ID CHSTF_MOUSE Reviewed; 561 AA.
AC Q91XQ5; Q80TW4; Q8BLQ5; Q9D2N6;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 24-JAN-2024, entry version 150.
DE RecName: Full=Carbohydrate sulfotransferase 15;
DE EC=2.8.2.33;
DE AltName: Full=B-cell RAG-associated gene protein;
DE AltName: Full=N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase;
DE Short=GalNAc4S-6ST;
GN Name=Chst15; Synonyms=Brag, Galnac4s6st, Kiaa0598;
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].
RX PubMed=9754571;
RX DOI=10.1002/(sici)1521-4141(199809)28:09<2839::aid-immu2839>3.0.co;2-6;
RA Verkoczy L.K., Marsden P.A., Berinstein N.L.;
RT "hBRAG, a novel B cell lineage cDNA encoding a type II transmembrane
RT glycoprotein potentially involved in the regulation of recombination
RT activating gene 1 (RAG1).";
RL Eur. J. Immunol. 28:2839-2853(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ohtake S., Morisaki T., Kondo S., Matsumura K., Kimata K., Habuchi O.;
RT "Characterization of GalNAc 4-sulfate 6-O-sulfotransferase expressed in
RT bone marrow derived mast cells synthesizing chondroitin sulfate E.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Brain cortex, Cerebellum, Skin, and Urinary bladder;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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: Sulfotransferase that transfers sulfate from 3'-
CC phosphoadenosine 5'-phosphosulfate (PAPS) to the C-6 hydroxyl group of
CC the GalNAc 4-sulfate residue of chondroitin sulfate A and forms
CC chondroitin sulfate E containing GlcA-GalNAc(4,6-SO(4)) repeating
CC units. It also transfers sulfate to a unique non-reducing terminal
CC sequence, GalNAc(4SO4)-GlcA(2SO4)-GalNAc(6SO4), to yield a highly
CC sulfated structure similar to the structure found in thrombomodulin
CC chondroitin sulfate. May also act as a B-cell receptor involved in BCR
CC ligation-mediated early activation that mediate regulatory signals key
CC to B-cell development and/or regulation of B-cell-specific RAG
CC expression; however such results are unclear in vivo (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=n 3'-phosphoadenylyl sulfate + dermatan 4'-sulfate = n
CC adenosine 3',5'-bisphosphate + dermatan 4',6'-bissulfate + n H(+);
CC Xref=Rhea:RHEA:54304, Rhea:RHEA-COMP:9965, Rhea:RHEA-COMP:13850,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:58465, ChEBI:CHEBI:138121; EC=2.8.2.33;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=n 3'-phosphoadenylyl sulfate + chondroitin 4'-sulfate = n
CC adenosine 3',5'-bisphosphate + chondroitin 4',6'-bissulfate + n H(+);
CC Xref=Rhea:RHEA:54300, Rhea:RHEA-COMP:9829, Rhea:RHEA-COMP:13849,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:58422, ChEBI:CHEBI:138112; EC=2.8.2.33;
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=glutathione; Xref=ChEBI:CHEBI:57925; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by phenyl beta-GalNAc(4,6-SO(4)).
CC -!- SUBUNIT: Homodimer; disulfide-linked (Potential). The relevance of
CC homodimerization is however unsure. May interact with phosphorylated
CC proteins in resting B-cells, including HCK (By similarity).
CC {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}. Note=A small fraction may
CC also be present at the cell surface, where it acts as a B-cell
CC receptor.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65606.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF320786; AAK69604.1; -; mRNA.
DR EMBL; AB187269; BAD89559.1; -; mRNA.
DR EMBL; AK122324; BAC65606.1; ALT_INIT; mRNA.
DR EMBL; AK019474; BAB31743.1; -; mRNA.
DR EMBL; AK035637; BAC29133.1; -; mRNA.
DR EMBL; AK043803; BAC31658.1; -; mRNA.
DR EMBL; AK082318; BAC38463.1; -; mRNA.
DR EMBL; AK083614; BAC38968.1; -; mRNA.
DR EMBL; BC031443; AAH31443.1; -; mRNA.
DR CCDS; CCDS21922.1; -.
DR RefSeq; NP_084211.2; NM_029935.5.
DR RefSeq; XP_006508395.1; XM_006508332.1.
DR RefSeq; XP_006508396.1; XM_006508333.3.
DR RefSeq; XP_017167875.1; XM_017312386.1.
DR AlphaFoldDB; Q91XQ5; -.
DR STRING; 10090.ENSMUSP00000076682; -.
DR GlyCosmos; Q91XQ5; 1 site, No reported glycans.
DR GlyGen; Q91XQ5; 1 site.
DR iPTMnet; Q91XQ5; -.
DR PhosphoSitePlus; Q91XQ5; -.
DR MaxQB; Q91XQ5; -.
DR PaxDb; 10090-ENSMUSP00000079105; -.
DR ProteomicsDB; 281681; -.
DR Antibodypedia; 2663; 78 antibodies from 24 providers.
DR Ensembl; ENSMUST00000077472.10; ENSMUSP00000076682.4; ENSMUSG00000030930.15.
DR Ensembl; ENSMUST00000080215.6; ENSMUSP00000079105.6; ENSMUSG00000030930.15.
DR GeneID; 77590; -.
DR KEGG; mmu:77590; -.
DR UCSC; uc009kbx.1; mouse.
DR AGR; MGI:1924840; -.
DR CTD; 51363; -.
DR MGI; MGI:1924840; Chst15.
DR VEuPathDB; HostDB:ENSMUSG00000030930; -.
DR eggNOG; ENOG502QU6N; Eukaryota.
DR GeneTree; ENSGT00390000004719; -.
DR HOGENOM; CLU_017703_2_1_1; -.
DR InParanoid; Q91XQ5; -.
DR OMA; HVDSKQM; -.
DR OrthoDB; 3939141at2759; -.
DR PhylomeDB; Q91XQ5; -.
DR TreeFam; TF333516; -.
DR BRENDA; 2.8.2.33; 3474.
DR Reactome; R-MMU-2022870; Chondroitin sulfate biosynthesis.
DR BioGRID-ORCS; 77590; 2 hits in 77 CRISPR screens.
DR PRO; PR:Q91XQ5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q91XQ5; Protein.
DR Bgee; ENSMUSG00000030930; Expressed in epithelium of cochlear duct and 283 other cell types or tissues.
DR Genevisible; Q91XQ5; MM.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050656; F:3'-phosphoadenosine 5'-phosphosulfate binding; ISS:UniProtKB.
DR GO; GO:0050659; F:N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase activity; ISS:UniProtKB.
DR GO; GO:0019319; P:hexose biosynthetic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR PANTHER; PTHR15723; CARBOHYDRATE SULFOTRANSFERASE 15; 1.
DR PANTHER; PTHR15723:SF0; CARBOHYDRATE SULFOTRANSFERASE 15; 1.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..561
FT /note="Carbohydrate sulfotransferase 15"
FT /id="PRO_0000225624"
FT TOPO_DOM 1..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..561
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 263..267
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 115
FT /note="G -> S (in Ref. 4; BAB31743)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="I -> V (in Ref. 4; BAC31658)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 561 AA; 64986 MW; E00ADD0584559278 CRC64;
MRHCINCCVQ LFPEDTHKQQ VACQGGPHHS HQACPTCKGE NKILFRVDSK QMNLLAVLEV
RTEGNENWGG FLRFRKGKRC SLVFGLIIMT LVMASYILSG AHQELLISSP FHYGGFPSNP
SVMDGENPSD VKEHHYQPSV NNISYVKDYP SIKLIIDSIA ARIEFTTRQL PDLQDLKRQE
LHMFSVIPSK FLPTSKSPCW YEEFSGRNTT DPYLTNSYVL YSKRFRSTFD ALRKVFWGHL
SHVQGKHFRL RCLPHFYIIG QPKCGTTDLY DRLRLHPEVK FSAIKEPHWW TRKRFGIVRL
RDGLRDRYPV EDYLDLFDLA AHQIHQGLQA ASAEQPSKMN KIIIGEASAS TMWDNNAWTF
FYDNSTDGEP PFLTQDFIHA FQPEAKLIVM LRDPVERLYS DYLYFASSNK SADDFHEKVT
EALQLFENCM LDYSLRACVY NNTLNNAMPV RLQVGLYAVY LLDWLTVFSK EQFLILRLED
HASNVKYTMH KVFQFLNLGP LSEKQEALMT KSPASNTRRP EDRSLGPMWP ITQKILREFY
GPFNTRLAQV LDDEAFAWKT T
//
