RAB2A_HUMAN
ID RAB2A_HUMAN Reviewed; 212 AA.
AC P61019; B2R5W8; B4DMQ5; P08886;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Ras-related protein Rab-2A {ECO:0000305};
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P53994};
GN Name=RAB2A {ECO:0000312|HGNC:HGNC:9763}; Synonyms=RAB2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3057444; DOI=10.1093/nar/16.21.10368;
RA Tachibana K., Umezawa A., Kato S., Takano T.;
RT "Nucleotide sequence of a new YPT1-related human cDNA which belongs to the
RT ras gene superfamily.";
RL Nucleic Acids Res. 16:10368-10368(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2501306; DOI=10.1016/s0021-9258(18)63872-4;
RA Zahraoui A., Touchot N., Chardin P., Tavitian A.;
RT "The human Rab genes encode a family of GTP-binding proteins related to
RT yeast YPT1 and SEC4 products involved in secretion.";
RL J. Biol. Chem. 264:12394-12401(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Brain cortex;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP ISOPRENYLATION AT CYS-211 AND CYS-212.
RX PubMed=1648736; DOI=10.1073/pnas.88.14.6264;
RA Khosravi-Far R., Lutz R.J., Cox A.D., Conroy L., Bourne J.R., Sinensky M.,
RA Balch W.E., Buss J.E., Der C.J.;
RT "Isoprenoid modification of rab proteins terminating in CC or CXC motifs.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6264-6268(1991).
RN [10]
RP INTERACTION WITH PRKCI.
RX PubMed=14570876; DOI=10.1074/jbc.m309343200;
RA Tisdale E.J.;
RT "Rab2 interacts directly with atypical protein kinase C (aPKC) iota/lambda
RT and inhibits aPKCiota/lambda-dependent glyceraldehyde-3-phosphate
RT dehydrogenase phosphorylation.";
RL J. Biol. Chem. 278:52524-52530(2003).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP FUNCTION.
RX PubMed=26209634; DOI=10.1074/jbc.m115.669242;
RA Aizawa M., Fukuda M.;
RT "Small GTPase Rab2B and Its Specific Binding Protein Golgi-associated Rab2B
RT Interactor-like 4 (GARI-L4) Regulate Golgi Morphology.";
RL J. Biol. Chem. 290:22250-22261(2015).
RN [15]
RP INTERACTION WITH TRIP11.
RX PubMed=25473115; DOI=10.1091/mbc.e14-10-1450;
RA Sato K., Roboti P., Mironov A.A., Lowe M.;
RT "Coupling of vesicle tethering and Rab binding is required for in vivo
RT functionality of the golgin GMAP-210.";
RL Mol. Biol. Cell 26:537-553(2015).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 2-170 IN COMPLEX WITH GDP.
RX PubMed=16034420; DOI=10.1038/nature03798;
RA Eathiraj S., Pan X., Ritacco C., Lambright D.G.;
RT "Structural basis of family-wide Rab GTPase recognition by rabenosyn-5.";
RL Nature 436:415-419(2005).
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:0000305|PubMed:26209634}.
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:0000305}.
CC -!- SUBUNIT: Interacts with PRKCI (PubMed:14570876). Interacts with TRIP11
CC (PubMed:25473115). Interacts (in GTP-bound form) with GARIN1B (By
CC similarity). {ECO:0000250|UniProtKB:P53994,
CC ECO:0000269|PubMed:14570876, ECO:0000269|PubMed:25473115}.
CC -!- INTERACTION:
CC P61019; Q9H2G9: BLZF1; NbExp=9; IntAct=EBI-752037, EBI-2548012;
CC P61019; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-752037, EBI-11977221;
CC P61019; Q9Y281: CFL2; NbExp=3; IntAct=EBI-752037, EBI-351218;
CC P61019; Q8IWE2: FAM114A1; NbExp=7; IntAct=EBI-752037, EBI-2686288;
CC P61019; Q9NRY5: FAM114A2; NbExp=3; IntAct=EBI-752037, EBI-10973142;
CC P61019; Q8IYT1: FAM71A; NbExp=3; IntAct=EBI-752037, EBI-20113335;
CC P61019; Q8NEG0: FAM71C; NbExp=7; IntAct=EBI-752037, EBI-752049;
CC P61019; Q6NXP2-2: FAM71F2; NbExp=4; IntAct=EBI-752037, EBI-12925824;
CC P61019; Q8N878: FRMD1; NbExp=3; IntAct=EBI-752037, EBI-11749206;
CC P61019; Q08379: GOLGA2; NbExp=7; IntAct=EBI-752037, EBI-618309;
CC P61019; Q96HZ4: HES6; NbExp=3; IntAct=EBI-752037, EBI-7469266;
CC P61019; Q05084: ICA1; NbExp=4; IntAct=EBI-752037, EBI-1046751;
CC P61019; Q13794-2: PMAIP1; NbExp=3; IntAct=EBI-752037, EBI-12170575;
CC P61019; Q96FJ0: STAMBPL1; NbExp=10; IntAct=EBI-752037, EBI-745021;
CC P61019; Q3MII6: TBC1D25; NbExp=3; IntAct=EBI-752037, EBI-11899977;
CC P61019; Q9BUB7: TMEM70; NbExp=3; IntAct=EBI-752037, EBI-726363;
CC P61019; Q9C029: TRIM7; NbExp=3; IntAct=EBI-752037, EBI-2813981;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000269|PubMed:17081065}; Lipid-anchor
CC {ECO:0000269|PubMed:17081065}. Melanosome
CC {ECO:0000269|PubMed:17081065}. Endoplasmic reticulum membrane
CC {ECO:0000305}; Lipid-anchor {ECO:0000305}. Golgi apparatus membrane
CC {ECO:0000305}; Lipid-anchor {ECO:0000305}. Cytoplasmic vesicle,
CC secretory vesicle, acrosome {ECO:0000250|UniProtKB:P53994}.
CC Note=Localized in the Golgi apparatus in the round spermatids and in
CC the acrosome in the elongating spermatid (By similarity). Identified by
CC mass spectrometry in melanosome fractions from stage I to stage IV
CC (PubMed:17081065). {ECO:0000250|UniProtKB:P53994,
CC ECO:0000269|PubMed:17081065}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P61019-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61019-2; Sequence=VSP_042917;
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; X12953; CAA31411.1; -; mRNA.
DR EMBL; M28213; AAA60241.1; -; mRNA.
DR EMBL; AF498930; AAM21078.1; -; mRNA.
DR EMBL; BT019695; AAV38501.1; -; mRNA.
DR EMBL; AK297576; BAG59967.1; -; mRNA.
DR EMBL; AK312344; BAG35265.1; -; mRNA.
DR EMBL; AC068389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471068; EAW86827.1; -; Genomic_DNA.
DR EMBL; BC008929; AAH08929.1; -; mRNA.
DR CCDS; CCDS56537.1; -. [P61019-2]
DR CCDS; CCDS6175.1; -. [P61019-1]
DR PIR; B34323; B34323.
DR RefSeq; NP_001229573.1; NM_001242644.1. [P61019-2]
DR RefSeq; NP_002856.1; NM_002865.2. [P61019-1]
DR PDB; 1Z0A; X-ray; 2.12 A; A/B/C/D=2-170.
DR PDBsum; 1Z0A; -.
DR AlphaFoldDB; P61019; -.
DR SMR; P61019; -.
DR BioGRID; 111800; 529.
DR DIP; DIP-316N; -.
DR IntAct; P61019; 78.
DR MINT; P61019; -.
DR STRING; 9606.ENSP00000262646; -.
DR ChEMBL; CHEMBL4105893; -.
DR GlyGen; P61019; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61019; -.
DR PhosphoSitePlus; P61019; -.
DR SwissPalm; P61019; -.
DR BioMuta; RAB2A; -.
DR DMDM; 46577636; -.
DR EPD; P61019; -.
DR jPOST; P61019; -.
DR MassIVE; P61019; -.
DR MaxQB; P61019; -.
DR PaxDb; P61019; -.
DR PeptideAtlas; P61019; -.
DR PRIDE; P61019; -.
DR ProteomicsDB; 57251; -. [P61019-1]
DR ProteomicsDB; 57252; -. [P61019-2]
DR TopDownProteomics; P61019-1; -. [P61019-1]
DR TopDownProteomics; P61019-2; -. [P61019-2]
DR Antibodypedia; 4367; 339 antibodies from 37 providers.
DR DNASU; 5862; -.
DR Ensembl; ENST00000262646.12; ENSP00000262646.7; ENSG00000104388.15. [P61019-1]
DR Ensembl; ENST00000531289.5; ENSP00000431846.1; ENSG00000104388.15. [P61019-2]
DR GeneID; 5862; -.
DR KEGG; hsa:5862; -.
DR MANE-Select; ENST00000262646.12; ENSP00000262646.7; NM_002865.3; NP_002856.1.
DR UCSC; uc003xud.3; human. [P61019-1]
DR CTD; 5862; -.
DR DisGeNET; 5862; -.
DR GeneCards; RAB2A; -.
DR HGNC; HGNC:9763; RAB2A.
DR HPA; ENSG00000104388; Low tissue specificity.
DR MIM; 179509; gene.
DR neXtProt; NX_P61019; -.
DR OpenTargets; ENSG00000104388; -.
DR PharmGKB; PA162400618; -.
DR VEuPathDB; HostDB:ENSG00000104388; -.
DR eggNOG; KOG0098; Eukaryota.
DR GeneTree; ENSGT00940000153886; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; P61019; -.
DR OMA; ANGVMQY; -.
DR PhylomeDB; P61019; -.
DR TreeFam; TF300032; -.
DR BRENDA; 3.6.5.2; 2681.
DR PathwayCommons; P61019; -.
DR Reactome; R-HSA-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR SignaLink; P61019; -.
DR SIGNOR; P61019; -.
DR BioGRID-ORCS; 5862; 27 hits in 1085 CRISPR screens.
DR ChiTaRS; RAB2A; human.
DR EvolutionaryTrace; P61019; -.
DR GeneWiki; RAB2A; -.
DR GenomeRNAi; 5862; -.
DR Pharos; P61019; Tchem.
DR PRO; PR:P61019; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P61019; protein.
DR Bgee; ENSG00000104388; Expressed in tendon of biceps brachii and 220 other tissues.
DR ExpressionAtlas; P61019; baseline and differential.
DR Genevisible; P61019; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; TAS:ProtInc.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasmic vesicle;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; GTP-binding;
KW Hydrolase; Lipoprotein; Membrane; Nucleotide-binding; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..212
FT /note="Ras-related protein Rab-2A"
FT /id="PRO_0000121066"
FT REGION 2..19
FT /note="Required for interaction with PRKCI"
FT /evidence="ECO:0000269|PubMed:14570876"
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:0007744|PDB:1Z0A"
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:0007744|PDB:1Z0A"
FT BINDING 149..151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:1Z0A"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT LIPID 211
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:1648736"
FT LIPID 212
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:1648736"
FT VAR_SEQ 16..39
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042917"
FT CONFLICT 144
FT /note="I -> M (in Ref. 2; AAA60241)"
FT /evidence="ECO:0000305"
FT STRAND 4..14
FT /evidence="ECO:0007829|PDB:1Z0A"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:1Z0A"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:1Z0A"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:1Z0A"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:1Z0A"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:1Z0A"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:1Z0A"
FT HELIX 91..95
FT /evidence="ECO:0007829|PDB:1Z0A"
FT HELIX 97..107
FT /evidence="ECO:0007829|PDB:1Z0A"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:1Z0A"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1Z0A"
FT HELIX 131..141
FT /evidence="ECO:0007829|PDB:1Z0A"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:1Z0A"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:1Z0A"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:1Z0A"
SQ SEQUENCE 212 AA; 23546 MW; F8731E3F8FB399A3 CRC64;
MAYAYLFKYI IIGDTGVGKS CLLLQFTDKR FQPVHDLTIG VEFGARMITI DGKQIKLQIW
DTAGQESFRS ITRSYYRGAA GALLVYDITR RDTFNHLTTW LEDARQHSNS NMVIMLIGNK
SDLESRREVK KEEGEAFARE HGLIFMETSA KTASNVEEAF INTAKEIYEK IQEGVFDINN
EANGIKIGPQ HAATNATHAG NQGGQQAGGG CC
