CHSTE_MOUSE
ID CHSTE_MOUSE Reviewed; 376 AA.
AC Q80V53; A2AQV3; Q3TXA1; Q8R304; Q9D0P2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Carbohydrate sulfotransferase 14;
DE EC=2.8.2.35;
DE AltName: Full=Dermatan 4-sulfotransferase 1;
DE Short=D4ST-1;
GN Name=Chst14; Synonyms=D4st1;
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], DEVELOPMENTAL STAGE, FUNCTION, AND ENZYME
RP ACTIVITY.
RC TISSUE=Heart;
RX PubMed=16702220; DOI=10.1074/jbc.m510870200;
RA Mitsunaga C., Mikami T., Mizumoto S., Fukuda J., Sugahara K.;
RT "Chondroitin sulfate/dermatan sulfate hybrid chains in the development of
RT cerebellum. Spatiotemporal regulation of the expression of critical
RT disulfated disaccharides by specific sulfotransferases.";
RL J. Biol. Chem. 281:18942-18952(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and 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).
CC -!- FUNCTION: Catalyzes the transfer of sulfate to position 4 of the N-
CC acetylgalactosamine (GalNAc) residue of dermatan sulfate. Plays a
CC pivotal role in the formation of 4-0-sulfated IdoA blocks in dermatan
CC sulfate. Transfers sulfate to the C-4 hydroxyl of beta1,4-linked GalNAc
CC that is substituted with an alpha-linked iduronic acid (IdoUA) at the
CC C-3 hydroxyl. Transfers sulfate more efficiently to GalNAc residues in
CC -IdoUA-GalNAc-IdoUA- than in -GlcUA-GalNAc-GlcUA-sequences. Has
CC preference for partially desulfated dermatan sulfate. Addition of
CC sulfate to GalNAc may occur immediately after epimerization of GlcUA to
CC IdoUA. Appears to have an important role in the formation of the
CC cerebellar neural network during postnatal brain development.
CC {ECO:0000269|PubMed:16702220}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=n 3'-phosphoadenylyl sulfate + dermatan = n adenosine 3',5'-
CC bisphosphate + dermatan 4'-sulfate + n H(+); Xref=Rhea:RHEA:48052,
CC Rhea:RHEA-COMP:9965, Rhea:RHEA-COMP:11986, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:58465,
CC ChEBI:CHEBI:60059; EC=2.8.2.35;
CC Evidence={ECO:0000269|PubMed:16702220};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Low levels of expression in olfactory bulb,
CC caudate putamen, cerebral cortex, hippocampus, thalamus, midbrain and
CC cerebellum during early postnatal development. In later stages,
CC exclusively expressed in cerebellum culminating at P14 of postnatal
CC development. {ECO:0000269|PubMed:16702220}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 2 family. {ECO:0000305}.
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DR EMBL; AK011230; BAB27480.1; -; mRNA.
DR EMBL; AK154636; BAE32731.1; -; mRNA.
DR EMBL; AK159357; BAE35015.1; -; mRNA.
DR EMBL; AK171614; BAE42565.1; -; mRNA.
DR EMBL; AL845164; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026886; AAH26886.1; -; mRNA.
DR EMBL; BC043700; AAH43700.1; -; mRNA.
DR EMBL; BC085479; AAH85479.1; -; mRNA.
DR CCDS; CCDS16587.1; -.
DR RefSeq; NP_082393.3; NM_028117.3.
DR AlphaFoldDB; Q80V53; -.
DR IntAct; Q80V53; 1.
DR MINT; Q80V53; -.
DR STRING; 10090.ENSMUSP00000099579; -.
DR GlyGen; Q80V53; 2 sites.
DR PhosphoSitePlus; Q80V53; -.
DR MaxQB; Q80V53; -.
DR PaxDb; Q80V53; -.
DR PeptideAtlas; Q80V53; -.
DR PRIDE; Q80V53; -.
DR ProteomicsDB; 279076; -.
DR Antibodypedia; 23111; 107 antibodies from 24 providers.
DR DNASU; 72136; -.
DR Ensembl; ENSMUST00000099546; ENSMUSP00000099579; ENSMUSG00000074916.
DR GeneID; 72136; -.
DR KEGG; mmu:72136; -.
DR UCSC; uc012cbn.1; mouse.
DR CTD; 113189; -.
DR MGI; MGI:1919386; Chst14.
DR VEuPathDB; HostDB:ENSMUSG00000074916; -.
DR eggNOG; KOG4651; Eukaryota.
DR GeneTree; ENSGT00940000162640; -.
DR HOGENOM; CLU_043398_1_3_1; -.
DR InParanoid; Q80V53; -.
DR OMA; SQKNMPH; -.
DR OrthoDB; 1330889at2759; -.
DR PhylomeDB; Q80V53; -.
DR TreeFam; TF325581; -.
DR BRENDA; 2.8.2.35; 3474.
DR Reactome; R-MMU-2022923; Dermatan sulfate biosynthesis.
DR BioGRID-ORCS; 72136; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Chst14; mouse.
DR PRO; PR:Q80V53; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q80V53; protein.
DR Bgee; ENSMUSG00000074916; Expressed in humerus cartilage element and 177 other tissues.
DR ExpressionAtlas; Q80V53; baseline and differential.
DR Genevisible; Q80V53; 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; ISS:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR GO; GO:0030208; P:dermatan sulfate biosynthetic process; ISO:MGI.
DR GO; GO:0050655; P:dermatan sulfate proteoglycan metabolic process; ISS:UniProtKB.
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..376
FT /note="Carbohydrate sulfotransferase 14"
FT /id="PRO_0000189673"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..376
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 155..161
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 213..221
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 172
FT /note="I -> V (in Ref. 4; AAH43700/AAH26886)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="R -> P (in Ref. 4; AAH43700)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 43145 MW; 319E5A82E3AA4ACF CRC64;
MFPRPLTPLA APKSAETLGR TPRRAPLGRA RAGLGGPPLL LPSMLMFAVI VASSGLLLMI
ERGILSEMKP LPLHPPSHKG AAWSGTDPKP RGLSLDAGDS DLQVREDIRN RTLRAVCGQP
GMPRDPWDLP VGQRRTLLRH ILVSDRYRFL YCYVPKVACS NWKRVLKVLA GILNNVDVRL
KMDHRSDLVF LADLRPEEIR YRLQHYFKFL FVRDPLERLL SAYRNKFGEI REYQQRYGAE
IVRRYRAGAG PSPAGDDVTF PEFLRYLVDE DPEHMNEHWM PVYHLCQPCA VHYDFVGSYE
RLEADANQVL EWVRAPPHVR FPARQAWYRP ASPESLHYHL CNVPRALLQD VLPKYILDFS
LFAYPLPNVT KEACHQ
