RAB8A_HUMAN
ID RAB8A_HUMAN Reviewed; 207 AA.
AC P61006; B4DEK7; P24407; Q6FHV5;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Ras-related protein Rab-8A;
DE EC=3.6.5.2 {ECO:0000305|PubMed:19864458};
DE AltName: Full=Oncogene c-mel;
DE Flags: Precursor;
GN Name=RAB8A; Synonyms=MEL, RAB8;
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=8294494; DOI=10.1083/jcb.124.1.101;
RA Zahraoui A., Joberty G., Arpin M., Fontaine J.J., Hellio R., Tavitian A.,
RA Louvard D.;
RT "A small rab GTPase is distributed in cytoplasmic vesicles in non polarized
RT cells but colocalizes with the tight junction marker ZO-1 in polarized
RT epithelial cells.";
RL J. Cell Biol. 124:101-115(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1886711;
RA Nimmo E.R., Sanders P.G., Padua R.A., Hughes D., Williamson R.,
RA Johnson K.J.;
RT "The MEL gene: a new member of the RAB/YPT class of RAS-related genes.";
RL Oncogene 6:1347-1351(1991).
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] (ISOFORM 2).
RC TISSUE=Cerebellum;
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=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [8]
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 [9]
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 [10]
RP ISOPRENYLATION AT CYS-204.
RX PubMed=8375503; DOI=10.1016/0014-5793(93)80897-4;
RA Joberty G., Tavitian A., Zahraoui A.;
RT "Isoprenylation of Rab proteins possessing a C-terminal CaaX motif.";
RL FEBS Lett. 330:323-328(1993).
RN [11]
RP INTERACTION WITH RAB3IP, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=12221131; DOI=10.1091/mbc.e02-03-0143;
RA Hattula K., Furuhjelm J., Arffman A., Peranen J.;
RT "A Rab8-specific GDP/GTP exchange factor is involved in actin remodeling
RT and polarized membrane transport.";
RL Mol. Biol. Cell 13:3268-3280(2002).
RN [12]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH OPTN.
RX PubMed=15837803; DOI=10.1083/jcb.200501162;
RA Sahlender D.A., Roberts R.C., Arden S.D., Spudich G., Taylor M.J.,
RA Luzio J.P., Kendrick-Jones J., Buss F.;
RT "Optineurin links myosin VI to the Golgi complex and is involved in Golgi
RT organization and exocytosis.";
RL J. Cell Biol. 169:285-295(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [14]
RP INTERACTION WITH BIRC6/BRUCE.
RX PubMed=18329369; DOI=10.1016/j.cell.2008.01.012;
RA Pohl C., Jentsch S.;
RT "Final stages of cytokinesis and midbody ring formation are controlled by
RT BRUCE.";
RL Cell 132:832-845(2008).
RN [15]
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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [17]
RP INTERACTION WITH PIFO.
RX PubMed=20643351; DOI=10.1016/j.devcel.2010.06.005;
RA Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B.,
RA Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.;
RT "Pitchfork regulates primary cilia disassembly and left-right asymmetry.";
RL Dev. Cell 19:66-77(2010).
RN [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20890297; DOI=10.1038/ncb2106;
RA Bryant D.M., Datta A., Rodriguez-Fraticelli A.E., Peraenen J.,
RA Martin-Belmonte F., Mostov K.E.;
RT "A molecular network for de novo generation of the apical surface and
RT lumen.";
RL Nat. Cell Biol. 12:1035-1045(2010).
RN [19]
RP SUBCELLULAR LOCATION, INTERACTION WITH EHD1 AND MICALL1, MUTAGENESIS OF
RP THR-22 AND GLN-67, AND CATALYTIC ACTIVITY.
RX PubMed=19864458; DOI=10.1091/mbc.e09-06-0535;
RA Sharma M., Giridharan S.S., Rahajeng J., Naslavsky N., Caplan S.;
RT "MICAL-L1 links EHD1 to tubular recycling endosomes and regulates receptor
RT recycling.";
RL Mol. Biol. Cell 20:5181-5194(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-185, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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 DCDC1, AND SUBCELLULAR LOCATION.
RX PubMed=22159412; DOI=10.1242/jcs.085407;
RA Kaplan A., Reiner O.;
RT "Linking cytoplasmic dynein and transport of Rab8 vesicles to the midbody
RT during cytokinesis by the doublecortin domain-containing 5 protein.";
RL J. Cell Sci. 124:3989-4000(2011).
RN [23]
RP FUNCTION, AND INTERACTION WITH MYO5B.
RX PubMed=21282656; DOI=10.1073/pnas.1010754108;
RA Roland J.T., Bryant D.M., Datta A., Itzen A., Mostov K.E., Goldenring J.R.;
RT "Rab GTPase-Myo5B complexes control membrane recycling and epithelial
RT polarization.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2789-2794(2011).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [25]
RP SUBCELLULAR LOCATION.
RX PubMed=21255211; DOI=10.1111/j.1600-0854.2011.01165.x;
RA Seto S., Tsujimura K., Koide Y.;
RT "Rab GTPases regulating phagosome maturation are differentially recruited
RT to mycobacterial phagosomes.";
RL Traffic 12:407-420(2011).
RN [26]
RP FUNCTION IN CILIOGENESIS, AND SUBCELLULAR LOCATION.
RX PubMed=21844891; DOI=10.1038/cr.2011.134;
RA Chen Y., Wu B., Xu L., Li H., Xia J., Yin W., Li Z., Shi D., Li S., Lin S.,
RA Shu X., Pei D.;
RT "A SNX10/V-ATPase pathway regulates ciliogenesis in vitro and in vivo.";
RL Cell Res. 22:333-345(2012).
RN [27]
RP INTERACTION WITH OCRL.
RX PubMed=22543976; DOI=10.1093/hmg/dds163;
RA Luo N., West C.C., Murga-Zamalloa C.A., Sun L., Anderson R.M., Wells C.D.,
RA Weinreb R.N., Travers J.B., Khanna H., Sun Y.;
RT "OCRL localizes to the primary cilium: a new role for cilia in Lowe
RT syndrome.";
RL Hum. Mol. Genet. 21:3333-3344(2012).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [30]
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 [31]
RP INTERACTION WITH DZIP1.
RX PubMed=25860027; DOI=10.1371/journal.pbio.1002129;
RA Zhang B., Zhang T., Wang G., Wang G., Chi W., Jiang Q., Zhang C.;
RT "GSK3beta-Dzip1-Rab8 cascade regulates ciliogenesis after mitosis.";
RL PLoS Biol. 13:e1002129-e1002129(2015).
RN [32]
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 [33]
RP INTERACTION WITH LRRK2; GDI1; GDI2; CHM; CHML; RABGGTA; RABGGTB; RAB3IP;
RP TBC1D15 AND INPP5B, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-72, AND
RP MUTAGENESIS OF THR-72.
RX PubMed=26824392; DOI=10.7554/elife.12813;
RA Steger M., Tonelli F., Ito G., Davies P., Trost M., Vetter M., Wachter S.,
RA Lorentzen E., Duddy G., Wilson S., Baptista M.A., Fiske B.K., Fell M.J.,
RA Morrow J.A., Reith A.D., Alessi D.R., Mann M.;
RT "Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates
RT a subset of Rab GTPases.";
RL Elife 5:0-0(2016).
RN [34]
RP FUNCTION.
RX PubMed=27103069; DOI=10.15252/embj.201593350;
RA Sellier C., Campanari M.L., Julie Corbier C., Gaucherot A.,
RA Kolb-Cheynel I., Oulad-Abdelghani M., Ruffenach F., Page A., Ciura S.,
RA Kabashi E., Charlet-Berguerand N.;
RT "Loss of C9ORF72 impairs autophagy and synergizes with polyQ Ataxin-2 to
RT induce motor neuron dysfunction and cell death.";
RL EMBO J. 35:1276-1297(2016).
RN [35]
RP INTERACTION WITH GDI1; GDI2; CHM; CHML; RILPL1 AND RILPL2, SUBCELLULAR
RP LOCATION, PHOSPHORYLATION AT THR-72, AND MUTAGENESIS OF THR-72.
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 [36]
RP FUNCTION, INTERACTION WITH RILPL1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP THR-72, AND MUTAGENESIS OF THR-72.
RX PubMed=30398148; DOI=10.7554/elife.40202;
RA Dhekne H.S., Yanatori I., Gomez R.C., Tonelli F., Diez F., Schuele B.,
RA Steger M., Alessi D.R., Pfeffer S.R.;
RT "A pathway for Parkinson's Disease LRRK2 kinase to block primary cilia and
RT Sonic hedgehog signaling in the brain.";
RL Elife 7:0-0(2018).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 6-176 IN COMPLEX WITH OCRL.
RX PubMed=21378754; DOI=10.1038/emboj.2011.60;
RA Hou X., Hagemann N., Schoebel S., Blankenfeldt W., Goody R.S.,
RA Erdmann K.S., Itzen A.;
RT "A structural basis for Lowe syndrome caused by mutations in the Rab-
RT binding domain of OCRL1.";
RL EMBO J. 30:1659-1670(2011).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-207 IN COMPLEX WITH MICALCL,
RP AND INTERACTION WITH MICAL3; MICAL1; EHBP1 AND EHBP1L1.
RX PubMed=27552051; DOI=10.7554/elife.18675;
RA Rai A., Oprisko A., Campos J., Fu Y., Friese T., Itzen A., Goody R.S.,
RA Gazdag E.M., Muller M.P.;
RT "bMERB domains are bivalent Rab8 family effectors evolved by gene
RT duplication.";
RL Elife 5:E18675-E18675(2016).
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 an inactive GDP-bound form
CC and an active GTP-bound form that is able to recruit to membranes
CC different sets of downstream effectors directly responsible for vesicle
CC formation, movement, tethering and fusion. That Rab is involved in
CC polarized vesicular trafficking and neurotransmitter release. Together
CC with RAB11A, RAB3IP, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42
CC and DNMBP promotes transcytosis of PODXL to the apical membrane
CC initiation sites (AMIS), apical surface formation and lumenogenesis
CC (PubMed:20890297). Regulates the compacted morphology of the Golgi
CC (PubMed:26209634). Together with MYO5B and RAB11A participates in
CC epithelial cell polarization (PubMed:21282656). Also involved in
CC membrane trafficking to the cilium and ciliogenesis (PubMed:21844891,
CC PubMed:30398148). Together with MICALL2, may also regulate adherens
CC junction assembly (By similarity). May play a role in insulin-induced
CC transport to the plasma membrane of the glucose transporter GLUT4 and
CC therefore play a role in glucose homeostasis (By similarity). Involved
CC in autophagy (PubMed:27103069). {ECO:0000250|UniProtKB:P35280,
CC ECO:0000250|UniProtKB:P55258, ECO:0000269|PubMed:20890297,
CC ECO:0000269|PubMed:21282656, ECO:0000269|PubMed:21844891,
CC ECO:0000269|PubMed:26209634, ECO:0000269|PubMed:27103069,
CC ECO:0000269|PubMed:30398148}.
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:0000305|PubMed:19864458};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000305|PubMed:19864458};
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 (Probable). Activated in response to insulin
CC (By similarity). {ECO:0000250|UniProtKB:P35280, ECO:0000305}.
CC -!- SUBUNIT: Interacts (GTP-bound form) with MICALL1; regulates RAB8A
CC association with recycling endosomes (By similarity). Interacts with
CC MICALL2; competes with RAB13 and is involved in E-cadherin endocytic
CC recycling (By similarity). Interacts (GTP-bound form) with MICAL1,
CC MICALCL, MICAL3, EHBP1 and EHBP1L1; at least in case of MICAL1,
CC MICALCL, MICAL3 and EHBP1L1 two molecules of RAB8A can bind to one
CC molecule of the effector protein; ternary complexes of RAB8A, RAB13 and
CC either MICAL1 or EHBP1L1 are possible (PubMed:27552051). Interacts with
CC EHD1 (PubMed:19864458). Interacts with MAP4K2 and SYTL4 (By
CC similarity). Interacts with SGSM1 and SGSM3 (By similarity). Interacts
CC with RABIF, RIMS2, RPH3A and RPH3A (By similarity). Interacts with OPTN
CC (PubMed:15837803). Interacts with RAB3IP (PubMed:12221131). Interacts
CC with MYO5B (PubMed:21282656). Interacts with PIFO (PubMed:20643351).
CC Interacts with BIRC6/bruce (PubMed:18329369). Interacts with OCRL
CC (PubMed:22543976, PubMed:21378754). Interacts with AHI1 (By
CC similarity). Interacts with DCDC1 (PubMed:22159412). Interacts with
CC LRRK2; interaction facilitates phosphorylation of Thr-72
CC (PubMed:26824392). Interacts with RAB31P, GDI1, GDI2, CHM, CHML,
CC RABGGTA, RABGGTB, TBC1D15 and INPP5B; these interactions are dependent
CC on Thr-72 not being phosphorylated (PubMed:26824392, PubMed:29125462).
CC Interacts with RILPL1 and RILPL2; these interactions are dependent on
CC the phosphorylation of Thr-72 by LRRK2 (PubMed:29125462,
CC PubMed:30398148). Interacts with DZIP1; prevents inhibition by the GDP-
CC dissociation inhibitor GDI2 (PubMed:25860027).
CC {ECO:0000250|UniProtKB:P55258, ECO:0000269|PubMed:12221131,
CC ECO:0000269|PubMed:15837803, ECO:0000269|PubMed:18329369,
CC ECO:0000269|PubMed:19864458, ECO:0000269|PubMed:20643351,
CC ECO:0000269|PubMed:21282656, ECO:0000269|PubMed:21378754,
CC ECO:0000269|PubMed:22159412, ECO:0000269|PubMed:22543976,
CC ECO:0000269|PubMed:25860027, ECO:0000269|PubMed:26824392,
CC ECO:0000269|PubMed:27552051, ECO:0000269|PubMed:29125462,
CC ECO:0000269|PubMed:30398148}.
CC -!- INTERACTION:
CC P61006; Q5S007: LRRK2; NbExp=7; IntAct=EBI-722293, EBI-5323863;
CC P61006; Q01968: OCRL; NbExp=15; IntAct=EBI-722293, EBI-6148898;
CC P61006; Q96CV9: OPTN; NbExp=4; IntAct=EBI-722293, EBI-748974;
CC P61006; Q96QF0: RAB3IP; NbExp=5; IntAct=EBI-722293, EBI-747844;
CC P61006; Q96QF0-2: RAB3IP; NbExp=2; IntAct=EBI-722293, EBI-747865;
CC P61006; P47224: RABIF; NbExp=6; IntAct=EBI-722293, EBI-713992;
CC P61006; Q5EBL4: RILPL1; NbExp=2; IntAct=EBI-722293, EBI-2797110;
CC P61006; Q969X0: RILPL2; NbExp=8; IntAct=EBI-722293, EBI-717552;
CC P61006; O60271: SPAG9; NbExp=3; IntAct=EBI-722293, EBI-1023301;
CC P61006; Q5ZWZ3: lpg0940; Xeno; NbExp=3; IntAct=EBI-722293, EBI-6417967;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26824392,
CC ECO:0000305|PubMed:12221131}; Lipid-anchor
CC {ECO:0000305|PubMed:12221131}; Cytoplasmic side
CC {ECO:0000305|PubMed:12221131}. Golgi apparatus
CC {ECO:0000269|PubMed:15837803}. Recycling endosome membrane
CC {ECO:0000269|PubMed:19864458}. Cell projection, cilium
CC {ECO:0000269|PubMed:21844891, ECO:0000269|PubMed:29125462}. Cytoplasmic
CC vesicle, phagosome {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle,
CC phagosome membrane {ECO:0000250|UniProtKB:Q92930}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q92930}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q92930}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:P55258}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:30398148}. Midbody
CC {ECO:0000269|PubMed:22159412}. Cytoplasm {ECO:0000269|PubMed:26824392}.
CC Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:30398148}.
CC Note=Colocalizes with OPTN at the Golgi complex and in vesicular
CC structures close to the plasma membrane (PubMed:15837803). In the GDP-
CC bound form, present in the perinuclear region (PubMed:12221131). Shows
CC a polarized distribution to distal regions of cell protrusions in the
CC GTP-bound form (PubMed:12221131). Colocalizes with PARD3, PRKCI, EXOC5,
CC OCLN, PODXL and RAB11A in apical membrane initiation sites (AMIS)
CC during the generation of apical surface and lumenogenesis
CC (PubMed:20890297). Localizes to tubular recycling endosome
CC (PubMed:19864458). Recruited to phagosomes containing S.aureus or
CC M.tuberculosis (PubMed:21255211). Non-phosphorylated RAB8A
CC predominantly localizes to the cytoplasm whereas phosphorylated RAB8A
CC localizes to the membrane (PubMed:26824392, PubMed:29125462,
CC PubMed:30398148). {ECO:0000269|PubMed:12221131,
CC ECO:0000269|PubMed:15837803, ECO:0000269|PubMed:19864458,
CC ECO:0000269|PubMed:20890297, ECO:0000269|PubMed:21255211,
CC ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:29125462,
CC ECO:0000269|PubMed:30398148}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P61006-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61006-2; Sequence=VSP_056399;
CC -!- PTM: Phosphorylation of Thr-72 in the switch II region by LRRK2
CC prevents the association of RAB regulatory proteins, including CHM,
CC CHML and RAB GDP dissociation inhibitors GDI1 and GDI2.
CC {ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:29125462}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; X56741; CAA40065.1; -; mRNA.
DR EMBL; S53268; AAB19681.1; -; mRNA.
DR EMBL; AF498943; AAM21091.1; -; mRNA.
DR EMBL; BT007184; AAP35848.1; -; mRNA.
DR EMBL; AK293676; BAG57118.1; -; mRNA.
DR EMBL; CR536583; CAG38820.1; -; mRNA.
DR EMBL; AC008894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR542274; CAG47070.1; -; mRNA.
DR EMBL; CH471106; EAW84526.1; -; Genomic_DNA.
DR EMBL; BC002977; AAH02977.1; -; mRNA.
DR CCDS; CCDS12339.1; -. [P61006-1]
DR PIR; B49647; B49647.
DR RefSeq; NP_005361.2; NM_005370.4. [P61006-1]
DR PDB; 3QBT; X-ray; 2.00 A; A/C/E/G=6-176.
DR PDB; 3TNF; X-ray; 2.50 A; A=6-176.
DR PDB; 4LHV; X-ray; 1.95 A; A/B/C/D/E=6-176.
DR PDB; 4LHW; X-ray; 1.55 A; A/B/C/D/E=6-176.
DR PDB; 4LHX; X-ray; 3.05 A; A/B=1-184.
DR PDB; 4LHY; X-ray; 3.10 A; A/B=1-184.
DR PDB; 4LHZ; X-ray; 3.20 A; A/B=1-184.
DR PDB; 4LI0; X-ray; 3.30 A; A/B=1-184.
DR PDB; 5SZI; X-ray; 2.85 A; A=1-207.
DR PDB; 6RIR; X-ray; 1.77 A; A/B=1-181.
DR PDB; 6SQ2; X-ray; 1.68 A; A/B=1-181.
DR PDB; 6STF; X-ray; 2.40 A; A/B/C/D/E=5-176.
DR PDB; 6STG; X-ray; 2.50 A; A/B=5-176.
DR PDB; 6WHE; X-ray; 1.73 A; A/B=1-181.
DR PDB; 6YX5; X-ray; 2.14 A; A=6-176.
DR PDB; 6ZSI; X-ray; 1.91 A; A/B=1-176.
DR PDB; 6ZSJ; X-ray; 2.00 A; A/B=1-176.
DR PDB; 7BWT; X-ray; 2.30 A; B=2-183.
DR PDB; 7LWB; X-ray; 1.90 A; A=1-181.
DR PDBsum; 3QBT; -.
DR PDBsum; 3TNF; -.
DR PDBsum; 4LHV; -.
DR PDBsum; 4LHW; -.
DR PDBsum; 4LHX; -.
DR PDBsum; 4LHY; -.
DR PDBsum; 4LHZ; -.
DR PDBsum; 4LI0; -.
DR PDBsum; 5SZI; -.
DR PDBsum; 6RIR; -.
DR PDBsum; 6SQ2; -.
DR PDBsum; 6STF; -.
DR PDBsum; 6STG; -.
DR PDBsum; 6WHE; -.
DR PDBsum; 6YX5; -.
DR PDBsum; 6ZSI; -.
DR PDBsum; 6ZSJ; -.
DR PDBsum; 7BWT; -.
DR PDBsum; 7LWB; -.
DR AlphaFoldDB; P61006; -.
DR SMR; P61006; -.
DR BioGRID; 110382; 183.
DR CORUM; P61006; -.
DR DIP; DIP-43703N; -.
DR IntAct; P61006; 105.
DR MINT; P61006; -.
DR STRING; 9606.ENSP00000300935; -.
DR GlyGen; P61006; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61006; -.
DR PhosphoSitePlus; P61006; -.
DR SwissPalm; P61006; -.
DR BioMuta; RAB8A; -.
DR DMDM; 46810392; -.
DR EPD; P61006; -.
DR jPOST; P61006; -.
DR MassIVE; P61006; -.
DR MaxQB; P61006; -.
DR PaxDb; P61006; -.
DR PeptideAtlas; P61006; -.
DR PRIDE; P61006; -.
DR ProteomicsDB; 57245; -. [P61006-1]
DR Antibodypedia; 27297; 294 antibodies from 37 providers.
DR DNASU; 4218; -.
DR Ensembl; ENST00000300935.8; ENSP00000300935.2; ENSG00000167461.12. [P61006-1]
DR Ensembl; ENST00000586682.1; ENSP00000467501.1; ENSG00000167461.12. [P61006-2]
DR GeneID; 4218; -.
DR KEGG; hsa:4218; -.
DR MANE-Select; ENST00000300935.8; ENSP00000300935.2; NM_005370.5; NP_005361.2.
DR UCSC; uc002ndn.5; human. [P61006-1]
DR CTD; 4218; -.
DR DisGeNET; 4218; -.
DR GeneCards; RAB8A; -.
DR HGNC; HGNC:7007; RAB8A.
DR HPA; ENSG00000167461; Low tissue specificity.
DR MIM; 165040; gene.
DR neXtProt; NX_P61006; -.
DR OpenTargets; ENSG00000167461; -.
DR PharmGKB; PA30743; -.
DR VEuPathDB; HostDB:ENSG00000167461; -.
DR eggNOG; KOG0078; Eukaryota.
DR GeneTree; ENSGT00940000157246; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; P61006; -.
DR OMA; SKMEQNE; -.
DR OrthoDB; 1426655at2759; -.
DR PhylomeDB; P61006; -.
DR TreeFam; TF314097; -.
DR BRENDA; 3.6.5.2; 2681.
DR PathwayCommons; P61006; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-5620916; VxPx cargo-targeting to cilium.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; P61006; -.
DR SIGNOR; P61006; -.
DR BioGRID-ORCS; 4218; 17 hits in 1088 CRISPR screens.
DR ChiTaRS; RAB8A; human.
DR GeneWiki; RAB8A; -.
DR GenomeRNAi; 4218; -.
DR Pharos; P61006; Tbio.
DR PRO; PR:P61006; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P61006; protein.
DR Bgee; ENSG00000167461; Expressed in monocyte and 210 other tissues.
DR ExpressionAtlas; P61006; baseline and differential.
DR Genevisible; P61006; HS.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0097546; C:ciliary base; IEA:Ensembl.
DR GO; GO:0060170; C:ciliary membrane; IEA:Ensembl.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0097730; C:non-motile cilium; IDA:BHF-UCL.
DR GO; GO:0045335; C:phagocytic vesicle; IDA: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:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IBA:GO_Central.
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:0031489; F:myosin V binding; IPI:UniProtKB.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IDA:BHF-UCL.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0048210; P:Golgi vesicle fusion to target membrane; IDA:BHF-UCL.
DR GO; GO:0098969; P:neurotransmitter receptor transport to postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0061512; P:protein localization to cilium; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0010506; P:regulation of autophagy; IMP:UniProtKB.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
DR GO; GO:0051223; P:regulation of protein transport; IEA:Ensembl.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IDA:BHF-UCL.
DR GO; GO:0099003; P:vesicle-mediated transport in synapse; IEA:Ensembl.
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; Autophagy; Cell membrane;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Endosome; Golgi apparatus; GTP-binding;
KW Hydrolase; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Phosphoprotein; Prenylation; Protein transport; Proto-oncogene;
KW Reference proteome; Transport.
FT CHAIN 1..204
FT /note="Ras-related protein Rab-8A"
FT /id="PRO_0000121130"
FT PROPEP 205..207
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370793"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 17..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:27552051,
FT ECO:0007744|PDB:5SZI"
FT BINDING 34..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:27552051,
FT ECO:0007744|PDB:5SZI"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9H0U4,
FT ECO:0000269|PubMed:27552051, ECO:0007744|PDB:5SZI"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:27552051,
FT ECO:0007744|PDB:5SZI"
FT BINDING 152..154
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9H0U4,
FT ECO:0000269|PubMed:27552051, ECO:0007744|PDB:5SZI"
FT MOD_RES 72
FT /note="Phosphothreonine; by LRRK2"
FT /evidence="ECO:0000269|PubMed:26824392,
FT ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:30398148"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 204
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 204
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:8375503"
FT VAR_SEQ 161..205
FT /note="AFFTLARDIKAKMDKKLEGNSPQGSNQGVKITPDQQKRSSFFRCV -> RYQ
FT SKNGQKIGRQQPPGEQPGSQNHTGPAEEEQLFPMCSSVRNTA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056399"
FT MUTAGEN 22
FT /note="T->N: Loss of interaction with MICALL1."
FT /evidence="ECO:0000269|PubMed:19864458"
FT MUTAGEN 67
FT /note="Q->L: Probable constitutively active mutant locked
FT in the active GTP-bound form. Stimulates interaction with
FT MICALL1."
FT /evidence="ECO:0000269|PubMed:19864458"
FT MUTAGEN 72
FT /note="T->A: Loss of phosphorylation. No effect on the
FT binding of GDP or GTP. Localizes primarily to the Golgi
FT complex but does not affect membrane localization."
FT /evidence="ECO:0000269|PubMed:26824392,
FT ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:30398148"
FT MUTAGEN 72
FT /note="T->E: Phosphomimetic mutant. No effect on the
FT binding of GDP or GTP. Loss of GDI1, GDI2, CHM, CHML,
FT RABGGTA, RABGGTB, RAB3IP, TBC1D15, and INPP5B binding.
FT Increases localization to the cell membrane."
FT /evidence="ECO:0000269|PubMed:26824392,
FT ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:30398148"
FT CONFLICT 177..183
FT /note="LEGNSPQ -> WKATAP (in Ref. 2; AAB19681)"
FT /evidence="ECO:0000305"
FT STRAND 7..14
FT /evidence="ECO:0007829|PDB:4LHW"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:4LHW"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:7BWT"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:4LHX"
FT STRAND 42..52
FT /evidence="ECO:0007829|PDB:4LHW"
FT STRAND 55..64
FT /evidence="ECO:0007829|PDB:4LHW"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:6STF"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:4LHW"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:4LHW"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:4LHW"
FT HELIX 93..97
FT /evidence="ECO:0007829|PDB:4LHW"
FT HELIX 99..109
FT /evidence="ECO:0007829|PDB:4LHW"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:4LHW"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:4LHX"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:4LHW"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:4LHW"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:4LHW"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:4LHW"
FT HELIX 158..174
FT /evidence="ECO:0007829|PDB:4LHW"
SQ SEQUENCE 207 AA; 23668 MW; AA52DBF54A2CD056 CRC64;
MAKTYDYLFK LLLIGDSGVG KTCVLFRFSE DAFNSTFIST IGIDFKIRTI ELDGKRIKLQ
IWDTAGQERF RTITTAYYRG AMGIMLVYDI TNEKSFDNIR NWIRNIEEHA SADVEKMILG
NKCDVNDKRQ VSKERGEKLA LDYGIKFMET SAKANINVEN AFFTLARDIK AKMDKKLEGN
SPQGSNQGVK ITPDQQKRSS FFRCVLL
