CHSTF_RAT
ID CHSTF_RAT Reviewed; 561 AA.
AC Q8CHI9; Q5U363;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Carbohydrate sulfotransferase 15;
DE EC=2.8.2.33;
DE AltName: Full=N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase;
DE Short=GalNAc4S-6ST;
GN Name=Chst15; Synonyms=Galnac4s6st;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Ichihara-Tanaka K., Muramatsu T.;
RT "N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase cDNA.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Heart;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CHI9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CHI9-2; Sequence=VSP_017388, VSP_017389;
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; BC085687; AAH85687.1; -; mRNA.
DR EMBL; AB086953; BAC53776.1; -; mRNA.
DR RefSeq; NP_775432.3; NM_173310.3. [Q8CHI9-1]
DR AlphaFoldDB; Q8CHI9; -.
DR STRING; 10116.ENSRNOP00000022157; -.
DR GlyGen; Q8CHI9; 1 site.
DR PhosphoSitePlus; Q8CHI9; -.
DR PaxDb; Q8CHI9; -.
DR PRIDE; Q8CHI9; -.
DR GeneID; 286974; -.
DR KEGG; rno:286974; -.
DR UCSC; RGD:628881; rat. [Q8CHI9-1]
DR CTD; 51363; -.
DR RGD; 628881; Chst15.
DR eggNOG; ENOG502QU6N; Eukaryota.
DR InParanoid; Q8CHI9; -.
DR PhylomeDB; Q8CHI9; -.
DR Reactome; R-RNO-2022870; Chondroitin sulfate biosynthesis.
DR PRO; PR:Q8CHI9; -.
DR Proteomes; UP000002494; Unplaced.
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: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; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..561
FT /note="Carbohydrate sulfotransferase 15"
FT /id="PRO_0000225625"
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 VAR_SEQ 397..403
FT /note="RLYSDYL -> SIQQSQV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017388"
FT VAR_SEQ 404..561
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017389"
FT CONFLICT 5
FT /note="I -> L (in Ref. 2; BAC53776)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="D -> N (in Ref. 2; BAC53776)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="N -> I (in Ref. 2; BAC53776)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 561 AA; 65044 MW; 77219992521FC054 CRC64;
MRHCINCCIQ LFPEDAHKQQ VACQGGPHHS HQACPSCKGE DKILFRVDSK QMNLLAVLEV
RTEGNENWGG FLRFRKGKRC SLVFGLIIMT LVMASYILSG AHQELLISSP FHYGGFPSNP
SVMDSESPSD VKEHHYQPSV NNISYVKDYP NIKLIIDSIA ARNEFTTRQL PDLQDLKRQE
LHMFSVIPNK FLPTSKSPCW YEEFSGRNTT DPYLTNSYVL YSKRFRSTFD TLRKAFWGHL
SHVHGKHFRL RCLPHFYIIG QPKCGTTDLY DRLRLHPEVK FSAIKEPHWW TRKRFGIVRL
RDGLRDRYPV EDYLDLFDLA AHQIHQGLQA ASAEQTSKMN RIIIGEASAS TMWDNNAWTF
FYDNSTDGEP PFLTQDFIHA FQPEAKLLVM LRDPVERLYS DYLYFASSNK SADDFHEKVT
EALQLFENCM LDYSLRACVY NNTLNNAMPV RLQVGLYAVY LLDWLTVFSK EQFLILRLED
HASNVKYTMH KVFQFLNLGP LSEKQEALMT KSPASNTRRP EDRSLGPMWP ITQKILRDFY
GPFNTRLAQV LDDEAFAWKT T
