RAB8A_MOUSE
ID RAB8A_MOUSE Reviewed; 207 AA.
AC P55258; Q8VCF6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Ras-related protein Rab-8A;
DE EC=3.6.5.2 {ECO:0000305|PubMed:16541104};
DE AltName: Full=Oncogene c-mel;
DE Flags: Precursor;
GN Name=Rab8a; Synonyms=Mel, Rab8;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [4]
RP PROTEIN SEQUENCE OF 11-21; 59-69 AND 139-153, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP INTERACTION WITH MAP4K2.
RC STRAIN=BALB/cJ; TISSUE=Melanoma;
RX PubMed=8643544; DOI=10.1073/pnas.93.10.5151;
RA Ren M., Zeng J., De Lemos-Chiarandini C., Rosenfeld M., Adesnik M.,
RA Sabatini D.D.;
RT "In its active form, the GTP-binding protein rab8 interacts with a stress-
RT activated protein kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:5151-5155(1996).
RN [6]
RP INTERACTION WITH RIMS2; RPH3A AND RPH3AL.
RX PubMed=12578829; DOI=10.1074/jbc.m212341200;
RA Fukuda M.;
RT "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2.
RT Identification of a critical determinant of Rab3A/Rab27A recognition by
RT Rim2.";
RL J. Biol. Chem. 278:15373-15380(2003).
RN [7]
RP INTERACTION WITH SYTL4.
RX PubMed=12590134; DOI=10.1074/jbc.m213090200;
RA Fukuda M.;
RT "Slp4-a/granuphilin-a inhibits dense-core vesicle exocytosis through
RT interaction with the GDP-bound form of Rab27A in PC12 cells.";
RL J. Biol. Chem. 278:15390-15396(2003).
RN [8]
RP INTERACTION WITH SGSM1 AND SGSM3.
RX PubMed=17509819; DOI=10.1016/j.ygeno.2007.03.013;
RA Yang H., Sasaki T., Minoshima S., Shimizu N.;
RT "Identification of three novel proteins (SGSM1, 2, 3) which modulate small
RT G protein (RAP and RAB)-mediated signaling pathway.";
RL Genomics 90:249-260(2007).
RN [9]
RP FUNCTION IN ENDOCYTIC RECYCLING, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP MICAL1; MICALL1 AND MICALL2.
RX PubMed=18094055; DOI=10.1091/mbc.e07-06-0551;
RA Yamamura R., Nishimura N., Nakatsuji H., Arase S., Sasaki T.;
RT "The interaction of JRAB/MICAL-L2 with Rab8 and Rab13 coordinates the
RT assembly of tight junctions and adherens junctions.";
RL Mol. Biol. Cell 19:971-983(2008).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH AHI1.
RX PubMed=19625297; DOI=10.1093/hmg/ddp335;
RA Hsiao Y.C., Tong Z.J., Westfall J.E., Ault J.G., Page-McCaw P.S.,
RA Ferland R.J.;
RT "Ahi1, whose human ortholog is mutated in Joubert syndrome, is required for
RT Rab8a localization, ciliogenesis and vesicle trafficking.";
RL Hum. Mol. Genet. 18:3926-3941(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
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 [14]
RP SUBCELLULAR LOCATION.
RX PubMed=23807208; DOI=10.1007/s00018-013-1401-6;
RA Kypri E., Christodoulou A., Maimaris G., Lethan M., Markaki M.,
RA Lysandrou C., Lederer C.W., Tavernarakis N., Geimer S., Pedersen L.B.,
RA Santama N.;
RT "The nucleotide-binding proteins Nubp1 and Nubp2 are negative regulators of
RT ciliogenesis.";
RL Cell. Mol. Life Sci. 71:517-538(2014).
RN [15]
RP FUNCTION, INTERACTION WITH DZIP1, AND SUBCELLULAR LOCATION.
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 [16]
RP PHOSPHORYLATION AT 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 [17]
RP INTERACTION WITH RILPL1 AND RILPL2, AND PHOSPHORYLATION AT 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 [18]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-175 IN COMPLEX WITH RABIF,
RP INTERACTION WITH RABIF, AND CATALYTIC ACTIVITY.
RX PubMed=16541104; DOI=10.1038/sj.emboj.7601044;
RA Itzen A., Pylypenko O., Goody R.S., Alexandrov K., Rak A.;
RT "Nucleotide exchange via local protein unfolding--structure of Rab8 in
RT complex with MSS4.";
RL EMBO J. 25:1445-1455(2006).
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 (By
CC similarity). Regulates the compacted morphology of the Golgi (By
CC similarity). Together with MYO5B and RAB11A participates in epithelial
CC cell polarization (By similarity). Also involved in membrane
CC trafficking to the cilium and ciliogenesis (PubMed:25860027). Together
CC with MICALL2, may also regulate adherens junction assembly
CC (PubMed:18094055). May play a role in insulin-induced transport to the
CC plasma membrane of the glucose transporter GLUT4 and therefore play a
CC role in glucose homeostasis (By similarity). Involved in autophagy (By
CC similarity). {ECO:0000250|UniProtKB:P35280,
CC ECO:0000250|UniProtKB:P61006, ECO:0000269|PubMed:18094055,
CC ECO:0000305|PubMed:25860027}.
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:16541104};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000305|PubMed:16541104};
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 (By similarity). Activated in response to
CC insulin (By similarity). {ECO:0000250|UniProtKB:P35280,
CC ECO:0000250|UniProtKB:P61006}.
CC -!- SUBUNIT: Interacts (GTP-bound form) with MICALL1; regulates RAB8A
CC association with recycling endosomes (PubMed:18094055). Interacts with
CC MICALL2; competes with RAB13 and is involved in E-cadherin endocytic
CC recycling (PubMed:18094055). Interacts (GTP-bound form) with 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 (By similarity). Interacts (GTP-
CC bound form) with EHBP1 (By similarity). Interacts with EHD1 (By
CC similarity). Interacts with MAP4K2 and SYTL4 (PubMed:8643544,
CC PubMed:12590134). Interacts with SGSM1 and SGSM3 (PubMed:17509819).
CC Interacts with RABIF, RIMS2, RPH3A and RPH3A (PubMed:12578829,
CC PubMed:16541104). Interacts with OPTN (By similarity). Interacts with
CC RAB3IP (PubMed:19625297). Interacts with MYO5B (By similarity).
CC Interacts with PIFO (PubMed:20643351). Interacts with BIRC6/bruce (By
CC similarity). Interacts with OCRL (By similarity). Interacts with AHI1
CC (PubMed:19625297). Interacts with DCDC1 (By similarity). Interacts with
CC LRRK2; interaction facilitates phosphorylation of Thr-72 (By
CC similarity). Interacts with RAB31P, GDI1, GDI2, CHM, CHML, RABGGTA,
CC RABGGTB, TBC1D15 and INPP5B; these interactions are dependent on Thr-72
CC not being phosphorylated (By similarity). Interacts with RILPL1 and
CC RILPL2; these interactions are dependent on the phosphorylation of Thr-
CC 72 by LRRK2 (PubMed:29125462). Interacts with DZIP1; prevents
CC inhibition by the GDP-dissociation inhibitor GDI2 (PubMed:25860027).
CC {ECO:0000250|UniProtKB:P61006, ECO:0000269|PubMed:12578829,
CC ECO:0000269|PubMed:12590134, ECO:0000269|PubMed:16541104,
CC ECO:0000269|PubMed:17509819, ECO:0000269|PubMed:18094055,
CC ECO:0000269|PubMed:19625297, ECO:0000269|PubMed:20643351,
CC ECO:0000269|PubMed:25860027, ECO:0000269|PubMed:29125462,
CC ECO:0000269|PubMed:8643544}.
CC -!- INTERACTION:
CC P55258; Q8BMD2: Dzip1; NbExp=2; IntAct=EBI-398411, EBI-7089968;
CC P55258; P47708: Rph3a; NbExp=2; IntAct=EBI-398411, EBI-398376;
CC P55258; O55042: Snca; NbExp=2; IntAct=EBI-398411, EBI-2310271;
CC P55258; P50395: GDI2; Xeno; NbExp=3; IntAct=EBI-398411, EBI-1049143;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18094055};
CC Lipid-anchor {ECO:0000269|PubMed:18094055}; Cytoplasmic side
CC {ECO:0000269|PubMed:18094055}. Golgi apparatus
CC {ECO:0000250|UniProtKB:P61006}. Recycling endosome membrane
CC {ECO:0000269|PubMed:18094055}. Cell projection, cilium
CC {ECO:0000269|PubMed:25860027}. Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000250|UniProtKB:P61006}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P61006}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P61006}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:23807208}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:19625297, ECO:0000269|PubMed:23807208,
CC ECO:0000269|PubMed:25860027}. Midbody {ECO:0000250|UniProtKB:P61006}.
CC Cytoplasm {ECO:0000250|UniProtKB:P61006}. Note=Colocalizes with OPTN at
CC the Golgi complex and in vesicular structures close to the plasma
CC membrane. In the GDP-bound form, present in the perinuclear region.
CC Shows a polarized distribution to distal regions of cell protrusions in
CC the GTP-bound form. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, PODXL
CC and RAB11A in apical membrane initiation sites (AMIS) during the
CC generation of apical surface and lumenogenesis. Localizes to tubular
CC recycling endosome. Recruited to phagosomes containing S.aureus or
CC Mycobacterium (By similarity). Non-phosphorylated RAB8A predominantly
CC localizes to the cytoplasm whereas phosphorylated RAB8A localizes to
CC the membrane (By similarity). {ECO:0000250|UniProtKB:P61006}.
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:0000250|UniProtKB:P61006}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; S53270; AAB19682.1; -; mRNA.
DR EMBL; AK076048; BAC36146.1; -; mRNA.
DR EMBL; AK079306; BAC37603.1; -; mRNA.
DR EMBL; AK080740; BAC38003.1; -; mRNA.
DR EMBL; BC019990; AAH19990.1; -; mRNA.
DR CCDS; CCDS22409.1; -.
DR RefSeq; NP_075615.2; NM_023126.2.
DR PDB; 2FU5; X-ray; 2.00 A; C/D=1-175.
DR PDBsum; 2FU5; -.
DR AlphaFoldDB; P55258; -.
DR SMR; P55258; -.
DR BioGRID; 201387; 14.
DR CORUM; P55258; -.
DR DIP; DIP-31053N; -.
DR IntAct; P55258; 25.
DR MINT; P55258; -.
DR STRING; 10090.ENSMUSP00000003121; -.
DR iPTMnet; P55258; -.
DR PhosphoSitePlus; P55258; -.
DR SwissPalm; P55258; -.
DR EPD; P55258; -.
DR jPOST; P55258; -.
DR PaxDb; P55258; -.
DR PeptideAtlas; P55258; -.
DR PRIDE; P55258; -.
DR ProteomicsDB; 300343; -.
DR Antibodypedia; 27297; 294 antibodies from 37 providers.
DR DNASU; 17274; -.
DR Ensembl; ENSMUST00000003121; ENSMUSP00000003121; ENSMUSG00000003037.
DR GeneID; 17274; -.
DR KEGG; mmu:17274; -.
DR UCSC; uc009mfj.1; mouse.
DR CTD; 4218; -.
DR MGI; MGI:96960; Rab8a.
DR VEuPathDB; HostDB:ENSMUSG00000003037; -.
DR eggNOG; KOG0078; Eukaryota.
DR GeneTree; ENSGT00940000157246; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; P55258; -.
DR OMA; SKMEQNE; -.
DR OrthoDB; 1426655at2759; -.
DR PhylomeDB; P55258; -.
DR TreeFam; TF314097; -.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-5620916; VxPx cargo-targeting to cilium.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 17274; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Rab8a; mouse.
DR EvolutionaryTrace; P55258; -.
DR PRO; PR:P55258; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P55258; protein.
DR Bgee; ENSMUSG00000003037; Expressed in granulocyte and 254 other tissues.
DR ExpressionAtlas; P55258; baseline and differential.
DR Genevisible; P55258; MM.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0097546; C:ciliary base; IDA:MGI.
DR GO; GO:0060170; C:ciliary membrane; IDA:MGI.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0097730; C:non-motile cilium; IDA:MGI.
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; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IDA:MGI.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0031489; F:myosin V binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
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; IMP:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0048210; P:Golgi vesicle fusion to target membrane; ISO:MGI.
DR GO; GO:0098969; P:neurotransmitter receptor transport to postsynaptic membrane; ISO:MGI.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; ISO:MGI.
DR GO; GO:0061512; P:protein localization to cilium; IMP: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; ISS:UniProtKB.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:MGI.
DR GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
DR GO; GO:0051223; P:regulation of protein transport; ISO:MGI.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; ISO:MGI.
DR GO; GO:0099003; P:vesicle-mediated transport in synapse; ISO:MGI.
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; Autophagy; Cell membrane; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Direct protein sequencing; Endosome; Golgi apparatus;
KW GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW Proto-oncogene; Reference proteome; Transport.
FT CHAIN 1..204
FT /note="Ras-related protein Rab-8A"
FT /id="PRO_0000121132"
FT PROPEP 205..207
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370795"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 17..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61006"
FT BINDING 34..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61006"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61006,
FT ECO:0000250|UniProtKB:Q9H0U4"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61006"
FT BINDING 152..154
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61006,
FT ECO:0000250|UniProtKB:Q9H0U4"
FT MOD_RES 72
FT /note="Phosphothreonine; by LRRK2"
FT /evidence="ECO:0000269|PubMed:26824392,
FT ECO:0000269|PubMed:29125462"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61006"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 204
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 204
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 176..183
FT /note="KLEGNSPQ -> NWKATAA (in Ref. 1; AAB19682)"
FT /evidence="ECO:0000305"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:2FU5"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:2FU5"
FT STRAND 43..52
FT /evidence="ECO:0007829|PDB:2FU5"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:2FU5"
FT TURN 76..80
FT /evidence="ECO:0007829|PDB:2FU5"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:2FU5"
FT HELIX 93..109
FT /evidence="ECO:0007829|PDB:2FU5"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:2FU5"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:2FU5"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:2FU5"
FT HELIX 158..175
FT /evidence="ECO:0007829|PDB:2FU5"
SQ SEQUENCE 207 AA; 23668 MW; AC89DC85588FB8F8 CRC64;
MAKTYDYLFK LLLIGDSGVG KTCVLFRFSE DAFNSTFIST IGIDFKIRTI ELDGKRIKLQ
IWDTAGQERF RTITTAYYRG AMGIMLVYDI TNEKSFDNIR NWIRNIEEHA SADVEKMILG
NKCDVNDKRQ VSKERGEKLA LDYGIKFMET SAKANINVEN AFFTLARDIK AKMDKKLEGN
SPQGSSHGVK ITVEQQKRTS FFRCSLL
