Q7KVA1
PR
Gene name |
oxt (CG17771, CG32300) |
Protein name |
Xylosyltransferase oxt |
Names |
Imaginal disk type I, Peptide O-xylosyltransferase |
Species |
Drosophila melanogaster (Fruit fly) |
KEGG Pathway |
dme:Dmel_CG32300 |
EC number |
2.4.2.26: Pentosyltransferases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q7KVA1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q7KVA1-F1 | Predicted | AlphaFoldDB |
No variants for Q7KVA1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q7KVA1 | |||||
No associated diseases with Q7KVA1
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.2.26 | Pentosyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| Golgi membrane | The lipid bilayer surrounding any of the compartments of the Golgi apparatus. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| protein xylosyltransferase activity | Catalysis of the transfer of a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| chondroitin sulfate biosynthetic process | The chemical reactions and pathways resulting in the formation of chondroitin sulfate, any member of a group of 10-60 kDa glycosaminoglycans, widely distributed in cartilage and other mammalian connective tissues, the repeat units of which consist of beta-(1,4)-linked D-glucuronyl beta-(1,3)-N-acetyl-D-galactosamine sulfate. |
| chondroitin sulfate metabolic process | The chemical reactions and pathways involving chondroitin sulfate, any member of a group of 10-60 kDa glycosaminoglycans, widely distributed in cartilage and other mammalian connective tissues, the repeat units of which consist of beta-(1,4)-linked D-glucuronyl beta-(1,3)-N-acetyl-D-galactosamine sulfate. They usually occur linked to a protein to form proteoglycans. Two subgroups exist, one in which the sulfate is on the 4-position (chondroitin sulfate A) and the second in which it is in the 6-position (chondroitin sulfate C). They often are polydisperse and often differ in the degree of sulfation from tissue to tissue. The chains of repeating disaccharide are covalently linked to the side chains of serine residues in the polypeptide backbone of a protein by a glycosidic attachment through the trisaccharide unit galactosyl-galactosyl-xylosyl. Chondroitin sulfate B is more usually known as dermatan sulfate. |
| chondroitin sulfate proteoglycan biosynthetic process | The chemical reactions and pathways resulting in the formation of chondroitin sulfate proteoglycan, any glycoprotein whose glycosaminoglycan units are chondroitin sulfate. Chondroitin sulfates are a group of 10-60 kDa glycosaminoglycans, widely distributed in cartilage and other mammalian connective tissues; the repeat units consist of beta-(1,4)-linked D-glucuronyl beta-(1,3)-N-acetyl-D-galactosamine sulfate. |
| D-xylose metabolic process | The chemical reactions and pathways involving D-xylose, a naturally occurring plant polysaccharide. |
| heparan sulfate proteoglycan biosynthetic process | The chemical reactions and pathways resulting in the formation of the heparan sulfate proteoglycan, a glycosaminoglycan with repeat unit consisting of alternating alpha-(1->4)-linked hexuronic acid and glucosamine residues; the former are a mixture of sulfated and nonsulfated D-glucuronic acid and L-iduronic acid; the L-iduronic acid is either sulfated or acetylated on its amino group as well as being sulfated on one of its hydroxyl groups; heparan sulfate chains are covalently linked to peptidyl-serine by a glycosidic attachment through the trisaccharide galactosyl-galactosyl-xylosyl to serine residues. |
| heparan sulfate proteoglycan metabolic process | The chemical reactions and pathways involving any proteoglycan containing heparan sulfate, any member of a group of glycosaminoglycans that have repeat units consisting of alternating alpha-(1->4)-linked hexuronic acid and glucosamine residues, the former being a mixture of sulfated and nonsulfated D-glucuronic and L-iduronic acids, and the latter being either sulfated or acetylated on its amino group as well as sulfated on one of its hydroxyl groups. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9EPI1 | Xylt1 | Xylosyltransferase 1 | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEQSVSARWL | KRYRAFFLIL | LLIVAIQLFL | AYKSLDIVGG | GSGSGFDAAE | APASPPPPHA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QARVQPPART | KLTAQQLGFQ | PECDILAREA | ISALQRAKTK | DCREHIAQIA | CAIQAGRFYA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PQLRSSCPAG | NHTANVSLGC | FKDEKDRRLL | AGYYSSSKTS | NSPAKCVELC | LQSGYPYAGV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QYGRECFCGY | DPPPKASKLP | DSSCNTKCLG | NAKEICGGFY | AMNIYETGIA | KFTAQLAATT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PSEETKRVRI | AFLLTLNGRA | LRQVHRLLKA | LYAPEHVYYI | HVDERQDYLY | RKLLELESKF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PNIRLARKRF | STIWGGASLL | TMLLQCMEDL | LQSNWHWDFV | INLSESDFPV | KTLDKLVDFL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SANPGRNFVK | GHGRETQKFI | QKQGLDKTFV | ECDTHMWRIG | DRKLPAGIQV | DGGSDWVALS |
| 430 | 440 | 450 | 460 | 470 | 480 |
| RPFVGYVTHP | REDDELLQAL | LKLFRHTLLP | AESFFHTVLR | NTKHCTSYVD | NNLHVTNWKR |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KQGCKCQYKH | VVDWCGCSPN | DFKPEDWPRL | QATEQKSLFF | ARKFEPVINQ | AVLLQLEEWL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| YGPYTSEYAN | LHGYWQSLYH | HEDVHGSGDD | LARSIGDSVM | RLSARQAKLY | PLELIELTHY |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LHRDQYKGFL | VRYRARGSTG | KPLHLETRVR | PTQQGKLARN | ARFSKRLRNF | EVSTDFDQKE |
| 670 | 680 | 690 | 700 | 710 | 720 |
| QIARNFGKLL | GPQSDLLLSY | TLQANADSGA | ASHSYNLTLL | WIDPLGRLQD | FNELHVEDST |
| 730 | 740 | 750 | 760 | 770 | 780 |
| SDVINHSKTL | LKHPITPGIW | TAKLIGRNSI | YAQLKFLIAP | LAYYKGYPLA | KSSDAEALNA |
| 790 | 800 | 810 | 820 | 830 | 840 |
| GLTVALPEDF | EMPVEWQQHL | QTDDEQFTMR | EESLAKGKML | GQELHSWIDG | LVGQFFQLRE |
| 850 | 860 | 870 | |||
| SCVVEADSEV | SLPLCSDAPW | SSLAPDPKSD | VDALLK |