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Carbohydrate sulfotransferase 15 (EC 2.8.2.33) (B-cell RAG-associated gene protein) (hBRAG) (N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase) (GalNAc4S-6ST)

 CHSTF_HUMAN             Reviewed;         561 AA.
Q7LFX5; O60338; O60474; Q86VM4;
07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
27-SEP-2017, entry version 137.
RecName: Full=Carbohydrate sulfotransferase 15;
EC=2.8.2.33;
AltName: Full=B-cell RAG-associated gene protein;
Short=hBRAG;
AltName: Full=N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase;
Short=GalNAc4S-6ST;
Name=CHST15; Synonyms=BRAG, GALNAC4S6ST, KIAA0598;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Pre-B cell;
PubMed=9754571;
DOI=10.1002/(SICI)1521-4141(199809)28:09<2839::AID-IMMU2839>3.0.CO;2-6;
Verkoczy L.K., Marsden P.A., Berinstein N.L.;
"hBRAG, a novel B cell lineage cDNA encoding a type II transmembrane
glycoprotein potentially involved in the regulation of recombination
activating gene 1 (RAG1).";
Eur. J. Immunol. 28:2839-2853(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11032940;
Yuki M., Yoshinaga K., Yamakawa H., Sakurada K., Sato S., Yajima A.,
Horii A.;
"Structure, expression and mutational analysis of the hBRAG gene on
10q in the frequently deleted region in human endometrial cancer.";
Oncol. Rep. 7:1339-1342(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
TISSUE=Brain;
PubMed=11572857; DOI=10.1074/jbc.M104922200;
Ohtake S., Ito Y., Fukuta M., Habuchi O.;
"Human N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase cDNA is
related to human B cell recombination activating gene-associated
gene.";
J. Biol. Chem. 276:43894-43900(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9628581; DOI=10.1093/dnares/5.1.31;
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
Ohara O.;
"Prediction of the coding sequences of unidentified human genes. IX.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:31-39(1998).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Blood, Duodenum, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
POSSIBLE FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION,
DISULFIDE BOND, AND INTERACTION WITH HCK.
PubMed=10749872; DOI=10.1074/jbc.M001866200;
Verkoczy L.K., Guinn B.-A., Berinstein N.L.;
"Characterization of the human B cell RAG-associated gene, hBRAG, as a
B cell receptor signal-enhancing glycoprotein dimer that associates
with phosphorylated proteins in resting B cells.";
J. Biol. Chem. 275:20967-20979(2000).
[9]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=12874280; DOI=10.1074/jbc.M306132200;
Ohtake S., Kimata K., Habuchi O.;
"A unique nonreducing terminal modification of chondroitin sulfate by
N-acetylgalactosamine 4-sulfate 6-o-sulfotransferase.";
J. Biol. Chem. 278:38443-38452(2003).
[10]
ENZYME REGULATION.
PubMed=16024005; DOI=10.1016/j.carres.2005.06.010;
Sawada T., Fujii S., Nakano H., Ohtake S., Kimata K., Habuchi O.;
"Synthesis of sulfated phenyl 2-acetamido-2-deoxy-D--D-
galactopyranosides. 4-O-Sulfated phenyl 2-acetamido-2-deoxy-beta-D-
galactopyranoside is a competitive acceptor that decreases sulfation
of chondroitin sulfate by N-acetylgalactosamine 4-sulfate 6-O-
sulfotransferase.";
Carbohydr. Res. 340:1983-1996(2005).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
-!- FUNCTION: Sulfotransferase that transfers sulfate from 3'-
phosphoadenosine 5'-phosphosulfate (PAPS) to the C-6 hydroxyl
group of the GalNAc 4-sulfate residue of chondroitin sulfate A and
forms chondroitin sulfate E containing GlcA-GalNAc(4,6-SO(4))
repeating units. It also transfers sulfate to a unique non-
reducing terminal sequence, GalNAc(4SO4)-GlcA(2SO4)-GalNAc(6SO4),
to yield a highly sulfated structure similar to the structure
found in thrombomodulin chondroitin sulfate. May also act as a B-
cell receptor involved in BCR ligation-mediated early activation
that mediate regulatory signals key to B-cell development and/or
regulation of B-cell-specific RAG expression; however such results
are unclear in vivo. {ECO:0000269|PubMed:11572857,
ECO:0000269|PubMed:12874280}.
-!- CATALYTIC ACTIVITY: 3-phospho-5-adenylyl sulfate + [dermatan]-4-O-
sulfo-N-acetylgalactosamine = adenosine 3',5'-bisphosphate +
[dermatan]-4,6-di-O-sulfo-N-acetyl-D-galactosamine.
{ECO:0000269|PubMed:12874280}.
-!- CATALYTIC ACTIVITY: 3-phospho-5-adenylyl sulfate + [chondroitin]-
4-O-sulfo-N-acetylgalactosamine = adenosine 3',5'-bisphosphate +
[chondroitin]-4,6-di-O-sulfo-N-acetyl-D-galactosamine.
{ECO:0000269|PubMed:12874280}.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000250};
-!- COFACTOR:
Name=glutathione; Xref=ChEBI:CHEBI:57925; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Inhibited by phenyl beta-GalNAc(4,6-SO(4)).
{ECO:0000269|PubMed:16024005}.
-!- SUBUNIT: Homodimer; disulfide-linked (Potential). The relevance of
homodimerization is however unsure. May interact with
phosphorylated proteins in resting B-cells, including HCK.
{ECO:0000269|PubMed:10749872, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000305|PubMed:10749872}; Single-pass type II membrane
protein {ECO:0000305|PubMed:10749872}. Note=A small fraction may
also be present at the cell surface, where it acts as a B-cell
receptor.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q7LFX5-1; Sequence=Displayed;
Name=2;
IsoId=Q7LFX5-2; Sequence=VSP_017387;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in B-cell-enriched tissues but not
in fetal or adult thymus. Expressed in fetal and adult spleen,
lymph node, tonsil, bone marrow and peripheral leukocytes. Not
expressed in T-cells. In pro-B, pre-B, and mature B-cell lines, it
colocalizes with RAG1. {ECO:0000269|PubMed:9754571}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:10749872}.
-!- SIMILARITY: Belongs to the sulfotransferase 1 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC71691.1; Type=Frameshift; Positions=180, 223, 489, 537; Evidence={ECO:0000305};
Sequence=AAH50540.1; Type=Frameshift; Positions=511; Evidence={ECO:0000305};
Sequence=BAA25524.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF026477; AAC71691.1; ALT_FRAME; mRNA.
EMBL; AB025341; BAA83686.1; -; Genomic_DNA.
EMBL; AB062423; BAB72145.1; -; mRNA.
EMBL; AB011170; BAA25524.2; ALT_INIT; mRNA.
EMBL; CR749804; CAH18664.1; -; mRNA.
EMBL; AL683842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC027908; AAH27908.1; -; mRNA.
EMBL; BC050540; AAH50540.1; ALT_FRAME; mRNA.
EMBL; BC075813; AAH75813.1; -; mRNA.
CCDS; CCDS55731.1; -. [Q7LFX5-2]
CCDS; CCDS7638.1; -. [Q7LFX5-1]
RefSeq; NP_001257693.1; NM_001270764.1. [Q7LFX5-1]
RefSeq; NP_001257694.1; NM_001270765.1. [Q7LFX5-2]
RefSeq; NP_056976.2; NM_015892.4. [Q7LFX5-1]
RefSeq; XP_005269948.1; XM_005269891.3. [Q7LFX5-1]
RefSeq; XP_006717954.1; XM_006717891.3. [Q7LFX5-1]
RefSeq; XP_016871808.1; XM_017016319.1. [Q7LFX5-1]
UniGene; Hs.287537; -.
UniGene; Hs.745222; -.
ProteinModelPortal; Q7LFX5; -.
BioGrid; 119498; 25.
IntAct; Q7LFX5; 20.
STRING; 9606.ENSP00000333947; -.
iPTMnet; Q7LFX5; -.
PhosphoSitePlus; Q7LFX5; -.
DMDM; 74749920; -.
PaxDb; Q7LFX5; -.
PeptideAtlas; Q7LFX5; -.
PRIDE; Q7LFX5; -.
Ensembl; ENST00000346248; ENSP00000333947; ENSG00000182022. [Q7LFX5-1]
Ensembl; ENST00000435907; ENSP00000402394; ENSG00000182022. [Q7LFX5-1]
Ensembl; ENST00000628426; ENSP00000485905; ENSG00000182022. [Q7LFX5-2]
GeneID; 51363; -.
KEGG; hsa:51363; -.
UCSC; uc001lhm.5; human. [Q7LFX5-1]
CTD; 51363; -.
DisGeNET; 51363; -.
EuPathDB; HostDB:ENSG00000182022.17; -.
GeneCards; CHST15; -.
HGNC; HGNC:18137; CHST15.
HPA; HPA017584; -.
MIM; 608277; gene.
neXtProt; NX_Q7LFX5; -.
OpenTargets; ENSG00000182022; -.
PharmGKB; PA165548385; -.
eggNOG; ENOG410IISS; Eukaryota.
eggNOG; ENOG410XSMU; LUCA.
GeneTree; ENSGT00390000004719; -.
HOGENOM; HOG000154435; -.
InParanoid; Q7LFX5; -.
KO; K08106; -.
OMA; HASNVKY; -.
OrthoDB; EOG091G039B; -.
PhylomeDB; Q7LFX5; -.
TreeFam; TF333516; -.
BioCyc; MetaCyc:HS11694-MONOMER; -.
BRENDA; 2.8.2.33; 2681.
Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis.
ChiTaRS; CHST15; human.
GeneWiki; GALNAC4S-6ST; -.
GenomeRNAi; 51363; -.
PRO; PR:Q7LFX5; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000182022; -.
ExpressionAtlas; Q7LFX5; baseline and differential.
Genevisible; Q7LFX5; HS.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0050656; F:3'-phosphoadenosine 5'-phosphosulfate binding; IDA:UniProtKB.
GO; GO:0050659; F:N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase activity; IDA:UniProtKB.
GO; GO:0030206; P:chondroitin sulfate biosynthetic process; TAS:Reactome.
GO; GO:0019319; P:hexose biosynthetic process; IDA:UniProtKB.
InterPro; IPR027417; P-loop_NTPase.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein;
Golgi apparatus; Membrane; Reference proteome; Signal-anchor;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 561 Carbohydrate sulfotransferase 15.
/FTId=PRO_0000225623.
TOPO_DOM 1 80 Cytoplasmic. {ECO:0000255}.
TRANSMEM 81 101 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 102 561 Lumenal. {ECO:0000255}.
NP_BIND 263 267 PAPS. {ECO:0000250}.
BINDING 392 392 PAPS. {ECO:0000250}.
BINDING 400 400 PAPS. {ECO:0000250}.
CARBOHYD 364 364 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 451 561 RLQVGLYAVYLLDWLSVFDKQQFLILRLEDHASNVKYTMHK
VFQFLNLGPLSEKQEALMTKSPASNARRPEDRNLGPMWPIT
QKILRDFYRPFNARLAQVLADEAFAWKTT -> CTPPPRTP
RAGPWQKELVCCYYASGIVGLRFSIGTERSVLMCKCCSPLF
MDVKAEN (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_017387.
SEQUENCE 561 AA; 64926 MW; 74643A7CFF7F242D CRC64;
MRHCINCCIQ LLPDGAHKQQ VNCQGGPHHG HQACPTCKGE NKILFRVDSK QMNLLAVLEV
RTEGNENWGG FLRFKKGKRC SLVFGLIIMT LVMASYILSG AHQELLISSP FHYGGFPSNP
SLMDSENPSD TKEHHHQSSV NNISYMKDYP SIKLIINSIT TRIEFTTRQL PDLEDLKKQE
LHMFSVIPNK FLPNSKSPCW YEEFSGQNTT DPYLTNSYVL YSKRFRSTFD ALRKAFWGHL
AHAHGKHFRL RCLPHFYIIG QPKCGTTDLY DRLRLHPEVK FSAIKEPHWW TRKRFGIVRL
RDGLRDRYPV EDYLDLFDLA AHQIHQGLQA SSAKEQSKMN TIIIGEASAS TMWDNNAWTF
FYDNSTDGEP PFLTQDFIHA FQPNARLIVM LRDPVERLYS DYLYFASSNK SADDFHEKVT
EALQLFENCM LDYSLRACVY NNTLNNAMPV RLQVGLYAVY LLDWLSVFDK QQFLILRLED
HASNVKYTMH KVFQFLNLGP LSEKQEALMT KSPASNARRP EDRNLGPMWP ITQKILRDFY
RPFNARLAQV LADEAFAWKT T


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