Q3KR97 · BI2L1_RAT
- ProteinBAR/IMD domain-containing adapter protein 2-like 1
- GeneBaiap2l1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids516 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
May function as adapter protein. Involved in the formation of clusters of actin bundles. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | actin cytoskeleton | |
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Molecular Function | actin binding | |
Molecular Function | proline-rich region binding | |
Biological Process | actin crosslink formation | |
Biological Process | actin filament bundle assembly | |
Biological Process | plasma membrane organization | |
Biological Process | positive regulation of actin filament polymerization | |
Biological Process | regulation of actin cytoskeleton organization |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBAR/IMD domain-containing adapter protein 2-like 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ3KR97
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Recruited to actin pedestals that are formed upon infection by bacteria at bacterial attachment sites.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000247856 | 1-516 | BAR/IMD domain-containing adapter protein 2-like 1 | |||
Sequence: MSRGPEEVNRLTENTYRNVVEQFNPGLRNLINLGKNYEKAVNAMILAGKAYYDGVAKIGEIATGSPVSTELGHVLIEISSTHKKLNETLDENFKKFHKEIIHELEKKTELDVKYMNATLKRYQAEHRNKLDSLEKSQAELKKIRRKSQGGRNALKYEHKEIEYVETVTSRQSEIQKFIADGCKEALLEEKRRFCFLVDKHCSFASHIHRYHLQSAELLNSKLPRWQETCCDATKVPEKIMNMIEEIKTPISTPVSGTPQPSPMTERSKMIGKDYDTLSKYSPKMPPAPSVKAYTSPLIDMFNNPATAGQSAEKTNNSTANTGDDPSLQRSVSVATGLNMMKKQKVKTIFPHTAGNNKTLLSFAQGDVLTLLIPEEKDGWLYGEHDTTKVRGWFPSSYTKLLEENMKEAMSVPTPSSAPVRSISTVDLTEKSSVVIPPPDYLECLSMGATSDKRADAAKIPSTSTFKAPVPRPDATSTSPSDSNGTAKPPFLSGENPFATVKLRPTVTNDRSAPIIR | ||||||
Modified residue | 248 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 257 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 261 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 281 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 332 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 413 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 415 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 421 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 423 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated on tyrosine in response to insulin.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, coiled coil, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-249 | IMD | ||||
Sequence: MSRGPEEVNRLTENTYRNVVEQFNPGLRNLINLGKNYEKAVNAMILAGKAYYDGVAKIGEIATGSPVSTELGHVLIEISSTHKKLNETLDENFKKFHKEIIHELEKKTELDVKYMNATLKRYQAEHRNKLDSLEKSQAELKKIRRKSQGGRNALKYEHKEIEYVETVTSRQSEIQKFIADGCKEALLEEKRRFCFLVDKHCSFASHIHRYHLQSAELLNSKLPRWQETCCDATKVPEKIMNMIEEIKTP | ||||||
Coiled coil | 115-148 | |||||
Sequence: MNATLKRYQAEHRNKLDSLEKSQAELKKIRRKSQ | ||||||
Region | 303-328 | Disordered | ||||
Sequence: NPATAGQSAEKTNNSTANTGDDPSLQ | ||||||
Domain | 340-403 | SH3 | ||||
Sequence: MKKQKVKTIFPHTAGNNKTLLSFAQGDVLTLLIPEEKDGWLYGEHDTTKVRGWFPSSYTKLLEE | ||||||
Region | 454-516 | Disordered | ||||
Sequence: ADAAKIPSTSTFKAPVPRPDATSTSPSDSNGTAKPPFLSGENPFATVKLRPTVTNDRSAPIIR | ||||||
Compositional bias | 468-489 | Polar residues | ||||
Sequence: PVPRPDATSTSPSDSNGTAKPP | ||||||
Region | 488-516 | Binds F-actin | ||||
Sequence: PPFLSGENPFATVKLRPTVTNDRSAPIIR |
Domain
The IMD domain is predicted to have a helical structure. It may induce actin bundling and filopodia formation (By similarity).
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q3KR97-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length516
- Mass (Da)57,468
- Last updated2005-11-08 v1
- Checksum97ED6E2199E853EB
Q3KR97-2
- Name2
- Differences from canonical
- 1-43: Missing
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8L2RB03 | A0A8L2RB03_RAT | Baiap2l1 | 504 | ||
A0A8L2QTC2 | A0A8L2QTC2_RAT | Baiap2l1 | 518 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_020077 | 1-43 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 468-489 | Polar residues | ||||
Sequence: PVPRPDATSTSPSDSNGTAKPP |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC089216 EMBL· GenBank· DDBJ | AAH89216.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC105815 EMBL· GenBank· DDBJ | AAI05816.1 EMBL· GenBank· DDBJ | mRNA |