ID   RAB2A_RABIT             Reviewed;         212 AA.
AC   Q01971;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Ras-related protein Rab-2A;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P53994};
GN   Name=RAB2A; Synonyms=RAB2;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1323270; DOI=10.1042/bj2850715;
RA   Tang L.H., Stoch S.A., Modlin I.M., Goldenring J.R.;
RT   "Identification of rab2 as a tubulovesicle-membrane-associated protein in
RT   rabbit gastric parietal cells.";
RL   Biochem. J. 285:715-719(1992).
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   -!- TISSUE SPECIFICITY: Brain and parietal cells.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; X68071; CAA48208.1; -; mRNA.
DR   PIR; S23979; S23979.
DR   RefSeq; NP_001095172.1; NM_001101702.1.
DR   AlphaFoldDB; Q01971; -.
DR   SMR; Q01971; -.
DR   STRING; 9986.ENSOCUP00000000293; -.
DR   GeneID; 100009281; -.
DR   KEGG; ocu:100009281; -.
DR   CTD; 5862; -.
DR   eggNOG; KOG0098; Eukaryota.
DR   InParanoid; Q01971; -.
DR   OrthoDB; 1271975at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
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:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
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_0000121068"
FT   REGION          2..19
FT                   /note="Required for interaction with PRKCI"
FT                   /evidence="ECO:0000250"
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;  23532 MW;  F8731E3F8B68B9A3 CRC64;
     MAYAYLFKYI IIGDTGVGKS CLLLQFTDKR FQPVHDLTIG VEFGARMITI DGKQIKLQIW
     DTAGQESFRS ITRSYYRGAA GALLVYDITR RDTFNHLTTW LEDARQHSNS NMVIMLIGNK
     SDLESRREVK KEEGEAFARE HGLIFMETSA KTASNVEEAF INTAKEIYEK IQEGVFDINN
     EANGIKIGPQ HGATNATHAG NQGGQQAGGG CC