Q04623
Gene name |
ECM18 (YDR125C, YD9727.20C) |
Protein name |
Protein ECM18 |
Names |
Extracellular mutant protein 18 |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YDR125C |
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 Q04623
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q04623-F1 | Predicted | AlphaFoldDB |
7 variants for Q04623
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s04-702703 | 18 | I>T | No | SGRP | |
| s04-702275 | 161 | M>L | No | SGRP | |
| s04-702244 | 171 | S>F | No | SGRP | |
| s04-702179 | 193 | K>E | No | SGRP | |
| s04-701707 | 350 | G>E | No | SGRP | |
| s04-701671 | 362 | A>G | No | SGRP | |
| s04-701666 | 364 | F>L | No | SGRP |
No associated diseases with Q04623
1 regional properties for Q04623
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Alpha/beta hydrolase fold-1 | 130 - 270 | IPR000073 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| mitochondrial inner membrane | The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| carboxylic ester hydrolase activity | Catalysis of the hydrolysis of a carboxylic ester bond. |
| lysophosphatidic acid acyltransferase activity | Catalysis of the transfer of acyl groups from an acyl-CoA to lysophosphatidic acid to form phosphatidic acid. |
| phospholipase A2 activity | Catalysis of the reaction: a 1,2-diacyl-sn-glycero-3-phospholipid + H2O = 1-acyl-sn-glycero-3-phospholipid + a fatty acid. This reaction removes the fatty acid attached to the sn2-position. Substrates include phosphatidylcholine, phosphatidylethanolamine, choline plasmalogen and phosphatides. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| cardiolipin acyl-chain remodeling | Remodeling the acyl chains of premature (de novo synthesized) cardiolipin (1,3-bis(3-phosphatidyl)glycerol), through sequential deacylation and re-acylation reactions, to generate mature cardiolipin containing high-levels of unsaturated fatty acids. |
| cell wall organization | A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis. |
| lipid homeostasis | Any process involved in the maintenance of an internal steady state of lipid within an organism or cell. |
| phosphatidic acid biosynthetic process | The chemical reactions and pathways resulting in the formation of phosphatidic acid, any derivative of glycerol phosphate in which both the remaining hydroxyl groups of the glycerol moiety are esterified with fatty acids. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P53264 | CLD1 | Cardiolipin-specific deacylase 1, mitochondrial | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLLIKRYLMD | PESLRRQIMN | VYKCYMWKRA | FHSNRSLLEV | KRREKSLQRK | ILERILRPKE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ENAVKKSGFK | LWSSHLNNPH | KTYMRLEELQ | RRIMEEVHVE | GIKKNDKLFN | EINQWHFQNE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NTSTVRTPTL | LIHGYAASSM | SFFRNYPGLS | KHIRNLYSID | MPASGLSSVP | SLEINTTTPL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PLDIKFIGEN | KFKVPYTINA | NHNKFVIQMY | EDFYLDRIEQ | WRIDNKLGKM | NVVGHSFGGY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LSFKYAVKYP | NSVNKLCLVS | PLGVERNIWS | VNNNFHSNTL | YTIDFKNPNS | KFYSKRNMIP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KYLFEQQFHI | LRMMGPLGAK | LCWNYIMAAY | SRVPSLAYKE | YIFELFYGKG | GIPEVTTDIF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KALFSRCILA | KDPLMDSLQY | LNVKKLLIVY | GQYDWMNKKA | GMFMVKELNN | LKNCLEGASY |
| 430 | 440 | 450 | |||
| LEIPSSGHNL | FLDNPESFNQ | SIVSFLSDET | KSP |