CHST8_MOUSE
ID CHST8_MOUSE Reviewed; 417 AA.
AC Q8BQ86; Q76EC6; Q80XD4;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Carbohydrate sulfotransferase 8;
DE EC=2.8.2.-;
DE AltName: Full=GalNAc-4-O-sulfotransferase 1;
DE Short=GalNAc-4-ST1;
DE Short=GalNAc4ST-1;
DE AltName: Full=N-acetylgalactosamine-4-O-sulfotransferase 1;
GN Name=Chst8;
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], ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12944377; DOI=10.1093/jb/mvg118;
RA Okuda T., Sawada T., Nakano H., Matsubara K., Matsuda Y., Fukuta M.,
RA Habuchi O.;
RT "Mouse N-acetylgalactosamine 4-sulfotransferases-1 and -2. Molecular
RT cloning, expression, chromosomal mapping and detection of their activity
RT with GalNAcbeta1-4GlcNAcbeta1-octyl.";
RL J. Biochem. 134:111-120(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Swiss Webster / NIH;
RA Hiraoka N., Fukuda M.;
RT "Mouse N-acetylgalactosamine 4 sulfotransferase (GalNAc4ST).";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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).
CC -!- FUNCTION: Catalyzes the transfer of sulfate to position 4 of non-
CC reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and
CC O-glycans. Required for biosynthesis of glycoprotein hormones lutropin
CC and thyrotropin, by mediating sulfation of their carbohydrate
CC structures. Only active against terminal GalNAcbeta1,GalNAcbeta. Not
CC active toward chondroitin.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in brain. Weakly expressed in
CC lung and kidney. Weakly expressed in pituitary.
CC {ECO:0000269|PubMed:12944377}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 2 family. {ECO:0000305}.
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DR EMBL; AB106878; BAC87753.1; -; mRNA.
DR EMBL; AF308145; AAQ14542.1; -; mRNA.
DR EMBL; AK051290; BAC34595.1; -; mRNA.
DR EMBL; BC051124; AAH51124.1; -; mRNA.
DR CCDS; CCDS21142.1; -.
DR RefSeq; NP_780349.3; NM_175140.4.
DR RefSeq; XP_006540400.1; XM_006540337.3.
DR RefSeq; XP_006540402.1; XM_006540339.2.
DR RefSeq; XP_006540403.1; XM_006540340.2.
DR RefSeq; XP_006540404.1; XM_006540341.1.
DR AlphaFoldDB; Q8BQ86; -.
DR STRING; 10090.ENSMUSP00000077752; -.
DR GlyConnect; 2179; 2 N-Linked glycans (1 site).
DR GlyGen; Q8BQ86; 5 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q8BQ86; -.
DR PhosphoSitePlus; Q8BQ86; -.
DR PaxDb; Q8BQ86; -.
DR PRIDE; Q8BQ86; -.
DR ProteomicsDB; 281469; -.
DR Antibodypedia; 2401; 144 antibodies from 27 providers.
DR DNASU; 68947; -.
DR Ensembl; ENSMUST00000078686; ENSMUSP00000077752; ENSMUSG00000060402.
DR Ensembl; ENSMUST00000205259; ENSMUSP00000145646; ENSMUSG00000060402.
DR Ensembl; ENSMUST00000238947; ENSMUSP00000159050; ENSMUSG00000060402.
DR GeneID; 68947; -.
DR KEGG; mmu:68947; -.
DR UCSC; uc009gjh.2; mouse.
DR CTD; 64377; -.
DR MGI; MGI:1916197; Chst8.
DR VEuPathDB; HostDB:ENSMUSG00000060402; -.
DR eggNOG; KOG4651; Eukaryota.
DR GeneTree; ENSGT00940000159100; -.
DR HOGENOM; CLU_043398_5_1_1; -.
DR InParanoid; Q8BQ86; -.
DR OMA; MDYLMFG; -.
DR OrthoDB; 1330889at2759; -.
DR PhylomeDB; Q8BQ86; -.
DR TreeFam; TF325581; -.
DR Reactome; R-MMU-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR BioGRID-ORCS; 68947; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Chst8; mouse.
DR PRO; PR:Q8BQ86; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BQ86; protein.
DR Bgee; ENSMUSG00000060402; Expressed in pelvic girdle bone/zone and 125 other tissues.
DR ExpressionAtlas; Q8BQ86; baseline and differential.
DR Genevisible; Q8BQ86; 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:0001537; F:N-acetylgalactosamine 4-O-sulfotransferase activity; IDA:MGI.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR GO; GO:0042446; P:hormone biosynthetic process; ISS:UniProtKB.
DR GO; GO:0016486; P:peptide hormone processing; TAS:MGI.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; IDA:MGI.
DR GO; GO:0006790; P:sulfur compound metabolic process; ISO:MGI.
DR InterPro; IPR018011; Carb_sulfotrans_8-10.
DR InterPro; IPR005331; Sulfotransferase.
DR PANTHER; PTHR12137; PTHR12137; 1.
DR Pfam; PF03567; Sulfotransfer_2; 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..417
FT /note="Carbohydrate sulfotransferase 8"
FT /id="PRO_0000189654"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..417
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 47..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 191..197
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 251..259
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 4
FT /note="R -> Q (in Ref. 2 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="A -> S (in Ref. 1; BAC87753)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="P -> L (in Ref. 1; BAC87753)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="H -> Y (in Ref. 1; BAC87753)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 48282 MW; 2902649D1839C3FA CRC64;
MTPRLGTMRL ACMFSSILLF GAAGLLLFIS LQDPIELSPQ QVPGIKFSIR PQQPQHDSHL
RISTEKGTRD SPSGSPRGLQ LQAPDQPRPH PKAAGSPLRL RQRRRRLLIK KMPAAGTNQG
NNSSETFIQP RPRTMDSRWV SLHQTQQERK RVMREACAKY RASSSRRAVT PRHVSRIFVE
DRHRVLYCEV PKAGCSNWKR VLMVLAGLAS STADIQHNTV HYGSALKRLD TFDRQGIVHR
LSTYTKMLFV REPFERLVSA FRDKFEHPNS YYHPVFGKAI LARYRANASR EALRTGSGVQ
FPEFVQYLLD VHRPVGMDIH WDHVSRLCSP CLIDYDFVGK FESMEDDANF FLRLIHAPGN
LTFPRFKDRH SEEARTTSRI THQYFAQLSS LQRQRTYDFY YMDYLMFNYS KPFSDLY
