| IED ID | IndEnz0002002751 |
| Enzyme Type ID | protease002751 |
| Protein Name |
Alpha-adducin Erythrocyte adducin subunit alpha |
| Gene Name | ADD1 |
| Organism | Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Ponginae Pongo Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
| Enzyme Sequence | MNGDSRAAVVTSPPPTTAPHKERYFDRVDENNPEYLRERNMAPDLRQDFNMMEQKKRVSMILQSPAFCEELESMIQEQFKKGKNPTGLLALQQIADFMTTNVPNVYPAAPQGGMAALNMSLGMVTPVNDLRGSDSIAYDKGEKLLRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDRGSTNLGVNQAGFTLHSAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSLGEVAYHDYHGILVDEEEKVLIQKNLGPKSKVLILRNHGLVSVGESVEEAFYYIHNLVVACEIQARTLASAGGPDNLVLLNPEKYKAKSRSPGSPVGEGTGSPPKWQIGEQEFEALMRMLDNLGYRTGYPYRYPALREKSKKYSDVEVPASVTGYSFTSDGDSGTCSPLRHSFQKQQREKTRWLNSGRGDEASEEGQNGSSPKSKTKWTKEDGHRTSTSAVPNLFVPLNTNPKEVQEMRNKIREQNLQDIKTAGPQSQVLCGVVMDRSLVQGELVTASKAIIEKEYQPHVIVSTTGPNPFTTLTDRELEEYRREVERKQKGSEENLDEAREQKEKSPPDQPAVPYPPPSTPIKLEEDLVPEPTTGDDSDAATFKPTLPDLSPDEPSEALGFPMLEKEEEAHRPPSPTEAPTEASPEPAPDPAPVAEEAAPSAAEEGAAADPGSDGSPGKSPSKKKKKFRTPSFLKKSKKKSES |
| Enzyme Length | 737 |
| Uniprot Accession Number | Q5RA10 |
| 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. Binds to calmodulin (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (6); Modified residue (30); Region (4) |
| Keywords | Acetylation;Actin-binding;Calmodulin-binding;Cell membrane;Cytoplasm;Cytoskeleton;Membrane;Phosphoprotein;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side. |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 12; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 59; /note=Phosphoserine; by PKA; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 64; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 331; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 334; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 353; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 355; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 358; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 366; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 408; /note=Phosphoserine; by PKA; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 427; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYC0; MOD_RES 429; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q9QYC0; MOD_RES 431; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 436; /note=Phosphoserine; by PKA; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 445; /note=Phosphothreonine; by ROCK2; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 464; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYC0; MOD_RES 465; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 480; /note=Phosphothreonine; by ROCK2; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 481; /note=Phosphoserine; by PKA; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 586; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYC0; MOD_RES 600; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYC0; MOD_RES 613; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYC0; MOD_RES 614; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q9QYC0; MOD_RES 678; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 707; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 710; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 714; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 716; /note=Phosphoserine; by PKC; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 726; /note=Phosphoserine; by PKA and PKC; /evidence=ECO:0000250|UniProtKB:P35611 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 80,969 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |