RB39B_MOUSE
ID RB39B_MOUSE Reviewed; 213 AA.
AC Q8BHC1; Q3TUJ3;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Ras-related protein Rab-39B;
GN Name=Rab39b;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, and Hypothalamus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Limb;
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20159109; DOI=10.1016/j.ajhg.2010.01.011;
RA Giannandrea M., Bianchi V., Mignogna M.L., Sirri A., Carrabino S.,
RA D'Elia E., Vecellio M., Russo S., Cogliati F., Larizza L., Ropers H.H.,
RA Tzschach A., Kalscheuer V., Oehl-Jaschkowitz B., Skinner C., Schwartz C.E.,
RA Gecz J., Van Esch H., Raynaud M., Chelly J., de Brouwer A.P., Toniolo D.,
RA D'Adamo P.;
RT "Mutations in the small GTPase gene RAB39B are responsible for X-linked
RT mental retardation associated with autism, epilepsy, and macrocephaly.";
RL Am. J. Hum. Genet. 86:185-195(2010).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Pancreas;
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 [5]
RP INTERACTION WITH UACA.
RX PubMed=23624502; DOI=10.1016/j.bbrc.2013.04.051;
RA Mori Y., Matsui T., Omote D., Fukuda M.;
RT "Small GTPase Rab39A interacts with UACA and regulates the retinoic acid-
RT induced neurite morphology of Neuro2A cells.";
RL Biochem. Biophys. Res. Commun. 435:113-119(2013).
RN [6]
RP INTERACTION WITH RASSF1.
RX PubMed=23294242; DOI=10.1111/gtc.12028;
RA Takenaka M., Inoue H., Takeshima A., Kakura T., Hori T.;
RT "C. elegans Rassf homolog, rasf-1, is functionally associated with rab-39
RT Rab GTPase in oxidative stress response.";
RL Genes Cells 18:203-210(2013).
RN [7]
RP FUNCTION.
RX PubMed=25434005; DOI=10.1016/j.ajhg.2014.10.015;
RA Wilson G.R., Sim J.C., McLean C., Giannandrea M., Galea C.A., Riseley J.R.,
RA Stephenson S.E., Fitzpatrick E., Haas S.A., Pope K., Hogan K.J.,
RA Gregg R.G., Bromhead C.J., Wargowski D.S., Lawrence C.H., James P.A.,
RA Churchyard A., Gao Y., Phelan D.G., Gillies G., Salce N., Stanford L.,
RA Marsh A.P., Mignogna M.L., Hayflick S.J., Leventer R.J., Delatycki M.B.,
RA Mellick G.D., Kalscheuer V.M., D'Adamo P., Bahlo M., Amor D.J.,
RA Lockhart P.J.;
RT "Mutations in RAB39B cause X-linked intellectual disability and early-onset
RT Parkinson disease with alpha-synuclein pathology.";
RL Am. J. Hum. Genet. 95:729-735(2014).
RN [8]
RP FUNCTION, AND INTERACTION WITH PICK1.
RX PubMed=25784538; DOI=10.1038/ncomms7504;
RA Mignogna M.L., Giannandrea M., Gurgone A., Fanelli F., Raimondi F.,
RA Mapelli L., Bassani S., Fang H., Van Anken E., Alessio M., Passafaro M.,
RA Gatti S., Esteban J.A., Huganir R., D'Adamo P.;
RT "The intellectual disability protein RAB39B selectively regulates GluA2
RT trafficking to determine synaptic AMPAR composition.";
RL Nat. Commun. 6:6504-6504(2015).
RN [9]
RP INTERACTION WITH DLG4.
RX PubMed=31651360; DOI=10.1186/s40478-019-0812-5;
RA Xiao S., McKeever P.M., Lau A., Robertson J.;
RT "Synaptic localization of C9orf72 regulates post-synaptic glutamate
RT receptor 1 levels.";
RL Acta Neuropathol. Commun. 7:161-161(2019).
CC -!- FUNCTION: Small GTPases Rab involved in autophagy. The small GTPases
CC Rab are key regulators of intracellular membrane trafficking, from the
CC formation of transport vesicles to their fusion with membranes. Rabs
CC cycle between an inactive GDP-bound form and an active GTP-bound form
CC that is able to recruit to membranes different sets of downstream
CC effectors directly responsible for vesicle formation, movement,
CC tethering and fusion (By similarity). May be involved in vesicular
CC trafficking (PubMed:20159109). Plays a role in synapse formation. May
CC regulate the homeostasis of SNCA/alpha-synuclein (PubMed:25434005).
CC Together with PICK1 proposed to ensure selectively GRIA2 exit from the
CC endoplasmic reticulum to the Golgi and to regulate AMPAR compostion at
CC the post-synapses and thus synaptic transmission (PubMed:25784538).
CC {ECO:0000250|UniProtKB:Q96DA2, ECO:0000269|PubMed:20159109,
CC ECO:0000269|PubMed:25434005}.
CC -!- SUBUNIT: Interacts (in GTP-bound form) with PICK1 (via PDZ domain); a
CC PICK1 homodimer may allow simultaneous association of RAB39B and GRIA2
CC to PICK1 which is involved in GRIA2 trafficking. Interacts with isoform
CC c of RASSF1; the interaction is strong (PubMed:23294242). Interacts
CC with isoform a of RASSF1; the interaction is weak (PubMed:23294242).
CC Interacts with the DLG4/PSD-95 (PubMed:31651360).
CC {ECO:0000269|PubMed:23294242, ECO:0000269|PubMed:25784538,
CC ECO:0000269|PubMed:31651360}.
CC -!- INTERACTION:
CC Q8BHC1; Q8CGB3-3: Uaca; NbExp=4; IntAct=EBI-10767682, EBI-10767725;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96DA2};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q96DA2}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q96DA2}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q96DA2}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q96DA2}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q96DA2}. Golgi apparatus
CC {ECO:0000269|PubMed:20159109}. Note=Partial colocalization with markers
CC that cycle from the cell surface to the trans-Golgi network.
CC {ECO:0000269|PubMed:20159109}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in neuron and neuronal
CC precursors in the brain. Expression is high in all regions of the brain
CC with highest levels observed in the hippocampus.
CC {ECO:0000269|PubMed:20159109}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AK039013; BAC30206.1; -; mRNA.
DR EMBL; AK048981; BAC33503.1; -; mRNA.
DR EMBL; AK160737; BAE35978.1; -; mRNA.
DR EMBL; BC050853; AAH50853.1; -; mRNA.
DR EMBL; BC052472; AAH52472.1; -; mRNA.
DR CCDS; CCDS30242.1; -.
DR RefSeq; NP_780331.1; NM_175122.6.
DR AlphaFoldDB; Q8BHC1; -.
DR SMR; Q8BHC1; -.
DR BioGRID; 212444; 3.
DR IntAct; Q8BHC1; 47.
DR MINT; Q8BHC1; -.
DR STRING; 10090.ENSMUSP00000033545; -.
DR iPTMnet; Q8BHC1; -.
DR PhosphoSitePlus; Q8BHC1; -.
DR jPOST; Q8BHC1; -.
DR MaxQB; Q8BHC1; -.
DR PaxDb; Q8BHC1; -.
DR PRIDE; Q8BHC1; -.
DR ProteomicsDB; 300357; -.
DR Antibodypedia; 350; 193 antibodies from 28 providers.
DR DNASU; 67790; -.
DR Ensembl; ENSMUST00000033545; ENSMUSP00000033545; ENSMUSG00000031202.
DR GeneID; 67790; -.
DR KEGG; mmu:67790; -.
DR UCSC; uc009tqe.2; mouse.
DR CTD; 116442; -.
DR MGI; MGI:1915040; Rab39b.
DR VEuPathDB; HostDB:ENSMUSG00000031202; -.
DR eggNOG; KOG0091; Eukaryota.
DR GeneTree; ENSGT00940000158132; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; Q8BHC1; -.
DR OMA; XSITRAY; -.
DR OrthoDB; 1416096at2759; -.
DR PhylomeDB; Q8BHC1; -.
DR TreeFam; TF300032; -.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 67790; 3 hits in 73 CRISPR screens.
DR PRO; PR:Q8BHC1; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8BHC1; protein.
DR Bgee; ENSMUSG00000031202; Expressed in supraoptic nucleus and 162 other tissues.
DR ExpressionAtlas; Q8BHC1; baseline and differential.
DR Genevisible; Q8BHC1; MM.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0031489; F:myosin V binding; ISO:MGI.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032482; P:Rab protein signal transduction; IEA:InterPro.
DR GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0050808; P:synapse organization; IMP:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:UniProtKB.
DR CDD; cd04111; Rab39; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041818; Rab39.
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 Autophagy; Cell membrane; Cytoplasmic vesicle; Golgi apparatus;
KW GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Phosphoprotein; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..213
FT /note="Ras-related protein Rab-39B"
FT /id="PRO_0000121256"
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 64..68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 123..126
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 213
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 211
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 213
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 213 AA; 24636 MW; 338F5B35C61FA88E CRC64;
MEAIWLYQFR LIVIGDSTVG KSCLIRRFTE GRFAQVSDPT VGVDFFSRLV EIEPGKRIKL
QIWDTAGQER FRSITRAYYR NSVGGLLLFD ITNRRSFQNV HEWLEETKVH VQPYQIVFVL
VGHKCDLDTQ RQVTRHEAEK LAAAYGMKYI ETSARDAINV EKAFTDLTRD IYELVKRGEI
TIQEGWEGVK SGFVPNVVHS SEEVIKSERR CLC
