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 02-SEP-2026, entry version 219. 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 {ECO:0000312|MGI:MGI:96960}; 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, RC Pancreas, 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 CIMAP3. 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] {ECO:0000305} RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT THR-72. RX PubMed=30209220; DOI=10.1073/pnas.1812196115; RA Eguchi T., Kuwahara T., Sakurai M., Komori T., Fujimoto T., Ito G., RA Yoshimura S.I., Harada A., Fukuda M., Koike M., Iwatsubo T.; RT "LRRK2 and its substrate Rab GTPases are sequentially targeted onto RT stressed lysosomes and maintain their homeostasis."; RL Proc. Natl. Acad. Sci. U.S.A. 115:E9115-E9124(2018). RN [19] RP INTERACTION WITH MICALL2. RX PubMed=33976349; DOI=10.1038/s42003-021-02080-7; RA Sakane A., Yano T.A., Uchihashi T., Horikawa K., Hara Y., Imoto I., RA Kurisu S., Yamada H., Takei K., Sasaki T.; RT "JRAB/MICAL-L2 undergoes liquid-liquid phase separation to form tubular RT recycling endosomes."; RL Commun. Biol. 4:551-551(2021). RN [20] 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. RAB8A 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). Participates in the export of a subset of neosynthesized CC proteins through a Rab8-Rab10-Rab11-dependent endososomal export route CC (By similarity). Targeted to and stabilized on stressed lysosomes CC through LRRK2 phosphorylation (PubMed:30209220). Suppresses stress- CC induced lysosomal enlargement through EHBP1 and EHNP1L1 effector CC proteins (By similarity). {ECO:0000250|UniProtKB:P35280, CC ECO:0000250|UniProtKB:P61006, ECO:0000269|PubMed:18094055, CC ECO:0000269|PubMed:30209220, ECO:0000305|PubMed:25860027}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + phosphate + H(+); 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P61006}; CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors CC (GEFs) such as RAB3IP/Rabin8 and RPGR which promote the exchange of CC bound GDP for free GTP, GTPase activating proteins (GAPs) which CC increase the GTP hydrolysis activity, and GDP dissociation inhibitors CC (GDIs) which inhibit the dissociation of the nucleotide from the GTPase CC (By similarity). Activated in response to insulin (By similarity). CC {ECO:0000250|UniProtKB:P35280, 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, PubMed:33976349). Interacts (GTP-bound CC form) with MICAL1, MICALCL, MICAL3 and EHBP1L1; two molecules of RAB8A CC can bind to one molecule of the effector protein; ternary complexes of CC RAB8A, RAB13 and either MICAL1 or EHBP1L1 are possible (By similarity). CC Interacts (GTP-bound form) with EHBP1 (By similarity). Interacts with CC EHD1 (By similarity). Interacts with MAP4K2 and SYTL4 (PubMed:12590134, CC PubMed:8643544). 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 MYO5B (By similarity). Interacts with CIMAP3 (PubMed:20643351). CC Interacts with BIRC6/bruce (By similarity). Interacts with OCRL (By CC similarity). Interacts with AHI1 (PubMed:19625297). Interacts with CC DCDC1 (By similarity). Interacts with LRRK2; interaction facilitates CC phosphorylation of Thr-72 (By similarity). Interacts with RAB31P, GDI1, CC GDI2, CHM, CHML, RABGGTA, RABGGTB, TBC1D15 and INPP5B; these CC interactions are dependent on Thr-72 not being phosphorylated (By CC similarity). Interacts with RILPL1 and RILPL2; these interactions are CC dependent on the phosphorylation of Thr-72 by LRRK2 (PubMed:29125462). CC Interacts with DZIP1; prevents inhibition by the GDP-dissociation CC inhibitor GDI2 (PubMed:25860027). Interacts with RAB3IP/Rabin8, RAB3IP CC functions as guanine exchange factor (GEF) towards RAB8A CC (PubMed:19625297). Interacts (in GDP-bound form) with RPGR, RPGR CC functions as GEF towards RAB8A (By similarity). 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:33976349, 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}. Endosome membrane 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}. Lysosome CC {ECO:0000269|PubMed:30209220}. Note=Colocalizes with OPTN at the Golgi CC complex and in vesicular structures close to the plasma membrane. In CC the GDP-bound form, present in the perinuclear region. Shows a CC polarized distribution to distal regions of cell protrusions in the CC GTP-bound form. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, PODXL and CC RAB11A in apical membrane initiation sites (AMIS) during the generation CC of apical surface and lumenogenesis. Localizes to tubular recycling CC endosome. Recruited to phagosomes containing S.aureus or Mycobacterium CC (By similarity). Non-phosphorylated RAB8A predominantly localizes to CC the cytoplasm whereas phosphorylated RAB8A localizes to the membrane CC (By similarity). Localizes to enlarged lysosomes through LRRK2 CC phosphorylation (PubMed:30209220). Colocalizes with RPGR at the primary CC cilia of epithelial cells (By similarity). CC {ECO:0000250|UniProtKB:P61006, ECO:0000250|UniProtKB:P61007, CC ECO:0000269|PubMed:30209220}. CC -!- DOMAIN: Switch 1, switch 2 and the interswitch regions are CC characteristic of Rab GTPases and mediate the interactions with Rab CC downstream effectors. The switch regions undergo conformational changes CC upon nucleotide binding which drives interaction with specific sets of CC effector proteins, with most effectors only binding to GTP-bound Rab. CC {ECO:0000250|UniProtKB:P62820}. 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 (By similarity). CC Phosphorylation by LRRK2 is required for localization to stressed CC lysosomes (PubMed:30209220). {ECO:0000250|UniProtKB:P61006, CC ECO:0000269|PubMed:30209220}. 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; 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 AlphaFoldDB; P55258; -. DR SMR; P55258; -. DR BioGRID; 201387; 18. DR CORUM; P55258; -. DR DIP; DIP-31053N; -. DR FunCoup; P55258; 3042. DR IntAct; P55258; 25. DR MINT; P55258; -. DR STRING; 10090.ENSMUSP00000003121; -. DR GlyGen; P55258; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P55258; -. DR PhosphoSitePlus; P55258; -. DR SwissPalm; P55258; -. DR jPOST; P55258; -. DR PaxDb; 10090-ENSMUSP00000003121; -. DR PeptideAtlas; P55258; -. DR ProteomicsDB; 300343; -. DR Pumba; P55258; -. DR Antibodypedia; 27297; 319 antibodies from 38 providers. DR DNASU; 17274; -. DR Ensembl; ENSMUST00000003121.9; ENSMUSP00000003121.9; ENSMUSG00000003037.17. DR GeneID; 17274; -. DR KEGG; mmu:17274; -. DR UCSC; uc009mfj.1; mouse. DR AGR; MGI:96960; -. 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; 9989112at2759; -. DR PhylomeDB; P55258; -. 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; 4 hits in 77 CRISPR screens. DR EvolutionaryTrace; P55258; -. DR PRO; PR:P55258; -. DR Proteomes; UP000000589; Chromosome 8. DR RNAct; P55258; protein. DR Bgee; ENSMUSG00000003037; Expressed in granulocyte and 258 other cell types or tissues. DR ExpressionAtlas; P55258; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; ISO:GO_Central. DR GO; GO:0034451; C:centriolar satellite; ISO:GO_Central. 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:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:GO_Central. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome. DR GO; GO:0005829; C:cytosol; ISO:GO_Central. DR GO; GO:0030425; C:dendrite; ISO:GO_Central. DR GO; GO:0005768; C:endosome; IBA:GO_Central. DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; ISO:GO_Central. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0030496; C:midbody; ISS:UniProtKB. DR GO; GO:0043025; C:neuronal cell body; ISO:GO_Central. DR GO; GO:0097730; C:non-motile cilium; IDA:MGI. DR GO; GO:0005730; C:nucleolus; ISO:GO_Central. DR GO; GO:0005654; C:nucleoplasm; ISO:GO_Central. 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:0055037; C:recycling endosome; IDA:UniProtKB. DR GO; GO:0055038; C:recycling endosome membrane; EXP:UniProtKB. DR GO; GO:0045202; C:synapse; ISO:GO_Central. 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:0003925; F:G protein activity; ISS:UniProtKB. 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:GO_Central. DR GO; GO:0031489; F:myosin V binding; ISO:GO_Central. DR GO; GO:0019901; F:protein kinase binding; ISO:GO_Central. DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:GO_Central. DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB. 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:0006887; P:exocytosis; IBA:GO_Central. DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB. DR GO; GO:0048210; P:Golgi vesicle fusion to target membrane; ISO:GO_Central. DR GO; GO:0098969; P:neurotransmitter receptor transport to postsynaptic membrane; ISO:GO_Central. DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; ISO:GO_Central. 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:0010506; P:regulation of autophagy; ISS:UniProtKB. DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:GO_Central. DR GO; GO:0032880; P:regulation of protein localization; ISO:GO_Central. DR GO; GO:0051223; P:regulation of protein transport; ISO:GO_Central. DR GO; GO:0006904; P:vesicle docking involved in exocytosis; ISO:GO_Central. DR GO; GO:0099003; P:vesicle-mediated transport in synapse; ISO:GO_Central. DR CDD; cd01867; Rab8_Rab10_Rab13_like; 1. DR FunFam; 3.40.50.300:FF:000202; ras-related protein Rab-8A; 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. DR InterPro; IPR001806; Small_GTPase. DR InterPro; IPR050305; Small_GTPase_Rab. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR47980; LD44762P; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00177; ARF; 1. 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 PDBsum; 2FU5; -. 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; Lysosome; Magnesium; Membrane; KW Metal-binding; Methylation; Nucleotide-binding; Phosphoprotein; KW Prenylation; Protein transport; Proto-oncogene; Reference proteome; KW 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 31..45 FT /note="Switch 1" FT /evidence="ECO:0000250|UniProtKB:P62820" FT MOTIF 63..80 FT /note="Switch 2" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 17 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61006" FT BINDING 18 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61006" FT BINDING 19 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61006" FT BINDING 20 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61006" FT BINDING 21 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61006" FT BINDING 22 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61006" FT BINDING 22 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P61006" FT BINDING 23 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61006" FT BINDING 35 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61006" FT BINDING 39 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61006" FT BINDING 40 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61006" FT BINDING 40 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P61006" FT BINDING 63 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P61006" FT BINDING 66 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61006" FT BINDING 121 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61006" FT BINDING 122 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61006" FT BINDING 124 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61006" FT BINDING 152 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61006" FT BINDING 153 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61006" FT MOD_RES 72 FT /note="Phosphothreonine; by LRRK2" FT /evidence="ECO:0000269|PubMed:26824392, FT ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:30209220" 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..143 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 //