RAB2A_RAT
ID RAB2A_RAT Reviewed; 212 AA.
AC P05712;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Ras-related protein Rab-2A;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P53994};
GN Name=Rab2a; Synonyms=Rab2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3317403; DOI=10.1073/pnas.84.23.8210;
RA Touchot N., Chardin P., Tavitian A.;
RT "Four additional members of the ras gene superfamily isolated by an
RT oligonucleotide strategy: molecular cloning of YPT-related cDNAs from a rat
RT brain library.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:8210-8214(1987).
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 Required for protein transport from the endoplasmic reticulum to the
CC Golgi complex. Regulates the compacted morphology of the Golgi.
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 -!- SUBUNIT: Interacts with PRKCI. Interacts with TRIP11 (By similarity).
CC Interacts (in GTP-bound form) with GARIN1B (By similarity).
CC {ECO:0000250|UniProtKB:P53994, ECO:0000250|UniProtKB:P61019}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000250|UniProtKB:P61019}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P61019}. Melanosome
CC {ECO:0000250|UniProtKB:P61019}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P61019}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P61019}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P61019}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P61019}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome {ECO:0000250|UniProtKB:P53994}. Note=Localized in the Golgi
CC apparatus in the round spermatids and in the acrosome in the elongating
CC spermatid (By similarity). Identified by mass spectrometry in
CC melanosome fractions from stage I to stage IV (By similarity).
CC {ECO:0000250|UniProtKB:P53994, ECO:0000250|UniProtKB:P61019}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; J02999; AAA42007.1; -; mRNA.
DR PIR; B39963; B39963.
DR RefSeq; NP_113906.1; NM_031718.1.
DR AlphaFoldDB; P05712; -.
DR SMR; P05712; -.
DR BioGRID; 249274; 3.
DR CORUM; P05712; -.
DR IntAct; P05712; 3.
DR MINT; P05712; -.
DR STRING; 10116.ENSRNOP00000008522; -.
DR iPTMnet; P05712; -.
DR PhosphoSitePlus; P05712; -.
DR SwissPalm; P05712; -.
DR World-2DPAGE; 0004:P05712; -.
DR jPOST; P05712; -.
DR PaxDb; P05712; -.
DR PRIDE; P05712; -.
DR GeneID; 65158; -.
DR KEGG; rno:65158; -.
DR UCSC; RGD:68323; rat.
DR CTD; 5862; -.
DR RGD; 68323; Rab2a.
DR eggNOG; KOG0098; Eukaryota.
DR InParanoid; P05712; -.
DR OrthoDB; 1271975at2759; -.
DR PhylomeDB; P05712; -.
DR Reactome; R-RNO-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR PRO; PR:P05712; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:RGD.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:RGD.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:RGD.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032482; P:Rab protein signal transduction; IC:RGD.
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 Acetylation; Cytoplasmic vesicle; Endoplasmic reticulum;
KW ER-Golgi transport; Golgi apparatus; GTP-binding; Hydrolase; Lipoprotein;
KW Membrane; Nucleotide-binding; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P61019"
FT CHAIN 2..212
FT /note="Ras-related protein Rab-2A"
FT /id="PRO_0000121069"
FT REGION 2..19
FT /note="Required for interaction with PRKCI"
FT /evidence="ECO:0000250"
FT REGION 190..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 35..43
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 13..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61019"
FT BINDING 61..65
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 119..122
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61019"
FT BINDING 149..151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61019"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P61019"
FT LIPID 211
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 212
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 212 AA; 23536 MW; B68AAFF894DBE819 CRC64;
MAYAYLFKYI IIGDTGVGKS CLLLQFTDKR FQPVHDLTMG VEFGARMITI DGKQIKLQIW
DTAGQESFRS ITRSYYRGAA GALLVYDITR RDTFNHLTTW LEDARQHSNS NMVIMLIGNK
SDLESRREVK KEEGEAFARE HGLIFMETSA KTASNVEEAF INTAKEIYEK IQEGVFDINN
EANGIKIGPQ HAATNASHGG NQGGQQAGGG CC
