Detail Information for IndEnz0002004176
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