RAB5A_HUMAN
ID RAB5A_HUMAN Reviewed; 215 AA.
AC P20339; B4DJA5; Q6FI44;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 231.
DE RecName: Full=Ras-related protein Rab-5A;
DE EC=3.6.5.2 {ECO:0000269|PubMed:15378032};
GN Name=RAB5A; Synonyms=RAB5;
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=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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ISOPRENYLATION AT CYS-212 AND
RP CYS-213, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=7991565; DOI=10.1073/pnas.91.25.11963;
RA Farnsworth C.C., Seabra M.C., Ericsson L.H., Gelb M.H., Glomset J.A.;
RT "Rab geranylgeranyl transferase catalyzes the geranylgeranylation of
RT adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:11963-11967(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kim J.W.;
RT "Identification of a new oncogene in human cancers.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Subthalamic nucleus;
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 MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix, and Placenta;
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 [10]
RP INTERACTION WITH EEA1.
RX PubMed=10491193; DOI=10.1046/j.1432-1327.1999.00743.x;
RA Callaghan J.M., Nixon S., Bucci C., Toh B.-H., Stenmark H.;
RT "Direct interaction of EEA1 with Rab5b.";
RL Eur. J. Biochem. 265:361-366(1999).
RN [11]
RP INTERACTION WITH SUN2, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10818110; DOI=10.1074/jbc.m909600199;
RA Hoffenberg S., Liu X., Nikolova L., Hall H.S., Dai W., Baughn R.E.,
RA Dickey B.F., Barbieri M.A., Aballay A., Stahl P.D., Knoll B.J.;
RT "A novel membrane-anchored Rab5 interacting protein required for homotypic
RT endosome fusion.";
RL J. Biol. Chem. 275:24661-24669(2000).
RN [12]
RP INTERACTION WITH ZFYVE20.
RC TISSUE=Cervix carcinoma;
RX PubMed=11062261; DOI=10.1083/jcb.151.3.601;
RA Nielsen E., Christoforidis S., Uttenweiler-Joseph S., Miaczynska M.,
RA Dewitte F., Wilm M., Hoflack B., Zerial M.;
RT "Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited
RT to endosomes through a FYVE finger domain.";
RL J. Cell Biol. 151:601-612(2000).
RN [13]
RP ACTIVATION BY RIN1.
RX PubMed=11703925; DOI=10.1016/s1534-5807(01)00008-9;
RA Tall G.G., Barbieri M.A., Stahl P.D., Horazdovsky B.F.;
RT "Ras-activated endocytosis is mediated by the Rab5 guanine nucleotide
RT exchange activity of RIN1.";
RL Dev. Cell 1:73-82(2001).
RN [14]
RP INTERACTION WITH ALS2CL.
RX PubMed=15388334; DOI=10.1016/j.febslet.2004.07.092;
RA Hadano S., Otomo A., Suzuki-Utsunomiya K., Kunita R., Yanagisawa Y.,
RA Showguchi-Miyata J., Mizumura H., Ikeda J.-E.;
RT "ALS2CL, the novel protein highly homologous to the carboxy-terminal half
RT of ALS2, binds to Rab5 and modulates endosome dynamics.";
RL FEBS Lett. 575:64-70(2004).
RN [15]
RP FUNCTION, AND INTERACTION WITH RUFY1.
RX PubMed=14617813; DOI=10.1091/mbc.e03-05-0343;
RA Fouraux M.A., Deneka M., Ivan V., van der Heijden A., Raymackers J.,
RA van Suylekom D., van Venrooij W.J., van der Sluijs P., Pruijn G.J.M.;
RT "Rabip4' is an effector of rab5 and rab4 and regulates transport through
RT early endosomes.";
RL Mol. Biol. Cell 15:611-624(2004).
RN [16]
RP FUNCTION, AND MUTAGENESIS OF GLN-79.
RX PubMed=14978216; DOI=10.1091/mbc.e03-07-0493;
RA Gauthier-Campbell C., Bredt D.S., Murphy T.H., El-Husseini A.;
RT "Regulation of dendritic branching and filopodia formation in hippocampal
RT neurons by specific acylated protein motifs.";
RL Mol. Biol. Cell 15:2205-2217(2004).
RN [17]
RP INTERACTION WITH ZFYVE20, AND MUTAGENESIS OF GLY-54; ALA-56 AND PHE-57.
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).
RN [18]
RP FUNCTION, AND INTERACTION WITH GAPVD1.
RX PubMed=16410077; DOI=10.1016/j.bbrc.2005.12.099;
RA Hunker C.M., Galvis A., Kruk I., Giambini H., Veisaga M.L., Barbieri M.A.;
RT "Rab5-activating protein 6, a novel endosomal protein with a role in
RT endocytosis.";
RL Biochem. Biophys. Res. Commun. 340:967-975(2006).
RN [19]
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 [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [21]
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 [22]
RP INTERACTION WITH CLN5, AND SUBCELLULAR LOCATION.
RX PubMed=22431521; DOI=10.1128/mcb.06726-11;
RA Mamo A., Jules F., Dumaresq-Doiron K., Costantino S., Lefrancois S.;
RT "The role of ceroid lipofuscinosis neuronal protein 5 (CLN5) in endosomal
RT sorting.";
RL Mol. Cell. Biol. 32:1855-1866(2012).
RN [23]
RP FUNCTION.
RX PubMed=22660413; DOI=10.1038/ncb2502;
RA Baietti M.F., Zhang Z., Mortier E., Melchior A., Degeest G., Geeraerts A.,
RA Ivarsson Y., Depoortere F., Coomans C., Vermeiren E., Zimmermann P.,
RA David G.;
RT "Syndecan-syntenin-ALIX regulates the biogenesis of exosomes.";
RL Nat. Cell Biol. 14:677-685(2012).
RN [24]
RP SUBCELLULAR LOCATION.
RX PubMed=23382462; DOI=10.1083/jcb.201209113;
RA Bluemer J., Rey J., Dehmelt L., Mazel T., Wu Y.W., Bastiaens P.,
RA Goody R.S., Itzen A.;
RT "RabGEFs are a major determinant for specific Rab membrane targeting.";
RL J. Cell Biol. 200:287-300(2013).
RN [25]
RP INTERACTION WITH GDI1, AND SUBCELLULAR LOCATION.
RX PubMed=23815289; DOI=10.3109/09687688.2013.818725;
RA Kirsten M.L., Baron R.A., Seabra M.C., Ces O.;
RT "Rab1a and Rab5a preferentially bind to binary lipid compositions with
RT higher stored curvature elastic energy.";
RL Mol. Membr. Biol. 30:303-314(2013).
RN [26]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH OCRL.
RX PubMed=25869668; DOI=10.1083/jcb.201409064;
RA Nakatsu F., Messa M., Nandez R., Czapla H., Zou Y., Strittmatter S.M.,
RA De Camilli P.;
RT "Sac2/INPP5F is an inositol 4-phosphatase that functions in the endocytic
RT pathway.";
RL J. Cell Biol. 209:85-95(2015).
RN [27]
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 [28]
RP INTERACTION WITH GDI1 AND GDI2, PHOSPHORYLATION AT SER-84, AND MUTAGENESIS
RP OF SER-84.
RX PubMed=29125462; DOI=10.7554/elife.31012;
RA Steger M., Diez F., Dhekne H.S., Lis P., Nirujogi R.S., Karayel O.,
RA Tonelli F., Martinez T.N., Lorentzen E., Pfeffer S.R., Alessi D.R.,
RA Mann M.;
RT "Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation
RT establishes a connection to ciliogenesis.";
RL Elife 6:0-0(2017).
RN [29]
RP GLYCOSYLATION AT ARG-120 (MICROBIAL INFECTION).
RX PubMed=32974215; DOI=10.3389/fcimb.2020.00419;
RA Gan J., Scott N.E., Newson J.P.M., Wibawa R.R., Wong Fok Lung T.,
RA Pollock G.L., Ng G.Z., van Driel I., Pearson J.S., Hartland E.L.,
RA Giogha C.;
RT "The Salmonella effector SseK3 targets small Rab GTPases.";
RL Front. Cell. Infect. Microbiol. 10:419-419(2020).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX PubMed=12433916; DOI=10.1074/jbc.m211042200;
RA Zhu G., Liu J., Terzyan S., Zhai P., Li G., Zhang X.C.;
RT "High resolution crystal structures of human Rab5a and five mutants with
RT substitutions in the catalytically important phosphate-binding loop.";
RL J. Biol. Chem. 278:2452-2460(2003).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 15-184 IN COMPLEX WITH GTP
RP ANALOG.
RX PubMed=14684892; DOI=10.1107/s0907444903021632;
RA Terzyan S., Zhu G., Li G., Zhang X.C.;
RT "Refinement of the structure of human Rab5a GTPase domain at 1.05 A
RT resolution.";
RL Acta Crystallogr. D 60:54-60(2004).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 15-184 IN COMPLEX WITH GTP ANALOG;
RP GDP AND RABEP1, FUNCTION, INTERACTION WITH RABEP1, MUTAGENESIS OF PHE-57;
RP TRP-74; GLN-79; TYR-82; TYR-89; LYS-116 AND ARG-120, AND CATALYTIC
RP ACTIVITY.
RX PubMed=15378032; DOI=10.1038/nsmb832;
RA Zhu G., Zhai P., Liu J., Terzyan S., Li G., Zhang X.C.;
RT "Structural basis of Rab5-Rabaptin5 interaction in endocytosis.";
RL Nat. Struct. Mol. Biol. 11:975-983(2004).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 16-183 OF MUTANT LEU-79 IN
RP COMPLEX WITH EEA1, AND INTERACTION WITH EEA1.
RX PubMed=20534488; DOI=10.1073/pnas.1000843107;
RA Mishra A., Eathiraj S., Corvera S., Lambright D.G.;
RT "Structural basis for Rab GTPase recognition and endosome tethering by the
RT C2H2 zinc finger of early endosomal autoantigen 1 (EEA1).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10866-10871(2010).
CC -!- FUNCTION: Small GTPase which cycles between active GTP-bound and
CC inactive GDP-bound states. In its active state, binds to a variety of
CC effector proteins to regulate cellular responses such as of
CC intracellular membrane trafficking, from the formation of transport
CC vesicles to their fusion with membranes. Active GTP-bound form is able
CC to recruit to membranes different sets of downstream effectors directly
CC responsible for vesicle formation, movement, tethering and fusion.
CC RAB5A is required for the fusion of plasma membranes and early
CC endosomes (PubMed:10818110, PubMed:14617813, PubMed:16410077,
CC PubMed:15378032). Contributes to the regulation of filopodia extension
CC (PubMed:14978216). Required for the exosomal release of SDCBP, CD63,
CC PDCD6IP and syndecan (PubMed:22660413). Regulates maturation of
CC apoptotic cell-containing phagosomes, probably downstream of DYN2 and
CC PIK3C3 (By similarity). {ECO:0000250|UniProtKB:Q9CQD1,
CC ECO:0000269|PubMed:10818110, ECO:0000269|PubMed:14617813,
CC ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:15378032,
CC ECO:0000269|PubMed:16410077, ECO:0000269|PubMed:22660413}.
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:0000269|PubMed:15378032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000305|PubMed:15378032};
CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC (GEFs) which promote the exchange of bound GDP for free GTP.
CC {ECO:0000250|UniProtKB:P18066}.
CC -!- SUBUNIT: Interacts with SGSM1 and SGSM3 (By similarity). Interacts with
CC PIK3CB (By similarity). Interacts with GDI1; this promotes dissociation
CC from membranes; phosphorylation at Ser-84 disrupts this interaction
CC (PubMed:23815289, PubMed:29125462). Interacts with GDI2;
CC phosphorylation at Ser-84 disrupts the interaction (PubMed:29125462).
CC Interacts with EEA1 (PubMed:10491193, PubMed:20534488). Interacts with
CC RIN1 and GAPVD1, which regulate its pathway, probably by acting as a
CC GEF (PubMed:11703925, PubMed:16410077). Interacts with RINL. Interacts
CC with ALS2CL, SUN2, ZFYVE20 and RUFY1 (PubMed:10818110, PubMed:11062261,
CC PubMed:15388334, PubMed:14617813, PubMed:16034420). Interacts with
CC RABEP1; one RABEP1 homodimer binds two RAB5A chains, but at opposite
CC sides of the dimer (PubMed:15378032). Interacts with OCRL
CC (PubMed:25869668). Interacts with INPP5F. May be a component of a
CC complex composed of RAB5A, DYN2 and PIK3C3 (By similarity). Does not
CC interact with BLOC-3 complex (heterodimer of HPS1 and HPS4) (By
CC similarity). Interacts with CLN5 (PubMed:22431521). Interacts with
CC APPL2 (By similarity). Interacts with F8A1/F8A2/F8A3 (By similarity).
CC Found in a complex with F8A1/F8A2/F8A3, HTT and RAB5A; mediates the
CC recruitment of HTT by RAB5A onto early endosomes (By similarity).
CC {ECO:0000250|UniProtKB:P18066, ECO:0000250|UniProtKB:Q0IIG7,
CC ECO:0000250|UniProtKB:Q9CQD1, ECO:0000269|PubMed:10491193,
CC ECO:0000269|PubMed:10818110, ECO:0000269|PubMed:11062261,
CC ECO:0000269|PubMed:11703925, ECO:0000269|PubMed:14617813,
CC ECO:0000269|PubMed:14684892, ECO:0000269|PubMed:15378032,
CC ECO:0000269|PubMed:15388334, ECO:0000269|PubMed:16034420,
CC ECO:0000269|PubMed:16410077, ECO:0000269|PubMed:20534488,
CC ECO:0000269|PubMed:22431521, ECO:0000269|PubMed:23815289,
CC ECO:0000269|PubMed:25869668, ECO:0000269|PubMed:29125462}.
CC -!- INTERACTION:
CC P20339; Q96Q42: ALS2; NbExp=2; IntAct=EBI-399437, EBI-1044902;
CC P20339; Q9P2R3: ANKFY1; NbExp=2; IntAct=EBI-399437, EBI-2513908;
CC P20339; Q9UKG1: APPL1; NbExp=23; IntAct=EBI-399437, EBI-741243;
CC P20339; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-399437, EBI-747505;
CC P20339; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-399437, EBI-1383687;
CC P20339; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-399437, EBI-744556;
CC P20339; Q9Y3D0: CIAO2B; NbExp=3; IntAct=EBI-399437, EBI-744045;
CC P20339; Q15075: EEA1; NbExp=4; IntAct=EBI-399437, EBI-298113;
CC P20339; O15287: FANCG; NbExp=3; IntAct=EBI-399437, EBI-81610;
CC P20339; P14136: GFAP; NbExp=3; IntAct=EBI-399437, EBI-744302;
CC P20339; Q0VD86: INCA1; NbExp=3; IntAct=EBI-399437, EBI-6509505;
CC P20339; Q6IAA8: LAMTOR1; NbExp=3; IntAct=EBI-399437, EBI-715385;
CC P20339; Q6ZQX7-4: LIAT1; NbExp=3; IntAct=EBI-399437, EBI-25830459;
CC P20339; Q9NS73-5: MBIP; NbExp=3; IntAct=EBI-399437, EBI-10182361;
CC P20339; Q01968: OCRL; NbExp=11; IntAct=EBI-399437, EBI-6148898;
CC P20339; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-399437, EBI-10171633;
CC P20339; Q9UH99: SUN2; NbExp=5; IntAct=EBI-399437, EBI-1044964;
CC P20339; Q9H7C4: SYNC; NbExp=3; IntAct=EBI-399437, EBI-11285923;
CC P20339; O60506-4: SYNCRIP; NbExp=3; IntAct=EBI-399437, EBI-11123832;
CC P20339; O15273: TCAP; NbExp=3; IntAct=EBI-399437, EBI-954089;
CC P20339; P15923-3: TCF3; NbExp=3; IntAct=EBI-399437, EBI-12000326;
CC P20339; P17024: ZNF20; NbExp=3; IntAct=EBI-399437, EBI-717634;
CC P20339; P23727: PIK3R1; Xeno; NbExp=5; IntAct=EBI-399437, EBI-520244;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23815289};
CC Lipid-anchor {ECO:0000305|PubMed:7991565}; Cytoplasmic side
CC {ECO:0000269|PubMed:23382462}. Early endosome membrane
CC {ECO:0000269|PubMed:23815289, ECO:0000269|PubMed:25869668}; Lipid-
CC anchor {ECO:0000305|PubMed:7991565}. Melanosome
CC {ECO:0000269|PubMed:17081065}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:10818110}. Cell projection, ruffle
CC {ECO:0000250|UniProtKB:P18066}. Membrane {ECO:0000269|PubMed:23815289}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:23382462}. Cytoplasmic vesicle,
CC phagosome membrane {ECO:0000250|UniProtKB:Q9CQD1}. Endosome membrane
CC {ECO:0000269|PubMed:22431521, ECO:0000269|PubMed:23382462}.
CC Note=Enriched in stage I melanosomes (PubMed:17081065). Alternates
CC between membrane-bound and cytosolic forms (Probable).
CC {ECO:0000269|PubMed:17081065, ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P20339-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P20339-2; Sequence=VSP_055830;
CC -!- PTM: Phosphorylation of Ser-84 in the switch II region by LRRK2
CC prevents the association of RAB regulatory proteins, including RAB GDP
CC dissociation inhibitors GDI1 and GDI2. {ECO:0000269|PubMed:29125462}.
CC -!- PTM: (Microbial infection) Glycosylated on arginine residues by
CC S.typhimurium protein Ssek3. {ECO:0000269|PubMed:32974215}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; M28215; AAA60245.1; -; mRNA.
DR EMBL; AF464088; AAO15677.1; -; mRNA.
DR EMBL; AF498936; AAM21084.1; -; mRNA.
DR EMBL; AK295992; BAG58767.1; -; mRNA.
DR EMBL; AK312618; BAG35504.1; -; mRNA.
DR EMBL; CR536492; CAG38731.1; -; mRNA.
DR EMBL; AC097635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW64301.1; -; Genomic_DNA.
DR EMBL; BC001267; AAH01267.1; -; mRNA.
DR EMBL; BC018288; AAH18288.1; -; mRNA.
DR CCDS; CCDS2633.1; -. [P20339-1]
DR CCDS; CCDS77710.1; -. [P20339-2]
DR PIR; F34323; F34323.
DR RefSeq; NP_001278977.1; NM_001292048.1. [P20339-2]
DR RefSeq; NP_004153.2; NM_004162.4. [P20339-1]
DR PDB; 1N6H; X-ray; 1.51 A; A=15-184.
DR PDB; 1N6I; X-ray; 1.60 A; A=15-184.
DR PDB; 1N6K; X-ray; 1.55 A; A=15-184.
DR PDB; 1N6L; X-ray; 1.60 A; A=15-184.
DR PDB; 1N6N; X-ray; 1.60 A; A=15-184.
DR PDB; 1N6O; X-ray; 1.80 A; A=15-184.
DR PDB; 1N6P; X-ray; 1.54 A; A=15-184.
DR PDB; 1N6R; X-ray; 1.55 A; A=15-184.
DR PDB; 1R2Q; X-ray; 1.05 A; A=15-184.
DR PDB; 1TU3; X-ray; 2.31 A; A/B/C/D/E=15-184.
DR PDB; 1TU4; X-ray; 2.20 A; A/B/C/D=15-184.
DR PDB; 3MJH; X-ray; 2.03 A; A/C=16-183.
DR PDB; 4Q9U; X-ray; 4.62 A; B/F=15-184.
DR PDB; 7BL1; EM; 9.80 A; DDD=16-183.
DR PDBsum; 1N6H; -.
DR PDBsum; 1N6I; -.
DR PDBsum; 1N6K; -.
DR PDBsum; 1N6L; -.
DR PDBsum; 1N6N; -.
DR PDBsum; 1N6O; -.
DR PDBsum; 1N6P; -.
DR PDBsum; 1N6R; -.
DR PDBsum; 1R2Q; -.
DR PDBsum; 1TU3; -.
DR PDBsum; 1TU4; -.
DR PDBsum; 3MJH; -.
DR PDBsum; 4Q9U; -.
DR PDBsum; 7BL1; -.
DR AlphaFoldDB; P20339; -.
DR SMR; P20339; -.
DR BioGRID; 111806; 691.
DR CORUM; P20339; -.
DR DIP; DIP-380N; -.
DR IntAct; P20339; 258.
DR MINT; P20339; -.
DR STRING; 9606.ENSP00000273047; -.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR DrugBank; DB04137; Guanosine-5'-Triphosphate.
DR DrugBank; DB02467; L-methionine (S)-S-oxide.
DR iPTMnet; P20339; -.
DR MetOSite; P20339; -.
DR PhosphoSitePlus; P20339; -.
DR SwissPalm; P20339; -.
DR BioMuta; RAB5A; -.
DR DMDM; 1346958; -.
DR EPD; P20339; -.
DR jPOST; P20339; -.
DR MassIVE; P20339; -.
DR MaxQB; P20339; -.
DR PaxDb; P20339; -.
DR PeptideAtlas; P20339; -.
DR PRIDE; P20339; -.
DR ProteomicsDB; 4362; -.
DR ProteomicsDB; 53751; -. [P20339-1]
DR TopDownProteomics; P20339-1; -. [P20339-1]
DR Antibodypedia; 3882; 780 antibodies from 41 providers.
DR DNASU; 5868; -.
DR Ensembl; ENST00000273047.9; ENSP00000273047.4; ENSG00000144566.11. [P20339-1]
DR Ensembl; ENST00000422242.1; ENSP00000411941.1; ENSG00000144566.11. [P20339-2]
DR GeneID; 5868; -.
DR KEGG; hsa:5868; -.
DR MANE-Select; ENST00000273047.9; ENSP00000273047.4; NM_004162.5; NP_004153.2.
DR UCSC; uc003cbn.4; human. [P20339-1]
DR CTD; 5868; -.
DR DisGeNET; 5868; -.
DR GeneCards; RAB5A; -.
DR HGNC; HGNC:9783; RAB5A.
DR HPA; ENSG00000144566; Low tissue specificity.
DR MIM; 179512; gene.
DR neXtProt; NX_P20339; -.
DR OpenTargets; ENSG00000144566; -.
DR PharmGKB; PA34143; -.
DR VEuPathDB; HostDB:ENSG00000144566; -.
DR eggNOG; KOG0092; Eukaryota.
DR GeneTree; ENSGT00940000154337; -.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; P20339; -.
DR OMA; DGIDCAE; -.
DR PhylomeDB; P20339; -.
DR TreeFam; TF300199; -.
DR PathwayCommons; P20339; -.
DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Reactome; R-HSA-9636383; Prevention of phagosomal-lysosomal fusion.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; P20339; -.
DR SIGNOR; P20339; -.
DR BioGRID-ORCS; 5868; 26 hits in 1086 CRISPR screens.
DR ChiTaRS; RAB5A; human.
DR EvolutionaryTrace; P20339; -.
DR GeneWiki; RAB5A; -.
DR GenomeRNAi; 5868; -.
DR Pharos; P20339; Tbio.
DR PRO; PR:P20339; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P20339; protein.
DR Bgee; ENSG00000144566; Expressed in gingival epithelium and 208 other tissues.
DR ExpressionAtlas; P20339; baseline and differential.
DR Genevisible; P20339; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0030424; C:axon; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043679; C:axon terminus; ISS:ParkinsonsUK-UCL.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0098559; C:cytoplasmic side of early endosome membrane; IMP:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR GO; GO:0032009; C:early phagosome; ISS:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; ISS:ParkinsonsUK-UCL.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098842; C:postsynaptic early endosome; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0036477; C:somatodendritic compartment; IDA:ParkinsonsUK-UCL.
DR GO; GO:0008021; C:synaptic vesicle; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043195; C:terminal bouton; IDA:ParkinsonsUK-UCL.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
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:0150093; P:amyloid-beta clearance by transcytosis; IGI:ARUK-UCL.
DR GO; GO:0045022; P:early endosome to late endosome transport; IMP:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0044788; P:modulation by host of viral process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR GO; GO:0045921; P:positive regulation of exocytosis; IMP:UniProtKB.
DR GO; GO:2000286; P:receptor internalization involved in canonical Wnt signaling pathway; IMP:BHF-UCL.
DR GO; GO:2000785; P:regulation of autophagosome assembly; TAS:ParkinsonsUK-UCL.
DR GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
DR GO; GO:0051036; P:regulation of endosome size; IMP:UniProtKB.
DR GO; GO:0051489; P:regulation of filopodium assembly; IDA:UniProtKB.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IBA:GO_Central.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IMP:ParkinsonsUK-UCL.
DR GO; GO:0036465; P:synaptic vesicle recycling; IDA:ParkinsonsUK-UCL.
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; Alternative splicing; Cell membrane; Cell projection;
KW Cytoplasm; Cytoplasmic vesicle; Endocytosis; Endosome; Glycoprotein;
KW GTP-binding; Hydrolase; Lipoprotein; Membrane; Nucleotide-binding;
KW Phagocytosis; Phosphoprotein; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..215
FT /note="Ras-related protein Rab-5A"
FT /id="PRO_0000121104"
FT REGION 181..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 49..57
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 27..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:12433916,
FT ECO:0000269|PubMed:14684892, ECO:0000269|PubMed:15378032,
FT ECO:0000269|PubMed:20534488, ECO:0007744|PDB:1N6H,
FT ECO:0007744|PDB:1N6L, ECO:0007744|PDB:1N6N,
FT ECO:0007744|PDB:1N6O, ECO:0007744|PDB:1N6P,
FT ECO:0007744|PDB:1N6R, ECO:0007744|PDB:1R2Q,
FT ECO:0007744|PDB:1TU3, ECO:0007744|PDB:3MJH"
FT BINDING 46..52
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:12433916,
FT ECO:0000269|PubMed:14684892, ECO:0000269|PubMed:15378032,
FT ECO:0000269|PubMed:20534488, ECO:0007744|PDB:1N6H,
FT ECO:0007744|PDB:1N6L, ECO:0007744|PDB:1N6N,
FT ECO:0007744|PDB:1N6O, ECO:0007744|PDB:1N6P,
FT ECO:0007744|PDB:1N6R, ECO:0007744|PDB:1R2Q,
FT ECO:0007744|PDB:1TU3, ECO:0007744|PDB:3MJH"
FT BINDING 75..79
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:12433916,
FT ECO:0000269|PubMed:14684892, ECO:0000269|PubMed:15378032,
FT ECO:0000269|PubMed:20534488, ECO:0007744|PDB:1N6H,
FT ECO:0007744|PDB:1N6L, ECO:0007744|PDB:1N6N,
FT ECO:0007744|PDB:1N6O, ECO:0007744|PDB:1N6P,
FT ECO:0007744|PDB:1N6R, ECO:0007744|PDB:1R2Q,
FT ECO:0007744|PDB:1TU3, ECO:0007744|PDB:3MJH"
FT BINDING 133..136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:12433916,
FT ECO:0000269|PubMed:14684892, ECO:0000269|PubMed:15378032,
FT ECO:0000269|PubMed:20534488, ECO:0007744|PDB:1N6H,
FT ECO:0007744|PDB:1N6L, ECO:0007744|PDB:1N6N,
FT ECO:0007744|PDB:1N6O, ECO:0007744|PDB:1N6P,
FT ECO:0007744|PDB:1N6R, ECO:0007744|PDB:1R2Q,
FT ECO:0007744|PDB:1TU3, ECO:0007744|PDB:3MJH"
FT BINDING 163..165
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:12433916,
FT ECO:0000269|PubMed:14684892, ECO:0000269|PubMed:15378032,
FT ECO:0000269|PubMed:20534488, ECO:0007744|PDB:1N6H,
FT ECO:0007744|PDB:1N6L, ECO:0007744|PDB:1N6N,
FT ECO:0007744|PDB:1N6O, ECO:0007744|PDB:1N6P,
FT ECO:0007744|PDB:1N6R, ECO:0007744|PDB:1R2Q,
FT ECO:0007744|PDB:1TU3, ECO:0007744|PDB:3MJH"
FT MOD_RES 84
FT /note="Phosphoserine; by LRRK2"
FT /evidence="ECO:0000269|PubMed:29125462"
FT LIPID 212
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:7991565"
FT LIPID 213
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:7991565"
FT CARBOHYD 120
FT /note="(Microbial infection) N-beta-linked (GlcNAc)
FT arginine"
FT /evidence="ECO:0000269|PubMed:32974215"
FT VAR_SEQ 55..68
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055830"
FT MUTAGEN 54
FT /note="G->Q: Strongly decreases ZFYVE20 binding affinity."
FT /evidence="ECO:0000269|PubMed:16034420"
FT MUTAGEN 56
FT /note="A->E: Strongly decreases ZFYVE20 binding affinity."
FT /evidence="ECO:0000269|PubMed:16034420"
FT MUTAGEN 57
FT /note="F->A: Strongly decreases RABEP1 and ZFYVE20 binding
FT affinity."
FT /evidence="ECO:0000269|PubMed:15378032,
FT ECO:0000269|PubMed:16034420"
FT MUTAGEN 74
FT /note="W->A: Strongly decreases RABEP1 binding affinity."
FT /evidence="ECO:0000269|PubMed:15378032"
FT MUTAGEN 79
FT /note="Q->L: Loss of GTPase activity. Does not inhibit
FT filopodia formation."
FT /evidence="ECO:0000269|PubMed:14978216,
FT ECO:0000269|PubMed:15378032"
FT MUTAGEN 82
FT /note="Y->A: Strongly decreases RABEP1 binding affinity.
FT Impairs endosome fusion."
FT /evidence="ECO:0000269|PubMed:15378032"
FT MUTAGEN 84
FT /note="S->A: Loss of phosphorylation. No effect on GDI1 and
FT GDI2 binding."
FT /evidence="ECO:0000269|PubMed:29125462"
FT MUTAGEN 84
FT /note="S->E: Phosphomimetic mutant. Loss of GDI1 and GDI2
FT binding."
FT /evidence="ECO:0000269|PubMed:29125462"
FT MUTAGEN 89
FT /note="Y->A: Strongly decreases RABEP1 binding affinity."
FT /evidence="ECO:0000269|PubMed:15378032"
FT MUTAGEN 116
FT /note="K->E: No effect on RABEP1 binding affinity."
FT /evidence="ECO:0000269|PubMed:15378032"
FT MUTAGEN 120
FT /note="R->E: No effect on RABEP1 binding affinity."
FT /evidence="ECO:0000269|PubMed:15378032"
FT CONFLICT 81
FT /note="R -> G (in Ref. 1; AAA60245)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="R -> G (in Ref. 1; AAA60245)"
FT /evidence="ECO:0000305"
FT STRAND 17..26
FT /evidence="ECO:0007829|PDB:1R2Q"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:1N6K"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:1R2Q"
FT STRAND 53..64
FT /evidence="ECO:0007829|PDB:1R2Q"
FT STRAND 67..76
FT /evidence="ECO:0007829|PDB:1R2Q"
FT HELIX 80..85
FT /evidence="ECO:0007829|PDB:1R2Q"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:1R2Q"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:1R2Q"
FT HELIX 105..121
FT /evidence="ECO:0007829|PDB:1R2Q"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:1R2Q"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:1R2Q"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:1R2Q"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:1R2Q"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:1R2Q"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:1R2Q"
SQ SEQUENCE 215 AA; 23659 MW; EC03DDF96BBEF821 CRC64;
MASRGATRPN GPNTGNKICQ FKLVLLGESA VGKSSLVLRF VKGQFHEFQE STIGAAFLTQ
TVCLDDTTVK FEIWDTAGQE RYHSLAPMYY RGAQAAIVVY DITNEESFAR AKNWVKELQR
QASPNIVIAL SGNKADLANK RAVDFQEAQS YADDNSLLFM ETSAKTSMNV NEIFMAIAKK
LPKNEPQNPG ANSARGRGVD LTEPTQPTRN QCCSN
