| IED ID | IndEnz0002003722 |
| Enzyme Type ID | protease003722 |
| Protein Name |
Importin subunit alpha-5 Karyopherin subunit alpha-1 Nucleoprotein interactor 1 NPI-1 RAG cohort protein 2 SRP1-beta Cleaved into: Importin subunit alpha-5, N-terminally processed |
| Gene Name | KPNA1 RCH2 |
| Organism | Homo sapiens (Human) |
| 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) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MTTPGKENFRLKSYKNKSLNPDEMRRRREEEGLQLRKQKREEQLFKRRNVATAEEETEEEVMSDGGFHEAQISNMEMAPGGVITSDMIEMIFSKSPEQQLSATQKFRKLLSKEPNPPIDEVISTPGVVARFVEFLKRKENCTLQFESAWVLTNIASGNSLQTRIVIQAGAVPIFIELLSSEFEDVQEQAVWALGNIAGDSTMCRDYVLDCNILPPLLQLFSKQNRLTMTRNAVWALSNLCRGKSPPPEFAKVSPCLNVLSWLLFVSDTDVLADACWALSYLSDGPNDKIQAVIDAGVCRRLVELLMHNDYKVVSPALRAVGNIVTGDDIQTQVILNCSALQSLLHLLSSPKESIKKEACWTISNITAGNRAQIQTVIDANIFPALISILQTAEFRTRKEAAWAITNATSGGSAEQIKYLVELGCIKPLCDLLTVMDSKIVQVALNGLENILRLGEQEAKRNGTGINPYCALIEEAYGLDKIEFLQSHENQEIYQKAFDLIEHYFGTEDEDSSIAPQVDLNQQQYIFQQCEAPMEGFQL |
| Enzyme Length | 538 |
| Uniprot Accession Number | P52294 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (4); Chain (2); Compositional bias (1); Domain (1); Helix (31); Initiator methionine (1); Modified residue (4); Motif (1); Natural variant (1); Region (4); Repeat (10); Sequence conflict (2); Turn (2) |
| Keywords | 3D-structure;Acetylation;Cytoplasm;Direct protein sequencing;Host-virus interaction;Nucleus;Phosphoprotein;Protein transport;Reference proteome;Repeat;Transport;Ubl conjugation |
| Interact With | Q9GZX7; Q92688; Q9HAZ1; Q5TAQ9; Q13255; Q14974; P20700; Q9BQ69; Q9HAN9; Q9UKX7; Q9BUI4; Q15637; P42224; Q16594; K9N643; B4URF7; P31345; Q9WMX2 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7604027}. Nucleus {ECO:0000269|PubMed:7604027}. |
| Modified Residue | MOD_RES 1; /note="N-acetylmethionine"; /evidence="ECO:0007744|PubMed:22814378"; MOD_RES 2; /note="N-acetylthreonine; in Importin subunit alpha-5, N-terminally processed"; /evidence="ECO:0007744|PubMed:22814378"; MOD_RES 3; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 63; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569" |
| Post Translational Modification | PTM: Polyubiquitinated in the presence of RAG1 (in vitro). {ECO:0000269|PubMed:19118899}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 2JDQ; 3TJ3; 4B18; 6WX9; |
| Mapped Pubmed ID | 10205180; 10846107; 12048190; 12062430; 12740372; 12783858; 14743216; 15161933; 15231748; 15702989; 15731250; 16291214; 16298512; 16439554; 16713569; 17310249; 17351669; 17353931; 17376915; 17938174; 17981117; 18238777; 18707546; 18985028; 19001869; 19066626; 19084525; 19596235; 19615732; 1985200; 19889762; 20064372; 20193720; 20195357; 20360068; 20406804; 20467437; 20643137; 20692258; 20974480; 21209321; 21307607; 21555516; 21851590; 21987768; 21988832; 21994455; 22110766; 22130666; 22157821; 22321063; 22399302; 22810585; 23425335; 23602568; 23752268; 24269683; 24284509; 25272585; 25416956; 25609649; 25999477; 26052702; 26420826; 26496610; 28071726; 28455446; 28864541; 29304174; 33326746; 33397924; 33439253; 34195786; 7510216; 7559393; 8313914; 8955125; 9436978; 9582382; 9651582; |
| Motif | MOTIF 42..51; /note=Nuclear localization signal; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 60,222 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |