynthesis of phosphacan, a major keratan sulfate proteoglycan in
CC the developing brain (PubMed:24152993). Involved in biosynthesis of 6-
CC sulfoGalbeta-containing O-linked glycans in high endothelial venules of
CC lymph nodes. May act in a synergistic manner with CHST4 to generate
CC sialyl 6',6-disulfo Lewis X motif, a recognition determinant for immune
CC cell receptors implicated in leukocyte trafficking (PubMed:23254996)
CC (By similarity). Catalyzes sulfation of N-acetyllactosamine (LacNAc)
CC oligosaccharides with highest efficiency for sialylated LacNAc
CC structures (By similarity). {ECO:0000250|UniProtKB:O43916,
CC ECO:0000269|PubMed:23254996, ECO:0000269|PubMed:24152993}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + keratan = adenosine 3',5'-
CC bisphosphate + keratan 6'-sulfate.; EC=2.8.2.21;
CC Evidence={ECO:0000269|PubMed:24152993};
CC -!- PATHWAY: Glycan metabolism. {ECO:0000269|PubMed:24152993}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Broadly expressed with highest levels in central
CC nervous system. Expressed in cortex (at protein level)
CC (PubMed:24152993, PubMed:23254996). Expressed in high endothelial
CC venules in peripheral lymph nodes, mesenteric lymph nodes and Peyer's
CC patches (PubMed:23254996). {ECO:0000269|PubMed:23254996,
CC ECO:0000269|PubMed:24152993}.
CC -!- DEVELOPMENTAL STAGE: Expressed in cortex and cerebellum throughout the
CC postnatal period (at protein level). {ECO:0000269|PubMed:24152993}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are born at the expected Mendelian
CC rate and have normal developmental and reproductive potential.
CC {ECO:0000269|PubMed:23254996}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF280087; AAG48245.1; -; mRNA.
DR EMBL; BC030667; AAH30667.1; -; mRNA.
DR EMBL; AK011344; BAB27556.2; -; mRNA.
DR CCDS; CCDS16450.1; -.
DR RefSeq; NP_076339.1; NM_023850.2.
DR RefSeq; XP_006500451.1; XM_006500388.1.
DR RefSeq; XP_006500452.1; XM_006500389.1.
DR AlphaFoldDB; Q9EQC0; -.
DR STRING; 10090.ENSMUSP00000064246; -.
DR GlyGen; Q9EQC0; 4 sites.
DR PhosphoSitePlus; Q9EQC0; -.
DR PaxDb; Q9EQC0; -.
DR PRIDE; Q9EQC0; -.
DR ProteomicsDB; 281673; -.
DR Antibodypedia; 13251; 208 antibodies from 29 providers.
DR DNASU; 76969; -.
DR Ensembl; ENSMUST00000065797; ENSMUSP00000064246; ENSMUSG00000027221.
DR GeneID; 76969; -.
DR KEGG; mmu:76969; -.
DR UCSC; uc008lfk.2; mouse.
DR CTD; 8534; -.
DR MGI; MGI:1924219; Chst1.
DR VEuPathDB; HostDB:ENSMUSG00000027221; -.
DR eggNOG; ENOG502S17I; Eukaryota.
DR GeneTree; ENSGT00940000161262; -.
DR HOGENOM; CLU_028381_3_2_1; -.
DR InParanoid; Q9EQC0; -.
DR OMA; CKEHGHV; -.
DR OrthoDB; 1246608at2759; -.
DR PhylomeDB; Q9EQC0; -.
DR TreeFam; TF342871; -.
DR BRENDA; 2.8.2.21; 3474.
DR Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
DR BioGRID-ORCS; 76969; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Chst1; mouse.
DR PRO; PR:Q9EQC0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9EQC0; protein.
DR Bgee; ENSMUSG00000027221; Expressed in lacrimal gland and 227 other tissues.
DR ExpressionAtlas; Q9EQC0; baseline and differential.
DR Genevisible; Q9EQC0; MM.
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; ISS:UniProtKB.
DR GO; GO:0001517; F:N-acetylglucosamine 6-O-sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0008146; F:sulfotransferase activity; ISO:MGI.
DR GO; GO:0006012; P:galactose metabolic process; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0018146; P:keratan sulfate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0042339; P:keratan sulfate metabolic process; ISO:MGI.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IBA:GO_Central.
DR GO; GO:0006790; P:sulfur compound metabolic process; ISO:MGI.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycoprotein; Golgi apparatus;
KW Inflammatory response; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..411
FT /note="Carbohydrate sulfotransferase 1"
FT /id="PRO_0000085183"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 3..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..411
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT MOTIF 337..339
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT BINDING 69..75
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 234..242
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 411 AA; 46904 MW; B1AE590EF5B9CBDC CRC64;
MQCSWKAVLL LALASIAIQY TAIRTFTAKS FHTCPGLTDT GLAERLCEEG PTFSYNLSRK
THVLILATTR SGSSFVGQLF NQHMDVFYLF EPLYHVQNTL IPRFTQGKSP ADRRVMLGAS
RDLLRSLYDC DLYFLENYIK PPPVNHTTNR VFRRGASRVL CSRPVCDPPG SSDLILEEGD
CVRMCGLLNL TLAAEACRER SHVAIKTVRV PEVNDLRALV EDPRLNLKVI QLVRDPRGIL
ASRSETFRDT YRLWRLWYGT GRKPYNLDVT QLTTVCEDFS SSVSTGLMRP SWLKGKYMLV
RYEDLARNPM KKTEEIYEFL GIPLDSHVAH WIQNNTRGDP TLGKHKYSTV RNSAATAEKW
RFRLSYDIVA FAQNACQQVL AQLGYKMANS EEELKNPAIS LVEERDFRPF L
