RAB2A_DICDI
ID RAB2A_DICDI Reviewed; 207 AA.
AC P36409; Q54DF6;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Ras-related protein Rab-2A;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P53994};
GN Name=rab2A; Synonyms=rab2; ORFNames=DDB_G0292268;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-207.
RC STRAIN=AX3;
RA Bush J.M. IV, Nolta K., Rodriguez-Paris J., Temesvari L., Ruscetti T.,
RA Steck T., Cardelli J.A.;
RT "Cloning and characterization of a rab 2-like GTPase in Dictyostelium
RT discoideum.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The small GTPases Rab are key regulators of intracellular
CC membrane trafficking, from the formation of transport vesicles to their
CC fusion with membranes. Rabs cycle between active GTP-bound and inactive
CC GDP-bound states. In their active state, drive transport of vesicular
CC carriers from donor organelles to acceptor organelles to regulate the
CC membrane traffic that maintains organelle identity and morphology.
CC {ECO:0000250|UniProtKB:P61019}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P53994};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P53994};
CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC (GEFs) which promote the exchange of bound GDP for free GTP, GTPase
CC activating proteins (GAPs) which increase the GTP hydrolysis activity,
CC and GDP dissociation inhibitors which inhibit the dissociation of the
CC nucleotide from the GTPase. {ECO:0000250|UniProtKB:P61019}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000189; EAL61258.1; -; Genomic_DNA.
DR EMBL; U02926; AAA80150.1; -; mRNA.
DR RefSeq; XP_629685.1; XM_629683.1.
DR AlphaFoldDB; P36409; -.
DR SMR; P36409; -.
DR STRING; 44689.DDB0216191; -.
DR PaxDb; P36409; -.
DR EnsemblProtists; EAL61258; EAL61258; DDB_G0292268.
DR GeneID; 8628601; -.
DR KEGG; ddi:DDB_G0292268; -.
DR dictyBase; DDB_G0292268; rab2A.
DR eggNOG; KOG0098; Eukaryota.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; P36409; -.
DR OMA; ANGVMQY; -.
DR PhylomeDB; P36409; -.
DR Reactome; R-DDI-8873719; RAB geranylgeranylation.
DR PRO; PR:P36409; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0031164; C:contractile vacuolar membrane; IDA:dictyBase.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IDA:dictyBase.
DR GO; GO:0005811; C:lipid droplet; HDA:dictyBase.
DR GO; GO:0140220; C:pathogen-containing vacuole; HDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0008219; P:cell death; IMP:dictyBase.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0047484; P:regulation of response to osmotic stress; IMP:dictyBase.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IMP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..207
FT /note="Ras-related protein Rab-2A"
FT /id="PRO_0000121271"
FT REGION 187..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 34..42
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 12..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61019"
FT BINDING 60..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 118..121
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61019"
FT BINDING 148..150
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61019"
FT LIPID 205
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 206
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 207 AA; 23093 MW; 44A3DA1C62FA4E3B CRC64;
MYSFLFKYII IGDTGVGKSC LLLQFTDKRF QPVHDLTIGV EFGARMITID NKAIKLQIWD
TAGQESFRSI TRSYYRGSAG ALLVYDITRR DTFNHLTCWL KDARSYANSN MTIILIGNKS
DMESKRAVSY EEGRQFADEN GLIFLETSAK TASNVEEAFV NTASKIYEKI QKGDFDINNE
SFGIKLGAPT SKQDGTDQKP AGGGCCK
