| IED ID | IndEnz0001000320 |
| Enzyme Type ID | amylase000320 |
| Protein Name |
MAP kinase-activating death domain protein Rab3 GDP/GTP exchange factor RabGEF Rab3 GDP/GTP exchange protein RabGEP |
| Gene Name | Madd |
| Organism | Rattus norvegicus (Rat) |
| 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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MVQKKFCPRLLDYLVIVGARHPSSDSVAQTPELLRRYPLEDHPEFPLPPDVVFFCQPEGCLSVRQRRMSLRDDTSFVFTLTDKDTGVTRYGICVNFYRSFQKRMPKEKAEGGAGPRGKEGAHAPCASEEAATESSESGSTLQPPSADSTPDVNQSPRGKRRAKAGNRSRNSTLTSLCVLSHYPFFSTFRECLYTLKRLVDCCSERLLGKKPGIPRGVQRDTMWRIFTGSLLVEEKSSALLHDLREIEAWIYRLLRSPVPVSGQKRVDIEVLPQEVQQALTFALPDPSRFTLVDFPLHLPLELLGVDACLQVLTCILLEHKVVLQSRDYNALSMSVMAFVAMIYPLEYMFPVIPLLPTCMASAEQLLLAPTPYIIGVPASFFLYKLDFKMPDDVWLVDLDSNRVIAPTNAEVLPILPEPESLELKKHLKQALASMSLNTQPILNLEKFHEGQETPLLLGRFSNDLQSTPSTEFNPLIYGNDVDSVDVATRVAMVRFFNSANVLQGFQMHTRTLRLFPRPVVAFQAGSFLASRPRQTPFAEKLARTQAVEYFGEWILNPSNYAFQRIHNNTFDPALIGDKPKWYAHQLQPIHYRVYDSNSQLAEALSVPPERDSESDPTDDSGSDSMDYDDSSSSYSSLGDFVSEMMKCDINGDTPNVDPLTHAALGDASEVEIDELQPQKEGEEPGPDSENSQENLPLRSSSSTTASSSPSTIVHGAHSEPADSTEVGDKAATGISKPLPPVPPSICKSTVDRRQTETGEGSVCQRTYDHPYFEPQYGSPAEEDDDEQGESYTPRFSQHASGSRAQKLLRPNSLKLASDSDAESDSRASSPNSTVSNNSTEGFGGIMSFASSLYRNHSTSFSLSNLTLPTKGAREKTTPFPSLKGNRRALVDQKSSVIKHSPTVKREPPSPQGRSSNSSENQQFLKEVVHSVLDGQGVGWLNMKKVRRLLESEQLRVFVLSKLSRAVQSEDDARQDVIQDVEISRKVYKGMLDLLKCTVLSLEQSYAHAGLGGMASIFGLLEIAQTHYYSKEPDKRKRSPTENVNTPVGKDPGLAGRGDPKAMAQLRVPQLGPRAPSATGRGPKELDTRSLKEENFVASVGPEVIKPVFDLGETEEKKSQISADSGVSLASASQRTDQDSVIGVSPAVMIRSSSQDSEVSNSSGETLGADSDLSSNAGDGPGGEGSAHLASSRATLSDSEIETNSATSTIFGKAHSLKPKEKPASSPVRSSEDVSQRVYLYEGLLGRDKGSMWDQLEDAAMETFSISKERSTLWDQMQFWEDAFLDAVMLEREGMGMDQGPQEMIDRYLSLGEHDRKRLEDDEDRLLATLLHNLISYMLLMKVNKNDIRKKVRRLMGKSHVGLVYSQQINEVLDQLTNLNGRDLSIRSSGSRHMKKQTFVVHAGTDTNGDIFFMEVCDDCVVLRSNIGTVYERWWYEKLINMTYCPKTKVLCLWRRNGSETQLNKFYTKKCRELYYCVKDSMERAAARQQSIKPGPELGGEFPVQDMKTGEGGLLQVTLEGINLKFMHNQVFIELNHIKKCNTVRGVFVLEEFVPEIKEVVSHKYKTPMAHEICYSVLCLFSYVAAVRSSEEDLRTPPRPVSS |
| Enzyme Length | 1602 |
| Uniprot Accession Number | O08873 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family (PubMed:9020086). Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms (By similarity). Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in synaptic vesicle exocytosis and vesicle secretion (PubMed:9020086). Plays a role in synaptic vesicle formation and in vesicle trafficking at the neuromuscular junction (By similarity). Involved in up-regulating a post-docking step of synaptic exocytosis in central synapses (By similarity). Probably by binding to the motor proteins KIF1B and KIF1A, mediates motor-dependent transport of GTP-RAB3A-positive vesicles to the presynaptic nerve terminals (By similarity). Plays a role in TNFA-mediated activation of the MAPK pathway, including ERK1/2 (By similarity). May link TNFRSF1A with MAP kinase activation (By similarity). May be involved in the regulation of TNFA-induced apoptosis (By similarity). {ECO:0000250|UniProtKB:Q80U28, ECO:0000250|UniProtKB:Q8WXG6, ECO:0000269|PubMed:9020086}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (7); Domain (4); Initiator methionine (1); Modified residue (19); Region (6) |
| Keywords | Apoptosis;Cell membrane;Cell projection;Cytoplasm;Direct protein sequencing;Guanine-nucleotide releasing factor;Membrane;Phosphoprotein;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8WXG6}. Cytoplasm {ECO:0000250|UniProtKB:Q8WXG6}. Cell projection, axon {ECO:0000250|UniProtKB:Q80U28}. |
| Modified Residue | MOD_RES 155; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q8WXG6"; MOD_RES 688; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:22673903"; MOD_RES 691; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:22673903"; MOD_RES 778; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:22673903"; MOD_RES 812; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:16641100, ECO:0007744|PubMed:22673903"; MOD_RES 817; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q8WXG6"; MOD_RES 819; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q8WXG6"; MOD_RES 857; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q8WXG6"; MOD_RES 861; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q8WXG6"; MOD_RES 895; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q8WXG6"; MOD_RES 900; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q8WXG6"; MOD_RES 909; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:22673903"; MOD_RES 1038; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:22673903"; MOD_RES 1040; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:22673903"; MOD_RES 1045; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:22673903"; MOD_RES 1089; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q80U28"; MOD_RES 1194; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:Q8WXG6"; MOD_RES 1196; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:22673903"; MOD_RES 1225; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q8WXG6" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12625816; 12786944; 16473592; 23702376; 9224661; 9852129; |
| Motif | |
| Gene Encoded By | |
| Mass | 177,992 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |