| 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 |
|