O54824 · IL16_MOUSE
- ProteinPro-interleukin-16
- GeneIl16
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1322 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Interleukin-16 stimulates a migratory response in CD4+ lymphocytes, monocytes, and eosinophils. Primes CD4+ T-cells for IL-2 and IL-15 responsiveness. Also induces T-lymphocyte expression of interleukin 2 receptor. Ligand for CD4.
Isoform 1 may act as a scaffolding protein that anchors ion channels in the membrane.
Isoform 2 is involved in cell cycle progression in T-cells. Appears to be involved in transcriptional regulation of SKP2 and is probably part of a transcriptional repression complex on the core promoter of the SKP2 gene. May act as a scaffold for GABPB1 (the DNA-binding subunit the GABP transcription factor complex) and HDAC3 thus maintaining transcriptional repression and blocking cell cycle progression in resting T-cells.
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 | collagen-containing extracellular matrix | |
Cellular Component | cytosol | |
Cellular Component | extracellular space | |
Cellular Component | Flemming body | |
Cellular Component | focal adhesion | |
Cellular Component | nuclear speck | |
Cellular Component | plasma membrane | |
Molecular Function | CD4 receptor binding | |
Molecular Function | cytokine activity | |
Biological Process | induction of positive chemotaxis | |
Biological Process | leukocyte chemotaxis | |
Biological Process | positive regulation of inflammatory response | |
Biological Process | positive regulation of interleukin-1 alpha production | |
Biological Process | positive regulation of interleukin-12 production | |
Biological Process | positive regulation of interleukin-6 production | |
Biological Process | regulation of calcium ion transport |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePro-interleukin-16
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionO54824
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000377546 | 1-1322 | Pro-interleukin-16 | |||
Sequence: MEPHGHSGKSRKSTKFRSISRSLILCNAKTSDDGSSPDEKYPDPFETSLCQGKEGFFHSSMQLADTFEAGLSNIPDLALASDSAQLAAAGSDRGKHCRKMFFMKESSSTSSKEKSGKPEAQSSSFLFPKACHQRTRSNSTSVNPYSAGEIDFPMTKKSAAPTDRQPYSLCSNRKSLSQQLDYPILGTARPTRSLSTAQLGQLSGGLQASVISNIVLMKGQAKGLGFSIVGGKDSIYGPIGIYVKSIFAGGAAAADGRLQEGDEILELNGESMAGLTHQDALQKFKQAKKGLLTLTVRTRLTTPPSLCSHLSPPLCRSLSSSTCGAQDSSPFSLESPASPASTAKPNYRIMVEVSLKKEAGVGLGIGLCSIPYFQCISGIFVHTLSPGSVAHLDGRLRCGDEIVEINDSPVHCLTLNEVYTILSHCDPGPVPIIVSRHPDPQVSEQQLKEAVAQAVEGVKFGKDRHQWSLEGVKRLESSWHGRPTLEKEREKHSAPPHRRAQKIMVRSSSDSSYMSGSPGGSPCSAGAEPQPSEREGSTHSPSLSPGEEQEPCPGVPSRPQQESPPLPESLERESHPPLRLKKSFEILVRKPTSSKPKPPPRKYFKNDSEPQKKLEEKEKVTDPSGHTLPTCSQETRELLPLLLQEDTAGRAPCTAACCPGPAASTQTSSSTEGESRRSASPETPASPGKHPLLKRQARMDYSFDITAEDPWVRISDCIKNLFSPIMSENHSHTPLQPNTSLGEEDGTQGCPEGGLSKMDAANGAPRVYKSADGSTVKKGPPVAPKPAWFRQSLKGLRNRAPDPRRPPEVASAIQPTPVSRDPPGPQPQASSSIRQRISSFENFGSSQLPDRGVQRLSLQPSSGETTKFPGKQDGGRFSGLLGQGATVTAKHRQTEVESMSTTFPNSSEVRDPGLPESPPPGQRPSTKALSPDPLLRLLTTQSEDTQGPGLKMPSQRARSFPLTRTQSCETKLLDEKASKLYSISSQLSSAVMKSLLCLPSSVSCGQITCIPKERVSPKSPCNNSSAAEGFGEAMASDTGFSLNLSELREYSEGLTEPGETEDRNHCSSQAGQSVISLLSAEELEKLIEEVRVLDEATLKQLDSIHVTILHKEEGAGLGFSLAGGADLENKVITVHRVFPNGLASQEGTIQKGNEVLSINGKSLKGATHNDALAILRQARDPRQAVIVTRRTTVEATHDLNSSTDSAASASAASDISVESKEATVCTVTLEKTSAGLGFSLEGGKGSLHGDKPLTINRIFKGTEQGEMVQPGDEILQLAGTAVQGLTRFEAWNVIKALPDGPVTIVIRRTSLQCKQTTASADS | ||||||
Modified residue | 917 | Phosphoserine | ||||
Sequence: S | ||||||
Chain | PRO_0000015418 | 1205-1322 | Interleukin-16 | |||
Sequence: SAASASAASDISVESKEATVCTVTLEKTSAGLGFSLEGGKGSLHGDKPLTINRIFKGTEQGEMVQPGDEILQLAGTAVQGLTRFEAWNVIKALPDGPVTIVIRRTSLQCKQTTASADS |
Post-translational modification
Synthesized as a chemo-attractant inactive precursor which is proteolytically cleaved by caspase-3 to yield IL-16.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homotetramer (Probable). Isoform 2 interacts with GRIN2A. Isoform 1 interacts with GRIN2D, KCNJ10, KCNJ15 and CACNA1C. Isoform 2 interacts (via PDZ 3 domain) with PPP1R12A, PPP1R12B and PPP1R12C. Isoform 1 interacts with PPP1R12B. Isoform 3 interacts with GABPB1. Isoform 2 interacts (via PDZ 3 domain) with HDAC3 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O54824 | Itpkc Q7TS72 | 3 | EBI-641708, EBI-648015 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 104-146 | Polar residues | ||||
Sequence: KESSSTSSKEKSGKPEAQSSSFLFPKACHQRTRSNSTSVNPYS | ||||||
Region | 104-147 | Disordered | ||||
Sequence: KESSSTSSKEKSGKPEAQSSSFLFPKACHQRTRSNSTSVNPYSA | ||||||
Region | 183-449 | Interaction with GRIN2A | ||||
Sequence: PILGTARPTRSLSTAQLGQLSGGLQASVISNIVLMKGQAKGLGFSIVGGKDSIYGPIGIYVKSIFAGGAAAADGRLQEGDEILELNGESMAGLTHQDALQKFKQAKKGLLTLTVRTRLTTPPSLCSHLSPPLCRSLSSSTCGAQDSSPFSLESPASPASTAKPNYRIMVEVSLKKEAGVGLGIGLCSIPYFQCISGIFVHTLSPGSVAHLDGRLRCGDEIVEINDSPVHCLTLNEVYTILSHCDPGPVPIIVSRHPDPQVSEQQLKE | ||||||
Domain | 213-299 | PDZ 1 | ||||
Sequence: NIVLMKGQAKGLGFSIVGGKDSIYGPIGIYVKSIFAGGAAAADGRLQEGDEILELNGESMAGLTHQDALQKFKQAKKGLLTLTVRTR | ||||||
Domain | 352-437 | PDZ 2 | ||||
Sequence: EVSLKKEAGVGLGIGLCSIPYFQCISGIFVHTLSPGSVAHLDGRLRCGDEIVEINDSPVHCLTLNEVYTILSHCDPGPVPIIVSRH | ||||||
Compositional bias | 480-497 | Basic and acidic residues | ||||
Sequence: HGRPTLEKEREKHSAPPH | ||||||
Region | 480-633 | Disordered | ||||
Sequence: HGRPTLEKEREKHSAPPHRRAQKIMVRSSSDSSYMSGSPGGSPCSAGAEPQPSEREGSTHSPSLSPGEEQEPCPGVPSRPQQESPPLPESLERESHPPLRLKKSFEILVRKPTSSKPKPPPRKYFKNDSEPQKKLEEKEKVTDPSGHTLPTCSQ | ||||||
Compositional bias | 505-519 | Polar residues | ||||
Sequence: VRSSSDSSYMSGSPG | ||||||
Compositional bias | 531-545 | Polar residues | ||||
Sequence: PSEREGSTHSPSLSP | ||||||
Compositional bias | 568-588 | Basic and acidic residues | ||||
Sequence: ESLERESHPPLRLKKSFEILV | ||||||
Compositional bias | 600-623 | Basic and acidic residues | ||||
Sequence: PRKYFKNDSEPQKKLEEKEKVTDP | ||||||
Region | 651-695 | Disordered | ||||
Sequence: APCTAACCPGPAASTQTSSSTEGESRRSASPETPASPGKHPLLKR | ||||||
Compositional bias | 660-682 | Polar residues | ||||
Sequence: GPAASTQTSSSTEGESRRSASPE | ||||||
Compositional bias | 729-745 | Polar residues | ||||
Sequence: NHSHTPLQPNTSLGEED | ||||||
Region | 729-963 | Disordered | ||||
Sequence: NHSHTPLQPNTSLGEEDGTQGCPEGGLSKMDAANGAPRVYKSADGSTVKKGPPVAPKPAWFRQSLKGLRNRAPDPRRPPEVASAIQPTPVSRDPPGPQPQASSSIRQRISSFENFGSSQLPDRGVQRLSLQPSSGETTKFPGKQDGGRFSGLLGQGATVTAKHRQTEVESMSTTFPNSSEVRDPGLPESPPPGQRPSTKALSPDPLLRLLTTQSEDTQGPGLKMPSQRARSFPLT | ||||||
Compositional bias | 825-868 | Polar residues | ||||
Sequence: PQPQASSSIRQRISSFENFGSSQLPDRGVQRLSLQPSSGETTKF | ||||||
Compositional bias | 887-908 | Polar residues | ||||
Sequence: VTAKHRQTEVESMSTTFPNSSE | ||||||
Compositional bias | 935-949 | Polar residues | ||||
Sequence: LRLLTTQSEDTQGPG | ||||||
Region | 1099-1195 | Interaction with PPP1R12A, PPP1R12B and PPP1R12C | ||||
Sequence: KQLDSIHVTILHKEEGAGLGFSLAGGADLENKVITVHRVFPNGLASQEGTIQKGNEVLSINGKSLKGATHNDALAILRQARDPRQAVIVTRRTTVEA | ||||||
Domain | 1105-1190 | PDZ 3 | ||||
Sequence: HVTILHKEEGAGLGFSLAGGADLENKVITVHRVFPNGLASQEGTIQKGNEVLSINGKSLKGATHNDALAILRQARDPRQAVIVTRR | ||||||
Domain | 1226-1309 | PDZ 4 | ||||
Sequence: TVTLEKTSAGLGFSLEGGKGSLHGDKPLTINRIFKGTEQGEMVQPGDEILQLAGTAVQGLTRFEAWNVIKALPDGPVTIVIRRT |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative promoter usage.
O54824-1
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
- SynonymsNIL-16
- NoteProduced by alternative promoter usage. Is probably proteolytically processed to yield IL-16.
- Length1,322
- Mass (Da)141,435
- Last updated2009-06-16 v3
- ChecksumDDB94003A5DCB738
O54824-2
- Name2
- SynonymsPro-IL-16
- NoteProduced by alternative promoter usage. Is proteolytically processed to yield IL-16.
- Differences from canonical
- 1-698: Missing
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_037460 | 1-698 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 104-146 | Polar residues | ||||
Sequence: KESSSTSSKEKSGKPEAQSSSFLFPKACHQRTRSNSTSVNPYS | ||||||
Sequence conflict | 264 | in Ref. 5; BAD90484 | ||||
Sequence: I → S | ||||||
Compositional bias | 480-497 | Basic and acidic residues | ||||
Sequence: HGRPTLEKEREKHSAPPH | ||||||
Compositional bias | 505-519 | Polar residues | ||||
Sequence: VRSSSDSSYMSGSPG | ||||||
Compositional bias | 531-545 | Polar residues | ||||
Sequence: PSEREGSTHSPSLSP | ||||||
Compositional bias | 568-588 | Basic and acidic residues | ||||
Sequence: ESLERESHPPLRLKKSFEILV | ||||||
Compositional bias | 600-623 | Basic and acidic residues | ||||
Sequence: PRKYFKNDSEPQKKLEEKEKVTDP | ||||||
Compositional bias | 660-682 | Polar residues | ||||
Sequence: GPAASTQTSSSTEGESRRSASPE | ||||||
Compositional bias | 729-745 | Polar residues | ||||
Sequence: NHSHTPLQPNTSLGEED | ||||||
Sequence conflict | 733 | in Ref. 1; AAC04383 | ||||
Sequence: T → R | ||||||
Compositional bias | 825-868 | Polar residues | ||||
Sequence: PQPQASSSIRQRISSFENFGSSQLPDRGVQRLSLQPSSGETTKF | ||||||
Compositional bias | 887-908 | Polar residues | ||||
Sequence: VTAKHRQTEVESMSTTFPNSSE | ||||||
Sequence conflict | 921 | in Ref. 2; AAC16039 | ||||
Sequence: G → S | ||||||
Compositional bias | 935-949 | Polar residues | ||||
Sequence: LRLLTTQSEDTQGPG | ||||||
Sequence conflict | 1067 | in Ref. 2; AAC16039 | ||||
Sequence: S → P | ||||||
Sequence conflict | 1224 | in Ref. 2; AAC16039 | ||||
Sequence: V → A | ||||||
Sequence conflict | 1262-1264 | in Ref. 1; AAC04383 | ||||
Sequence: TEQ → DRT |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF006001 EMBL· GenBank· DDBJ | AAC04383.1 EMBL· GenBank· DDBJ | mRNA | ||
AF017111 EMBL· GenBank· DDBJ | AAC16039.1 EMBL· GenBank· DDBJ | mRNA | ||
AF175292 EMBL· GenBank· DDBJ | AAD55393.1 EMBL· GenBank· DDBJ | mRNA | ||
AK038319 EMBL· GenBank· DDBJ | BAC29967.1 EMBL· GenBank· DDBJ | mRNA | ||
AK169551 EMBL· GenBank· DDBJ | BAE41224.1 EMBL· GenBank· DDBJ | mRNA | ||
AK220455 EMBL· GenBank· DDBJ | BAD90484.1 EMBL· GenBank· DDBJ | mRNA | ||
CH466543 EMBL· GenBank· DDBJ | EDL06877.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC026894 EMBL· GenBank· DDBJ | AAH26894.1 EMBL· GenBank· DDBJ | mRNA | ||
BC058709 EMBL· GenBank· DDBJ | AAH58709.1 EMBL· GenBank· DDBJ | mRNA |