Q9VTK2
Gene name |
rt |
Protein name |
Protein O-mannosyltransferase 1 |
Names |
Dolichyl-phosphate-mannose--protein mannosyltransferase 1, dPOMT1, Protein rotated abdomen |
Species |
Drosophila melanogaster (Fruit fly) |
KEGG Pathway |
dme:Dmel_CG6097 |
EC number |
2.4.1.109: Hexosyltransferases |
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 Q9VTK2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9VTK2-F1 | Predicted | AlphaFoldDB |
No variants for Q9VTK2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9VTK2 | |||||
No associated diseases with Q9VTK2
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.1.109 | Hexosyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| dolichyl-phosphate-mannose-protein mannosyltransferase complex | A complex that possesses dolichyl-phosphate-mannose-protein mannosyltransferase activity; usually includes members of the PMT1 and PMT2 protein subfamilies. |
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| 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. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| dolichyl-phosphate-mannose-protein mannosyltransferase activity | Catalysis of the reaction: dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| muscle attachment | The developmental process in which a skeletal muscle attaches to its target (such as bone or body wall). |
| muscle organ development | The process whose specific outcome is the progression of the muscle over time, from its formation to the mature structure. The muscle is an organ consisting of a tissue made up of various elongated cells that are specialized to contract and thus to produce movement and mechanical work. |
| protein O-linked mannosylation | The transfer of mannose from dolichyl activated mannose to the hydroxyl group of a seryl or threonyl residue of a protein acceptor molecule, to form an O-linked protein-sugar linkage. |
| regulation of synaptic activity | Any process that modulates the frequency, rate or extent of synaptic activity, the controlled release of neurotransmitters into the synaptic cleft and their subsequent detection by a postsynaptic cell. |
| sarcomere organization | The myofibril assembly process that results in the organization of muscle actomyosin into sarcomeres. The sarcomere is the repeating unit of a myofibril in a muscle cell, composed of an array of overlapping thick and thin filaments between two adjacent Z discs. |
| somatic muscle development | The process whose specific outcome is the progression of the somatic muscle over time, from its formation to the mature structure. Somatic muscles are striated muscle structures that connect to the exoskeleton or cuticle. |
| specification of segmental identity, abdomen | The specification of the characteristic structures of the abdominal segments following establishment of segment boundaries. Identity is considered to be the aggregate of characteristics by which a structure is recognized. |
3 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P46971 | PMT4 | Dolichyl-phosphate-mannose--protein mannosyltransferase 4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| Q9UKY4 | POMT2 | Protein O-mannosyl-transferase 2 | Homo sapiens (Human) | PR |
| Q8BGQ4 | Pomt2 | Protein O-mannosyl-transferase 2 | Mus musculus (Mouse) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSATYTNTIT | QRRKTAKVRQ | QQQHQWTGSD | LSGESNERLH | FRSRSTNSMQ | QHTAISNSPS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PLCCNGARAL | TMLNCCVDVN | CHLNAPLRGS | VNRHTTPTPT | PTATPTPVAT | PKQASPSPTS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DRSRSLSRSP | SPSRSRSLSC | QKQIDKNSAG | AASAEERKTA | NASSQPFTVN | LRIDLFSWTL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FLLAFGTRFY | KLATPPHIVF | DELHYGKYIS | MYMRNIFFFD | QHPPLGKQLI | AGLVSLAGYD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GNYTFTRIGE | PYSPEMPIFW | FRFLPAMCGS | LLAPAVYNLL | LEAKLSRWSS | ALGGLLVVLD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NSLLTQSRFV | LMESMLLLAT | TVGIACLLRF | QRSRLGSLEW | FFTGTAAAVC | LGAAGTVKYV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GFLALGLAFY | LLCRHLWQLL | YDAGLTDRQL | WMHAISRLLI | FVGIPLAVYL | GVFYIHFKTL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| HRAGPHDSIM | TSAFQASLDG | GLASITKGQP | LAVVHGSQIT | LRHTHGRTCW | LHSHAAVYPV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| RYPDKRGSSH | QQQVTCYSFK | DVNNWWLVKR | PTKENLVVGD | EPDIIRHGEI | IQLVHGITSR |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ALNSHDVAAA | MTPQCQEVSC | YIDYEIKMAG | ELLWRVEILN | RDSEGDIWHA | IKSEVRLVHV |
| 610 | 620 | 630 | 640 | 650 | 660 |
| STEASLKFSG | RQLPEWGFNQ | HEVVADREKA | IHEDAIWNVE | EHRYTQTEDH | RERERQMLTA |
| 670 | 680 | 690 | 700 | 710 | 720 |
| EMIPTKRTRI | SFWAKLLELQ | SKMLFQTKSV | PNHMYSSMPH | EWPLMDKGIA | YWLDSQSSAQ |
| 730 | 740 | 750 | 760 | 770 | 780 |
| IYLLGNILLW | YTATMGILVY | AGLLAFYAMR | RQRLCFDISE | QEWQRFVLAG | DTFFMGYVMH |
| 790 | 800 | 810 | 820 | 830 | 840 |
| YIPYFCVDRT | LFLHNYLPAF | VFKLLLLCFV | VEHLDYLLRR | FCTGRGVHLV | RLYRLMLILW |
| 850 | 860 | 870 | 880 | ||
| LVGVLSIFSK | FIPFSYGARK | MTLNEVRSLR | WKDTWDFVLH | KNHHLY |