Detail Information for IndEnz0002019202
IED ID IndEnz0002019202
Enzyme Type ID protease019202
Protein Name ADP-ribosylation factor 1
Gene Name ARF1
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 MGNIFANLFKGLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQLRNQK
Enzyme Length 181
Uniprot Accession Number P84077
Absorption
Active Site
Activity Regulation
Binding Site BINDING 160; /note="GTP; via amide nitrogen"; /evidence="ECO:0007744|PDB:1HUR, ECO:0007744|PDB:1RE0, ECO:0007744|PDB:3O47"
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: GTP-binding protein involved in protein trafficking among different compartments. Modulates vesicle budding and uncoating within the Golgi complex. Deactivation induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, suggesting a crucial role in protein trafficking. In its GTP-bound form, its triggers the association with coat proteins with the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles. The GTP-bound form interacts with PICK1 to limit PICK1-mediated inhibition of Arp2/3 complex activity; the function is linked to AMPA receptor (AMPAR) trafficking, regulation of synaptic plasicity of excitatory synapses and spine shrinkage during long-term depression (LTD).; FUNCTION: (Microbial infection) Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. {ECO:0000305}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 24..32; /note="GTP"; /evidence="ECO:0000305, ECO:0007744|PDB:1HUR"; NP_BIND 126..129; /note="GTP"; /evidence="ECO:0000305, ECO:0007744|PDB:1HUR, ECO:0007744|PDB:1RE0, ECO:0007744|PDB:1U81, ECO:0007744|PDB:3O47"
Features Beta strand (11); Binding site (1); Chain (1); Helix (10); Initiator methionine (1); Lipidation (1); Modified residue (1); Natural variant (3); Nucleotide binding (2); Turn (2)
Keywords 3D-structure;Acetylation;Cell junction;Cytoplasm;Direct protein sequencing;Disease variant;ER-Golgi transport;GTP-binding;Golgi apparatus;Lipoprotein;Membrane;Myristate;Nucleotide-binding;Protein transport;Reference proteome;Synapse;Synaptosome;Transport
Interact With P53367; Q99418; O60271
Induction
Subcellular Location SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:17555535}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17555535}. Cell junction, synapse, synaptosome {ECO:0000250}. Cell junction, synapse, postsynaptic density {ECO:0000250}. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P84078}; Lipid-anchor {ECO:0000250|UniProtKB:P84078}.
Modified Residue MOD_RES 2; /note="N-acetylglycine; alternate"; /evidence="ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895"
Post Translational Modification PTM: Demyristoylated by S.flexneri cysteine protease IpaJ which cleaves the peptide bond between N-myristoylated Gly-2 and Asn-3. {ECO:0000269|PubMed:20213681, ECO:0000269|PubMed:23535599}.
Signal Peptide
Structure 3D NMR spectroscopy (1); Electron microscopy (6); X-ray crystallography (5)
Cross Reference PDB 1HUR; 1RE0; 1U81; 3O47; 4HMY; 6CM9; 6CRI; 6D83; 6D84; 6DFF; 6FAE; 7MGE;
Mapped Pubmed ID 10052452; 10189370; 10198630; 10318838; 10394364; 10480952; 10559940; 10593899; 10652308; 10652516; 10761932; 10921873; 11172815; 11461920; 11689559; 11694590; 11703931; 11726511; 11748249; 11914273; 11994746; 12047556; 12383348; 12799371; 14654833; 14654841; 14665636; 14676827; 14731593; 15143060; 15202998; 15336557; 15504911; 15581351; 15616190; 15632110; 15680326; 15781476; 15793564; 15813748; 15814706; 15876864; 16030262; 16038020; 16169070; 16308272; 1631136; 16545942; 16633337; 16669702; 1680566; 16912072; 16926190; 16940185; 17112341; 17116749; 17253781; 17289033; 17360540; 17429068; 17451557; 17693410; 17760859; 17927562; 17956946; 17981261; 18182008; 18283113; 18287528; 18451304; 18524849; 18551169; 18597672; 18693248; 18809720; 1898986; 18990689; 19015319; 19109418; 19141284; 19296914; 19338310; 19359423; 19367725; 1957170; 19596022; 19631211; 19644450; 19715559; 19738201; 19805454; 20089835; 20164217; 20214751; 20228810; 20357002; 20360068; 20427317; 20457610; 20529868; 20562859; 20637885; 20711500; 20861011; 20881058; 21068255; 2121367; 21219331; 21478909; 21789191; 21844168; 21844371; 21893600; 21988832; 22013193; 22025613; 22094269; 22158626; 22291037; 22304919; 22304920; 22348287; 22573888; 22573891; 22907437; 22962618; 22971977; 23255605; 23386615; 23415225; 23416715; 23707487; 23783033; 23804711; 23940353; 24196838; 24407288; 24497546; 24582959; 24911624; 24916416; 25114232; 25436559; 25530216; 25609649; 25754106; 25773595; 26169956; 26330566; 26494761; 26908458; 27213581; 27302278; 27320911; 27517156; 28007915; 28238095; 28428254; 28631186; 28830537; 28969640; 29467256; 29743604; 30053425; 30459446; 30610939; 30869179; 31232491; 31591270; 31875226; 32394429; 32558345; 32581103; 33335292; 33345740; 33405949; 34145292; 7592972; 7650016; 8001155; 8128252; 8132710; 8253837; 8505331; 8636227; 8810314; 8939989; 8945478; 8991093; 9114004; 9148941; 9244307; 9288971; 9380700; 9405360; 9405935; 9476900; 9497313; 9510256; 9614177; 9653114; 9671725; 9707577; 9751720; 9819391; 9990005;
Motif
Gene Encoded By
Mass 20,697
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda