| Gene ID | Annotation | Scaffold | Start | End | Strand |
|---|---|---|---|---|---|
| Bpl_scaf_60708-1.10 | HRAS-LIKE SUPPRESSOR - RELATED | Bpl_scaf_60708 | 173821 | 184335 | + |
| CDS | |||||
| Bpl_scaf_60708-1.10 | |||||
| Transcript |
| Bpl_scaf_60708-1.10 |
| Protein |
| Bpl_scaf_60708-1.10 |
| Gene family | Subfamily |
|---|---|
| - | - |
| Pfam accession | Pfam name | Description | Type | Source |
|---|---|---|---|---|
| PF04970 | LRAT | Lecithin retinol acyltransferase | Domain | Interproscan |
| InterPro term | Type | Description | Source |
|---|---|---|---|
| IPR007053 | Domain | LRAT domain | Interproscan |
| IPR038765 | Homologous_superfamily | Papain-like cysteine peptidase superfamily | Interproscan |
| IPR051496 | Family | H-rev107 Phospholipase/Acyltransferase | Interproscan |
| PANTHER term | Description | Source |
|---|---|---|
| PTHR13943 | HRAS-LIKE SUPPRESSOR - RELATED | Interproscan |
| GO terms | Category | Description | Source |
|---|---|---|---|
| GO:0004623 | Molecular Function | phospholipase A2 activity | Interproscan |
| GO:0005737 | Cellular Component | cytoplasm | Interproscan |
| GO:0008970 | Molecular Function | phospholipase A1 activity | Interproscan |
| GO:0016410 | Molecular Function | N-acyltransferase activity | Interproscan |
| GO:0070292 | Biological Process | N-acylphosphatidylethanolamine metabolic process | Interproscan |
| KO | Enzyme | Enzyme ID | pathway | mapID | Source |
|---|---|---|---|---|---|
| K16817 | PLA2G16; HRAS-like suppressor 3 | EC:3.1.1.32 EC:3.1.1.4 | Glycerophospholipid metabolism | ko00564 | PMID: 28812709 |
| Ether lipid metabolism | ko00565 | PMID: 28812709 | |||
| Arachidonic acid metabolism | ko00590 | PMID: 28812709 | |||
| Linoleic acid metabolism | ko00591 | PMID: 28812709 | |||
| alpha-Linolenic acid metabolism | ko00592 | PMID: 28812709 | |||
| Ras signaling pathway | ko04014 | PMID: 28812709 | |||
| Regulation of lipolysis in adipocyte | ko04923 | PMID: 28812709 |
| 1. Expression trend for Bpl_scaf_60708-1.10 global RNA-seq network |
Maintained by Dr. Jiajie She in Longjun Wu's Lab & Pei-yuan Qian's Lab and supported by Southern Marine Science and Engineering Guangdong Laboratory (Guangzhou) & The Hong Kong University of Science and Technology
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