| IED ID | IndEnz0002016380 |
| Enzyme Type ID | protease016380 |
| Protein Name |
Alpha-adducin Erythrocyte adducin subunit alpha |
| Gene Name | Add1 |
| 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 | MNGDTRAAVVTSPPPTTAPHKERYFDRVDENNPEYLRERNMAPDLRQDFNMMEQKKRVSMILQSPAFCEELESMIQEQFKKGKNPTGLLALQQIADFMTASVPNVYPAAPQGGMAALNMSLGMVTPVNDLRGSDSIAYDKGEKLLRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKVNLQGDIVDRGSTNLGVNQAGFTLHSAIYAARPDAKCIVHIHTPAGAAVSAMKCGLLPISPEALSLGEVAYHDYHGILVDEEEKILIQKNLGPKSKVLILRNHGLVSVGESVEEAFYYIHNLVVACEIQVRTLASAGGPDNLVLLDPGKYKAKSRSPGTPAGEGSGSPPKWQIGEQEFEALMRMLDNLGYRTGYPYRYPALRERSKKYSDVEVPASVTGHSFASDGDSGTCSPLRHSFQKQQREKTRWLNSGRGDDASEEGQNGSSPKSKTKWTKEDGHRTSTSAVPNLFVPLNTNPKEVQEMRNKIREQNLQDIKTAGPQSQVLCGVMMDRSLVQGELVTASKAIIEKEYQPHVIVSTTGPNPFNTLTDRELEEYRREVERKQKGSEENLDETREQKEKSPPDQSAVPNTPPSTPVKLEGGLPQEPTSRDGSDATTSKPTPPDLSPDEPSEALAFPTVAEEAHASPDTTQPLAEADPEPASASAPGAEEVASPATEEGSPMDPGSDGSPGKSPSKKKKKFRTPSFLKKSKKKSDS |
| Enzyme Length | 735 |
| Uniprot Accession Number | Q63028 |
| 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. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Chain (1); Compositional bias (3); Modified residue (32); Natural variant (1); Region (4); Sequence conflict (2) |
| Keywords | Acetylation;Actin-binding;Alternative splicing;Calmodulin-binding;Cell membrane;Cytoplasm;Cytoskeleton;Membrane;Phosphoprotein;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 12; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; 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:0007744|PubMed:22673903; MOD_RES 358; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 364; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYC0; MOD_RES 366; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; 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:0007744|PubMed:22673903; 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:0007744|PubMed:22673903; MOD_RES 600; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 605; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYC0; MOD_RES 610; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 613; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYC0; MOD_RES 614; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 705; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 708; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 712; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 714; /note=Phosphoserine; by PKC; /evidence=ECO:0000250|UniProtKB:P35611; MOD_RES 724; /note=Phosphoserine; by PKA and PKC; /evidence=ECO:0000250|UniProtKB:P35611 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11226670; 15163540; 15474463; 17512505; 18524856; 20493242; 7592723; 8675693; 9607561; |
| Motif | |
| Gene Encoded By | |
| Mass | 80,355 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |