UniProt data
UniProt name: CHSTF_HUMAN (Q7LFX5)
Gene name: CHST15; Synonyms=BRAG, GALNAC4S6ST, KIAA0598
Organism: Homo sapiens (Human).
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}.
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.
Transmembrane domains:
- 81-101, 21 AA, Helical; Signal-anchor for type II membrane protein. {ECO:0000255}.
Sequence: 561 AA
CATM prediction
The sequence of CHSTF_HUMAN returned 1 potential models
The positions at the dimer's interface are highlighted in yellow. The position at the crossing point is highlighted in orange.
| # | Sequence and interface | d | θ | Z' | ω' | Score |
|---|---|---|---|---|---|---|
| 80 90 100 | + | + | |
(Å) | (°) | (Å) | (°) | ||
| Model 1 | KRCSLVFGLIIMTLVMASYILSGAHQE | 7.3 | -45.1° | 4.0 | 39.3 | -13.5 |
Click on the model number to visualize its details below.
MODEL 1 DETAILS
Precited structure:
Download model 1 structure: PDB, PyMOL session
List of hydrogen bonds:
| Donor | Acceptor | Distance |
|---|---|---|
| B, 82, LEU, HA | A, 81, SER, O | 3.22Å |
| B, 85, GLY, HA1 | A, 82, LEU, O | 3.38Å |
| A, 82, LEU, HA | B, 81, SER, O | 3.22Å |
| A, 85, GLY, HA1 | B, 82, LEU, O | 3.38Å |

