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 27-MAR-2024, entry version 240. 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 INTERACTION WITH ATP9A, AND MUTAGENESIS OF SER-34. RX PubMed=36604604; DOI=10.1038/s41380-022-01940-w; RA Meng T., Chen X., He Z., Huang H., Lin S., Liu K., Bai G., Liu H., Xu M., RA Zhuang H., Zhang Y., Waqas A., Liu Q., Zhang C., Sun X.D., Huang H., RA Umair M., Yan Y., Feng D.; RT "ATP9A deficiency causes ADHD and aberrant endosomal recycling via RT modulating RAB5 and RAB11 activity."; RL Mol. Psychiatry 28:1219-1231(2023). RN [31] 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 [32] 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 [33] 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 [34] 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 Interacts with ATP9A (PubMed:36604604). {ECO:0000250|UniProtKB:P18066, CC ECO:0000250|UniProtKB:Q0IIG7, ECO:0000250|UniProtKB:Q9CQD1, CC ECO:0000269|PubMed:10491193, ECO:0000269|PubMed:10818110, CC ECO:0000269|PubMed:11062261, ECO:0000269|PubMed:11703925, CC ECO:0000269|PubMed:14617813, ECO:0000269|PubMed:14684892, CC ECO:0000269|PubMed:15378032, ECO:0000269|PubMed:15388334, CC ECO:0000269|PubMed:16034420, ECO:0000269|PubMed:16410077, CC ECO:0000269|PubMed:20534488, ECO:0000269|PubMed:22431521, CC ECO:0000269|PubMed:23815289, ECO:0000269|PubMed:25869668, CC ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:36604604}. 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; Q6ZMI0: PPP1R21; NbExp=2; IntAct=EBI-399437, EBI-5235703; 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}. 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; 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 EMDB; EMD-12214; -. DR EMDB; EMD-12237; -. DR EMDB; EMD-12238; -. DR SMR; P20339; -. DR BioGRID; 111806; 703. DR CORUM; P20339; -. DR DIP; DIP-380N; -. DR IntAct; P20339; 264. 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 GlyCosmos; P20339; 1 site, No reported glycans. 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; 9606-ENSP00000273047; -. DR PeptideAtlas; P20339; -. DR ProteomicsDB; 4362; -. DR ProteomicsDB; 53751; -. [P20339-1] DR Pumba; P20339; -. DR TopDownProteomics; P20339-1; -. [P20339-1] DR Antibodypedia; 3882; 838 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 AGR; HGNC:9783; -. 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; RSYADDN; -. DR OrthoDB; 5483572at2759; -. 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 1164 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 210 other cell types or tissues. DR ExpressionAtlas; P20339; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl. 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:0012505; C:endomembrane system; 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; IEA:UniProtKB-SubCell. 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:0060070; P:canonical Wnt signaling pathway; IDA:BHF-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:0031623; P:receptor internalization; IMP:BHF-UCL. DR GO; GO:2000785; P:regulation of autophagosome assembly; TAS:ParkinsonsUK-UCL. 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 CDD; cd01860; Rab5_related; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR001806; Small_GTPase. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR47978; -; 1. DR PANTHER; PTHR47978:SF65; RAB43, MEMBER RAS ONCOGENE FAMILY; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR SMART; SM00176; RAN; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51419; RAB; 1. DR Genevisible; P20339; HS. 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 34 FT /note="S->N: Increased interaction wih ATP9A." FT /evidence="ECO:0000269|PubMed:36604604" 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 //