Q3MHZ7
Gene name |
PIGK |
Protein name |
GPI-anchor transamidase |
Names |
GPI transamidase, Phosphatidylinositol-glycan biosynthesis class K protein, PIG-K |
Species |
Bos taurus (Bovine) |
KEGG Pathway |
bta:508700 |
EC number |
|
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 Q3MHZ7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q3MHZ7-F1 | Predicted | AlphaFoldDB |
29 variants for Q3MHZ7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs379960599 | 4 | T>I | No | EVA | |
| rs718006499 | 6 | F>L | No | EVA | |
| rs383719733 | 9 | R>P | No | EVA | |
| rs383719733 | 9 | R>Q | No | EVA | |
| rs3423649933 | 60 | R>Q | No | EVA | |
| rs448274254 | 127 | T>N | No | EVA | |
| rs468273355 | 129 | E>D | No | EVA | |
| rs433262106 | 156 | N>H | No | EVA | |
| rs453381390 | 157 | I>L | No | EVA | |
| rs451347431 | 190 | M>I | No | EVA | |
| rs476395298 | 235 | H>N | No | EVA | |
| rs438551519 | 236 | Q>H | No | EVA | |
| rs441206758 | 255 | E>A | No | EVA | |
| rs461176638 | 269 | N>K | No | EVA | |
| rs481795075 | 270 | D>Y | No | EVA | |
| rs133339335 | 277 | R>K | No | EVA | |
| rs439221456 | 331 | K>* | No | EVA | |
| rs439221456 | 331 | K>E | No | EVA | |
| rs439221456 | 331 | K>Q | No | EVA | |
| rs459256846 | 331 | K>R | No | EVA | |
| rs459256846 | 331 | K>T | No | EVA | |
| rs473377278 | 332 | K>I | No | EVA | |
| rs441882724 | 332 | K>N | No | EVA | |
| rs461998184 | 333 | D>Y | No | EVA | |
| rs482017058 | 337 | E>Q | No | EVA | |
| rs450688314 | 341 | E>* | No | EVA | |
| rs478333620 | 353 | Q>* | No | EVA | |
| rs446888976 | 355 | I>V | No | EVA | |
| rs1115615710 | 357 | Q>K | No | EVA |
No associated diseases with Q3MHZ7
No regional properties for Q3MHZ7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q3MHZ7 | |||
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| GPI-anchor transamidase complex | An enzyme complex which in humans and yeast consists of at least five proteins; for example, the complex contains GAA1, GPI8, PIG-S, PIG-U, and PIG-T in human, and Gaa1p, Gab1p, Gpi8p, Gpi16p, and Gpi17p in yeast. Catalyzes the posttranslational attachment of the carboxy-terminus of a precursor protein to a GPI-anchor. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| GPI-anchor transamidase activity | Catalysis of the formation of the linkage between a protein and a glycosylphosphatidylinositol anchor. The reaction probably occurs by subjecting a peptide bond to nucleophilic attack by the amino group of ethanolamine-GPI, transferring the protein from a signal peptide to the GPI anchor. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| attachment of GPI anchor to protein | A transamidation reaction that results in the cleavage of the polypeptide chain and the concomitant transfer of the GPI anchor to the newly formed carboxy-terminal amino acid of the anchored protein. The cleaved C-terminal contains the C-terminal GPI signal sequence of the newly synthesized polypeptide chain. |
| protein localization to cell surface | A process in which a protein is transported to, or maintained in, a location within the external part of the cell wall and/or plasma membrane. |
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVDTCFLSRG | LTTLAGLLLL | PFGSLAASQI | EDQAEQFFRS | GHTNNWAVLV | CTSRFWFNYR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| HVANTLSVYR | SVKRLGIPDS | HIVLMLADDM | ACNPRNPKPA | TVYSHKNMEL | NVYGDDVEVD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| YRSYEVTVEN | FLRVLTGRIP | SSTPRSKRLL | SDDRSNILIY | MTGHGGNGFL | KFQDSEEITN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IELADAFEQM | WQKRRYNELL | FIIDTCQGAS | MYERFYSPNI | MALASSQVGE | DSLSHQPDPA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VGVHLMDRYT | FYVLEFLEEI | NPASQTNMND | LFQVCPRSLC | VSTPGHRTDL | FQRDPKNVLI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TDFFGSVRKV | EITTETISLQ | PDSGVVESSY | KKDQMVEELM | EPLKYAEQLP | VAQIIHQKPK |
| 370 | 380 | 390 | |||
| LKDWHPPGGF | ILGLWALIIM | VFFKTYGIKH | MKFIF |