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Overview

Uniprot IDQ15042
Protein NameRab3 GTPase-activating protein catalytic subunit
Gene NameRAB3GAP1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
366 DITHALSKLTEPASV

Function

Catalytic subunit of the Rab3 GTPase-activating (Rab3GAP) complex composed of RAB3GAP1 and RAB3GAP2, which accelerates the otherwise slow GTP hydrolysis catalyzed by Rab proteins (PubMed:9030515, PubMed:10859313, PubMed:39779760). Has GTPase-activating protein (GAP) activity towards various Rab3 subfamily members (RAB3A, RAB3B, RAB3C and RAB3D), RAB5A and RAB43 (PubMed:10859313, PubMed:9030515, PubMed:39779760). Additionally, it has guanine nucleotide exchange factor (GEF) activity towards RAB18, promoting GDP release from RAB18 and the conversion of inactive RAB18-GDP to the active form RAB18-GTP (PubMed:24891604, PubMed:39779760). Recruits and stabilizes RAB18 at the cis-Golgi membrane in fibroblasts where RAB18 is most likely activated (PubMed:26063829). Also involved in RAB18 recruitment at the endoplasmic reticulum (ER) membrane where it maintains proper ER structure (PubMed:24891604). Required for normal eye and brain development (PubMed:15696165, PubMed:23420520). May participate in neurodevelopmental processes such as cell proliferation, migration and differentiation before synapse formation, and is involved in regulating non-synaptic vesicular release of neurotransmitters (PubMed:9030515, PubMed:9852129)

Protein Sequence

10 MAADSEPESE 20 VFEITDFTTA 30 SEWERFISKV 40 EEVLNDWKLI 50 GNSLGKPLEK 60 GIFTSGTWEE 70 KSDEISFADF 80 KFSVTHHYLV 90 QESTDKEGKD 100 ELLEDVVPQS 110 MQDLLGMNND 120 FPPRAHCLVR 130 WYGLREFVVI 140 APAAHSDAVL 150 SESKCNLLLS 160 SVSIALGNTG 170 CQVPLFVQIH 180 HKWRRMYVGE 190 CQGPGVRTDF 200 EMVHLRKVPN 210 QYTHLSGLLD 220 IFKSKIGCPL 230 TPLPPVSIAI 240 RFTYVLQDWQ 250 QYFWPQQPPD 260 IDALVGGEVG 270 GLEFGKLPFG 280 ACEDPISELH 290 LATTWPHLTE 300 GIIVDNDVYS 310 DLDPIQAPHW 320 SVRVRKAENP 330 QCLLGDFVTE 340 FFKICRRKES 350 TDEILGRSAF 360 EEEGKETADI 370 THALSKLTEP 380 ASVPIHKLSV 390 SNMVHTAKKK 400 IRKHRGVEES 410 PLNNDVLNTI 420 LLFLFPDAVS 430 EKPLDGTTST 440 DNNNPPSESE 450 DYNLYNQFKS 460 APSDSLTYKL 470 ALCLCMINFY 480 HGGLKGVAHL 490 WQEFVLEMRF 500 RWENNFLIPG 510 LASGPPDLRC 520 CLLHQKLQML 530 NCCIERKKAR 540 DEGKKTSASD 550 VTNIYPGDAG 560 KAGDQLVPDN 570 LKETDKEKGE 580 VGKSWDSWSD 590 SEEEFFECLS 600 DTEELKGNGQ 610 ESGKKGGPKE 620 MANLRPEGRL 630 YQHGKLTLLH 640 NGEPLYIPVT 650 QEPAPMTEDL 660 LEEQSEVLAK 670 LGTSAEGAHL 680 RARMQSACLL 690 SDMESFKAAN 700 PGCSLEDFVR 710 WYSPRDYIEE 720 EVIDEKGNVV 730 LKGELSARMK 740 IPSNMWVEAW 750 ETAKPIPARR 760 QRRLFDDTRE 770 AEKVLHYLAI 780 QKPADLARHL 790 LPCVIHAAVL 800 KVKEEESLEN 810 ISSVKKIIKQ 820 IISHSSKVLH 830 FPNPEDKKLE 840 EIIHQITNVE 850 ALIARARSLK 860 AKFGTEKCEQ 870 EEEKEDLERF 880 VSCLLEQPEV 890 LVTGAGRGHA 900 GRIIHKLFVN 910 AQRAAAMTPP 920 EEELKRMGSP 930 EERRQNSVSD 940 FPPPAGREFI 950 LRTTVPRPAP 960 YSKALPQRMY 970 SVLTKEDFRL 980 AGAFSSDTSF F

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005801 cis-Golgi network
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005789 endoplasmic reticulum membrane
Cellular Component GO:0071782 endoplasmic reticulum tubular network
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005794 Golgi apparatus
Cellular Component GO:0005811 lipid droplet
Cellular Component GO:0098794 postsynapse
Cellular Component GO:0032991 protein-containing complex
Molecular Function GO:0005096 GTPase activator activity
Molecular Function GO:0005085 guanyl-nucleotide exchange factor activity
Molecular Function GO:0031267 small GTPase binding
Biological Process GO:0007420 brain development
Biological Process GO:0043010 camera-type eye development
Biological Process GO:0097051 establishment of protein localization to endoplasmic reticulum membrane
Biological Process GO:0060079 excitatory postsynaptic potential
Biological Process GO:0060325 face morphogenesis
Biological Process GO:0021854 hypothalamus development
Biological Process GO:0034389 lipid droplet organization
Biological Process GO:2000786 positive regulation of autophagosome assembly
Biological Process GO:1903373 positive regulation of endoplasmic reticulum tubular network organization
Biological Process GO:0061646 positive regulation of glutamate neurotransmitter secretion in response to membrane depolarization
Biological Process GO:1903061 positive regulation of protein lipidation
Biological Process GO:0032482 Rab protein signal transduction
Biological Process GO:1903233 regulation of calcium ion-dependent exocytosis of neurotransmitter
Biological Process GO:0048172 regulation of short-term neuronal synaptic plasticity

Reference

[1] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.