Detail Information for IndEnz0002016629
IED ID IndEnz0002016629
Enzyme Type ID protease016629
Protein Name Gamma-adducin
Adducin-like protein 70
Protein kinase C-binding protein 35H
Gene Name Add3
Organism Rattus norvegicus (Rat)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat)
Enzyme Sequence MSSDSSQAVITTPPPPSMPHKERYFDRINESDPEYLRERNMSPDLREDFNMMEQRKRVTQILQSPAFREDLECLTQEQMKKGHDPTGLLALQQIADYIMANSFTGFSSPPLSLGMVTPINDLPGADTSSYVKGEKLTRCELASLYRLADLFGWAHLANTYISVRVSKEQDHIIIIPRGLPFSEATASALVKVNIIGEVVDQGSTNLKIDHSGFSPHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLILGDVAYYDYQGSLDEEEERIELQKVLGPSCKVLVLRNHGVVALGETLEEAFHYIFNVQMACEIQVQAVAGAGGVDNLLILDLQKYKAFTHGVAMTGGGGVNMGSHQKWKVGEIEFEGLMRTLDNLGYRTGYAYRHPLVREKPRHKSDVEIPATVTAFSFEDDSVPLSPLKYMAQRQQREKTRWLNSPNTYMKVNVPEESRNGETSPRTKITWMKAEDPSKVSSGTPIKIEDPNQFVPLNTNPTEVLEKRNKIREQNRYDLKTAGPQSQLLAGIVVDKPPSTMRFEDDDQGPPAPPNPFSHLMEGELEEYTKTIERQQQGLDDAEQESLSDDAASVSQIQSQTQSPQSVPERLEENHELFSKSFTSVDVPVIVNGKDEMHDVEDELAQRVSRLTTSTTIENIEITIKSPDRTEEVLSPDGSPSKSPSKKKKKFRTPSFLKKNKKKEKVEA
Enzyme Length 705
Uniprot Accession Number Q62847
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Plays a role in actin filament capping. Binds to calmodulin. {ECO:0000250|UniProtKB:Q9UEY8}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (1); Chain (1); Compositional bias (2); Cross-link (1); Initiator methionine (1); Modified residue (17); Natural variant (1); Region (6); Sequence conflict (1)
Keywords Acetylation;Actin-binding;Alternative splicing;Calmodulin-binding;Cell membrane;Cytoplasm;Cytoskeleton;Isopeptide bond;Membrane;Phosphoprotein;Reference proteome;Ubl conjugation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Modified Residue MOD_RES 2; /note=N-acetylserine; /evidence=ECO:0000250|UniProtKB:Q9UEY8; MOD_RES 31; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYB5; MOD_RES 42; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9UEY8; MOD_RES 64; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9UEY8; MOD_RES 402; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9UEY8; MOD_RES 414; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYB5; MOD_RES 423; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 442; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9UEY8; MOD_RES 461; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9UEY8; MOD_RES 583; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 585; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 590; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYB5; MOD_RES 672; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 676; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 678; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYB5; MOD_RES 680; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 682; /note=Phosphoserine; by PKC; /evidence=ECO:0000250|UniProtKB:Q9UEY8
Post Translational Modification PTM: Sumoylated. {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10823823; 12364392; 15329129; 27927653; 32029431; 33308016; 33414130; 8442667; 9607561;
Motif
Gene Encoded By
Mass 78,804
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda