RB39A_MOUSE
ID RB39A_MOUSE Reviewed; 217 AA.
AC Q8BHD0;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Ras-related protein Rab-39A;
DE Short=Rab-39;
GN Name=Rab39a; Synonyms=Rab39;
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, and Eye;
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 TISSUE=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, AND 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 [4]
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).
CC -!- FUNCTION: Plays a role in the maturation and acidification of
CC phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis.
CC Plays a role in vesicular trafficking. Plays a role in the fusion of
CC phagosomes with lysosomes. Negatively regulates LPS-induced
CC autophagosome formation in macrophages possibly by implicating PI3K (By
CC similarity). May be involved in multiple neurite formation
CC (PubMed:23624502). {ECO:0000250|UniProtKB:Q14964,
CC ECO:0000269|PubMed:23624502}.
CC -!- SUBUNIT: Interacts with BECN1. Probably associates with the PI3K
CC (PI3KC3/PI3K-III/class III phosphatidylinositol 3-kinase) complex (By
CC similarity). Interacts with UACA. Interacts with isoform a of RASSF1
CC (PubMed:23294242). Does not interact with isoform c of RASSF1
CC (PubMed:23294242). {ECO:0000250|UniProtKB:Q14964,
CC ECO:0000269|PubMed:23294242, ECO:0000269|PubMed:23624502}.
CC -!- INTERACTION:
CC Q8BHD0; Q8CGB3-3: Uaca; NbExp=3; IntAct=EBI-10767908, EBI-10767725;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle,
CC phagosome {ECO:0000250}. Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Lysosome {ECO:0000250|UniProtKB:Q14964}. Note=Recruited
CC to phagosomes containing S.aureus or Mycobacterium. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AK049038; BAC33522.1; -; mRNA.
DR EMBL; AK053487; BAC35399.1; -; mRNA.
DR EMBL; BC049787; AAH49787.1; -; mRNA.
DR CCDS; CCDS23185.1; -.
DR RefSeq; NP_780771.1; NM_175562.3.
DR AlphaFoldDB; Q8BHD0; -.
DR SMR; Q8BHD0; -.
DR IntAct; Q8BHD0; 2.
DR STRING; 10090.ENSMUSP00000063804; -.
DR iPTMnet; Q8BHD0; -.
DR PhosphoSitePlus; Q8BHD0; -.
DR EPD; Q8BHD0; -.
DR jPOST; Q8BHD0; -.
DR MaxQB; Q8BHD0; -.
DR PaxDb; Q8BHD0; -.
DR PRIDE; Q8BHD0; -.
DR ProteomicsDB; 300248; -.
DR Antibodypedia; 31924; 115 antibodies from 26 providers.
DR DNASU; 270160; -.
DR Ensembl; ENSMUST00000068449; ENSMUSP00000063804; ENSMUSG00000055069.
DR GeneID; 270160; -.
DR KEGG; mmu:270160; -.
DR UCSC; uc009pmm.1; mouse.
DR CTD; 270160; -.
DR MGI; MGI:2442855; Rab39.
DR VEuPathDB; HostDB:ENSMUSG00000055069; -.
DR eggNOG; KOG0091; Eukaryota.
DR GeneTree; ENSGT00940000159933; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; Q8BHD0; -.
DR OMA; NEAFHMI; -.
DR OrthoDB; 1416096at2759; -.
DR PhylomeDB; Q8BHD0; -.
DR TreeFam; TF300032; -.
DR Reactome; R-MMU-6811438; Intra-Golgi traffic.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 270160; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Rab39; mouse.
DR PRO; PR:Q8BHD0; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BHD0; protein.
DR Bgee; ENSMUSG00000055069; Expressed in lumbar dorsal root ganglion and 62 other tissues.
DR ExpressionAtlas; Q8BHD0; baseline and differential.
DR Genevisible; Q8BHD0; MM.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0090383; P:phagosome acidification; ISS:UniProtKB.
DR GO; GO:0090385; P:phagosome-lysosome fusion; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032482; P:Rab protein signal transduction; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
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; GTP-binding; Lipoprotein;
KW Lysosome; Membrane; Methylation; Nucleotide-binding; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..217
FT /note="Ras-related protein Rab-39A"
FT /id="PRO_0000121254"
FT MOTIF 41..49
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 68..72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 127..130
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 217
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 215
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 217
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 217 AA; 24978 MW; 311A00AC545C4CE6 CRC64;
METIWIYQFR LIVIGDSTVG KSCLLHRFTQ GRFPGLHSPA CDPTVGVDFF SRLLEIEPGK
RIKLQLWDTA GQERFRSITR SYYRNSVGGF LVFDITNRRS FEHVKDWLEE AKMHVQPFQI
VFLLVGHKCD LASQRQVSRE EAERLSTDCG MKYIETSAKD ATNVEESFTI LTRDIYELIK
KGEICIQDGW EGVKSGFVPN TVHSSEEAVK PRKECFC
