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Protein

Carbohydrate sulfotransferase 15

Gene

Chst15

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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-SO4) 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 (By similarity).By similarity

Catalytic activityi

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.
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.

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Inhibited by phenyl beta-GalNAc(4,6-SO4).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei392 – 3921PAPSBy similarity
Binding sitei400 – 4001PAPSBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi263 – 2675PAPSBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Carbohydrate sulfotransferase 15 (EC:2.8.2.33)
Alternative name(s):
N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase
Short name:
GalNAc4S-6ST
Gene namesi
Name:Chst15
Synonyms:Galnac4s6st
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi628881. Chst15.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8080CytoplasmicSequence analysisAdd
BLAST
Transmembranei81 – 10121Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini102 – 561460LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 561561Carbohydrate sulfotransferase 15PRO_0000225625Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi364 – 3641N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8CHI9.
PRIDEiQ8CHI9.

PTM databases

PhosphoSiteiQ8CHI9.

Interactioni

Subunit structurei

Homodimer; disulfide-linked (Potential). The relevance of homodimerization is however unsure. May interact with phosphorylated proteins in resting B-cells, including HCK (By similarity).By similarityCurated

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022157.

Structurei

3D structure databases

ProteinModelPortaliQ8CHI9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfotransferase 1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IISS. Eukaryota.
ENOG410XSMU. LUCA.
HOGENOMiHOG000154435.
InParanoidiQ8CHI9.
KOiK08106.
PhylomeDBiQ8CHI9.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8CHI9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRHCINCCIQ LFPEDAHKQQ VACQGGPHHS HQACPSCKGE DKILFRVDSK
60 70 80 90 100
QMNLLAVLEV RTEGNENWGG FLRFRKGKRC SLVFGLIIMT LVMASYILSG
110 120 130 140 150
AHQELLISSP FHYGGFPSNP SVMDSESPSD VKEHHYQPSV NNISYVKDYP
160 170 180 190 200
NIKLIIDSIA ARNEFTTRQL PDLQDLKRQE LHMFSVIPNK FLPTSKSPCW
210 220 230 240 250
YEEFSGRNTT DPYLTNSYVL YSKRFRSTFD TLRKAFWGHL SHVHGKHFRL
260 270 280 290 300
RCLPHFYIIG QPKCGTTDLY DRLRLHPEVK FSAIKEPHWW TRKRFGIVRL
310 320 330 340 350
RDGLRDRYPV EDYLDLFDLA AHQIHQGLQA ASAEQTSKMN RIIIGEASAS
360 370 380 390 400
TMWDNNAWTF FYDNSTDGEP PFLTQDFIHA FQPEAKLLVM LRDPVERLYS
410 420 430 440 450
DYLYFASSNK SADDFHEKVT EALQLFENCM LDYSLRACVY NNTLNNAMPV
460 470 480 490 500
RLQVGLYAVY LLDWLTVFSK EQFLILRLED HASNVKYTMH KVFQFLNLGP
510 520 530 540 550
LSEKQEALMT KSPASNTRRP EDRSLGPMWP ITQKILRDFY GPFNTRLAQV
560
LDDEAFAWKT T
Length:561
Mass (Da):65,044
Last modified:March 1, 2003 - v1
Checksum:i77219992521FC054
GO
Isoform 2 (identifier: Q8CHI9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     397-403: RLYSDYL → SIQQSQV
     404-561: Missing.

Note: No experimental confirmation available.
Show »
Length:403
Mass (Da):46,568
Checksum:iAE4A0F780E142A6B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51I → L in BAC53776 (PubMed:15489334).Curated
Sequence conflicti41 – 411D → N in BAC53776 (PubMed:15489334).Curated
Sequence conflicti163 – 1631N → I in BAC53776 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei397 – 4037RLYSDYL → SIQQSQV in isoform 2. 1 PublicationVSP_017388
Alternative sequencei404 – 561158Missing in isoform 2. 1 PublicationVSP_017389Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC085687 mRNA. Translation: AAH85687.1.
AB086953 mRNA. Translation: BAC53776.1.
RefSeqiNP_775432.3. NM_173310.3. [Q8CHI9-1]
XP_008758091.1. XM_008759869.1.
UniGeneiRn.217784.

Genome annotation databases

GeneIDi286974.
KEGGirno:286974.
UCSCiRGD:628881. rat. [Q8CHI9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC085687 mRNA. Translation: AAH85687.1.
AB086953 mRNA. Translation: BAC53776.1.
RefSeqiNP_775432.3. NM_173310.3. [Q8CHI9-1]
XP_008758091.1. XM_008759869.1.
UniGeneiRn.217784.

3D structure databases

ProteinModelPortaliQ8CHI9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022157.

PTM databases

PhosphoSiteiQ8CHI9.

Proteomic databases

PaxDbiQ8CHI9.
PRIDEiQ8CHI9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi286974.
KEGGirno:286974.
UCSCiRGD:628881. rat. [Q8CHI9-1]

Organism-specific databases

CTDi51363.
RGDi628881. Chst15.

Phylogenomic databases

eggNOGiENOG410IISS. Eukaryota.
ENOG410XSMU. LUCA.
HOGENOMiHOG000154435.
InParanoidiQ8CHI9.
KOiK08106.
PhylomeDBiQ8CHI9.

Miscellaneous databases

PROiQ8CHI9.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase cDNA."
    Ichihara-Tanaka K., Muramatsu T.
    Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Heart.

Entry informationi

Entry nameiCHSTF_RAT
AccessioniPrimary (citable) accession number: Q8CHI9
Secondary accession number(s): Q5U363
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.