IED ID | IndEnz0002004176 |
Enzyme Type ID | protease004176 |
Protein Name |
Nuclear pore complex protein Nup98-Nup96 EC 3.4.21.- Cleaved into: Nuclear pore complex protein Nup98 Nucleoporin Nup98 Nup98 ; Nuclear pore complex protein Nup96 Nucleoporin Nup96 Nup96 |
Gene Name | Nup98-96 Nup145 Nup98 CG10198 |
Organism | Drosophila melanogaster (Fruit fly) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly) |
Enzyme Sequence | MFGGAKPSFGATPAATSFGGFSGTTTTTPFGQSAFGKPAAPAFGNTSTFAAQPAQQSLFGAAATPAQPAGGLFGANTSTGFGSTATAQPTAFGAFSQPQQTSNIFGSTQTAASTSLFGQSTLPAFGAAKPTMTAFGQTAAAQPTGSLFGQPAAATSTTGFGGFGTSAPTTTNVFGSGTASAFAQPQATAVGASGVNTGTAVAKYQPTIGTDTLMKSGQANSVNTKQHCITAMKEFEGKSLEELRLEDYMCGRKGPQAGNAPGAFGFGAQVTQPAQPASGGLFGSTAQPSTGLFGQTVTENKSMFGTTAFGQQPATNNAFGAATQQNNFLQKPFGATTTTPFAAPAADASNPFGAKPAFGQGGSLFGQAPATSAAPAFGQTNTGFGGFGTTAGATQQSTLFGATPAADPNKSAFGLGTAASAATTGFGFGAPATSTAGGGLFGNKPATSFAAPTFGATSTASTPFSNFGLNTSTAATGGGLFNSGLNKPATSGFGGFGATSAAPLNFNAGNTGGSLFGNTAKPGGGLFGGGTTTLGGTGAAPTGGLFGGGTTSFGGVGGSLGGGGFGMGTNNSLTGGIMGAQPTLGIMTPSHQPIHQQILARVTSPYGDSPIFKDLKLSSEADATRATNPAAQQAVLDLTSNQYKISTSNNPAPMKVKALGSTLNRKSLFDGLEEFDASVEGFNLKPSAKRLVIKPKVKSVEGGNPSSSIGSAPNTPQSRPKGATPNKERESFSGAIPSEPLPPAGNSPGATNGRESQDNGRRESWLHPNNLEKVRQHNIQTGMDQGSPHNSTLNELVPRKPLDTYRPSSTVRLSVSTIPENPFEDQSSTIARRETFTSQQANESVLSNRSNEAEDSAANQSRLAIEAAAAEAADDESHPTGIVLRRVGYYTIPSLDDLRSYLAEDGSCVVPNFTVGREGYGNVFFGKEMDVAGLNLDEIVHFRNKEIIIYPDDENKPPIGQGLNRDAQVTLDQVWPLDKTKHEAIKDPQRLLEMDWEGKLRRVCDKNDTRFIEYRPETGSWVFRVKHFSKYGLGDSDEEDELPTDPKKAKIATLEAQQRANAEKMTLNSLRQAQKISEDAARNLDPKALVAGVASGFRPMDDTAEFLLMDKTQFFQAGGNSDFSMFDPPRQRPTITSPTAVLAQEMVGNEAHKMQLMKSSFFVEDNAPEDEPMETTGRLLRHRKFFNVEPLVWKDGASESSSQYDFEHPSPALPISSSVSEASLMCDAHYEETSSMATGSIVAAVKETKFEMPVTKAFKFVCKPKVAPIKLRATTVPLPRSIAYEMRDNWIADLGFYKGRSFKLSFGPQNSLVLPSTYNNMQNLKEFTGPSLPVSMVFAPRSATDLSPSVMQLVEFNMVKGNEGFRESIIPHLEVQLNDCLSVNVEGSECPCIHPDSGTKLVSKHFSESLKQRNAGLKEDYSVSVWSLLFALWGDHDELVDLEKNSHYMVMCRRNLLSEWLENTLLGKDLLSKKVSTHSYLEHMLDLLSCHRVNEACELAFSYDDANLALVLSQLSSGAVFRLLMEEQLFAWQQSKSDKYIDLERLKMYMLAAGAPMMQSSHGAINLLENKNWLTALALQLWYFTAPTSSITDALNAYNDAFQAEECYAEPPKPSYRDAPTDTKKPVYDLRYHLLQLHSKRMHSLEETLNPITHTADAMDFRLSWLLLQTLRALGYRHCSPLTEARLSVDFASQLENEGLWQWGIFVLLHIKQQTQRERAVQQMLQRNVSVSAKVALYAEERFIVEELGIPMSWVDYAKAVKAGASGKHHLQAKYLLKAKHFATAHDVIFQHIAPDAIINGKMKYLHSLLIQFEDTEGSSIRVPNWANQGQIFLDFIDISAKFKQIRSVTNIADINARWENLKPQLSELCSRISLLPCPTSKHRLCQSEISQSLSCLVHGMCIVCPEMESSTVLKVALERLPLPQEFASKELRIWLEELLDKIQNEPPFSERQQPTMMEI |
Enzyme Length | 1960 |
Uniprot Accession Number | Q9VCH5 |
Absorption | |
Active Site | ACT_SITE 1029; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P52948 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.21.- |
Enzyme Function | FUNCTION: Part of the nuclear pore complex (NPC) (PubMed:25197089). Required for MAD import as part of the Nup107-160 complex and required for nuclear export of Moe probably via its association with Rae1 (PubMed:20547758, PubMed:28554770). Plays a role in nuclear mRNA export (PubMed:28554770). Promotes cell antiviral response by up-regulating FoxK-dependent antiviral gene transcription (PubMed:25197089, PubMed:25852164). In germline stem cells, involved in their maintenance and division together with the TGF-Beta and EGFR signaling pathways (PubMed:21949861). In larval lymph glands, has a role in the maintenance of hematopoiesis by regulating Pvr expression (PubMed:25201876). {ECO:0000269|PubMed:20547758, ECO:0000269|PubMed:21949861, ECO:0000269|PubMed:25197089, ECO:0000269|PubMed:25201876, ECO:0000269|PubMed:25852164, ECO:0000269|PubMed:28554770}.; FUNCTION: [Nuclear pore complex protein Nup98]: Part of the nuclear pore complex (NPC) (PubMed:25310983). In the nucleoplasm, binds to transcriptionally active chromatin with a preference for regulatory regions; co-localizes with RNA polymerase II in a RNA-independent manner and before transition into transcription elongation (PubMed:20144760, PubMed:20144761, PubMed:28366641). Plays a role in the transcriptional memory process by stabilizing enhancer-promoter loops and by mediating anchoring of chromatin to the nuclear pore complex region (PubMed:28366641). During larval development, interacts with trx and MBD-R2 and regulates transcription of developmental genes including ecdysone-responsive genes such as Eip74 and E23 (PubMed:20144761, PubMed:25310983, PubMed:28366641). {ECO:0000269|PubMed:20144760, ECO:0000269|PubMed:20144761, ECO:0000269|PubMed:25310983, ECO:0000269|PubMed:28366641}.; FUNCTION: [Nuclear pore complex protein Nup96]: Part of the nuclear pore complex (NPC). {ECO:0000269|PubMed:25310983}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Alternative sequence (2); Chain (2); Compositional bias (2); Domain (1); Region (3); Repeat (46); Sequence conflict (1); Site (1) |
Keywords | Alternative splicing;Autocatalytic cleavage;Chromosome;Hydrolase;Membrane;Nuclear pore complex;Nucleus;Protease;Protein transport;Reference proteome;Repeat;Serine protease;Transcription;Transcription regulation;Translocation;Transport;mRNA transport |
Interact With | |
Induction | INDUCTION: Up-regulated upon Drosophila C virus (DCV) or Sindbis virus (SINV) infection. {ECO:0000269|PubMed:25197089}. |
Subcellular Location | SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:20144761}. Nucleus, nucleoplasm {ECO:0000269|PubMed:20144760}. Nucleus membrane {ECO:0000269|PubMed:20144761, ECO:0000269|PubMed:25197089}; Peripheral membrane protein {ECO:0000250|UniProtKB:P52948}; Nucleoplasmic side {ECO:0000250|UniProtKB:P52948}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:25310983}. Nucleus {ECO:0000269|PubMed:28366641}. Note=Associates with transcriptionally active chromatin. {ECO:0000269|PubMed:20144760, ECO:0000269|PubMed:20144761, ECO:0000269|PubMed:28366641}.; SUBCELLULAR LOCATION: [Nuclear pore complex protein Nup98]: Nucleus, nuclear pore complex {ECO:0000269|PubMed:25310983}.; SUBCELLULAR LOCATION: [Nuclear pore complex protein Nup96]: Nucleus, nuclear pore complex {ECO:0000269|PubMed:25310983}. |
Modified Residue | |
Post Translational Modification | PTM: Isoform A and isoform C are autoproteolytically cleaved to yield Nup98 and Nup96 or Nup98 only, respectively. {ECO:0000250|UniProtKB:P52948}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 12802320; 12802326; 14605208; 14638324; 15090076; 15531163; 15579690; 15851676; 15854890; 15996653; 16055650; 16311596; 16336044; 16543150; 17056646; 17124304; 17151602; 17409061; 19057646; 19197064; 20044587; 20051985; 20220848; 20371351; 20530634; 20818332; 20949036; 21074052; 21150273; 21368190; 21505791; 21771720; 21903731; 22191063; 22751930; 23071443; 23087834; 23087835; 23090414; 23827710; 24171912; 24615017; 25172915; 25242144; 25294943; 25312911; 25687947; 26021350; 26308899; 26526100; 26551273; 26870755; 26896675; 27582081; 28472469; 29138279; 29723993; 29773558; 30549175; 31626769; 31722958; 31941789; 33477509; 33629655; 33827210; 33856346; 34059832; 34484226; 9245788; 9769169; |
Motif | |
Gene Encoded By | |
Mass | 210,139 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |