RB39A_HUMAN
ID RB39A_HUMAN Reviewed; 217 AA.
AC Q14964; A8KAA4; Q8N6W2;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Ras-related protein Rab-39A;
DE Short=Rab-39;
GN Name=RAB39A; Synonyms=RAB39;
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].
RX PubMed=9119394; DOI=10.1006/geno.1996.4595;
RA Stankovic T., Byrd P.J., Cooper P.R., McConville C.M., Munroe D.J.,
RA Riley J.H., Watts G.D.J., Ambrose H., McGuire G., Smith A.D., Sutcliffe A.,
RA Mills T., Taylor A.M.R.;
RT "Construction of a transcription map around the gene for ataxia
RT telangiectasia; identification of at least four novel genes.";
RL Genomics 40:267-276(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
RP FUNCTION, AND 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 [6]
RP FUNCTION, INTERACTION WITH BECN1, SUBUNIT, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 34-PRO--CYS-41.
RX PubMed=24349490; DOI=10.1371/journal.pone.0083324;
RA Seto S., Sugaya K., Tsujimura K., Nagata T., Horii T., Koide Y.;
RT "Rab39a interacts with phosphatidylinositol 3-kinase and negatively
RT regulates autophagy induced by lipopolysaccharide stimulation in
RT macrophages.";
RL PLoS ONE 8:E83324-E83324(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
CC (PubMed:24349490). May be involved in multiple neurite formation (By
CC similarity). {ECO:0000250|UniProtKB:Q8BHD0,
CC ECO:0000269|PubMed:21255211, ECO:0000269|PubMed:24349490}.
CC -!- SUBUNIT: Interacts with BECN1. Probably associates with the PI3K
CC (PI3KC3/PI3K-III/class III phosphatidylinositol 3-kinase) complex
CC (PubMed:24349490). Interacts with UACA (By similarity). Interacts with
CC isoform a of RASSF1 (By similarity). Does not interact with isoform c
CC of RASSF1 (By similarity). {ECO:0000250|UniProtKB:Q8BHD0,
CC ECO:0000269|PubMed:24349490, ECO:0000305}.
CC -!- INTERACTION:
CC Q14964; Q14457: BECN1; NbExp=2; IntAct=EBI-3048577, EBI-949378;
CC Q14964; Q9H2G9: BLZF1; NbExp=8; IntAct=EBI-3048577, EBI-2548012;
CC Q14964; Q08379: GOLGA2; NbExp=6; IntAct=EBI-3048577, EBI-618309;
CC Q14964; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-3048577, EBI-739467;
CC Q14964; P61026: RAB10; NbExp=2; IntAct=EBI-3048577, EBI-726075;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle,
CC phagosome {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome
CC membrane {ECO:0000269|PubMed:24349490}; Lipid-anchor {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Lysosome {ECO:0000269|PubMed:24349490}.
CC Note=Recruited to phagosomes containing S.aureus or M.tuberculosis.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; X99962; CAA68227.1; -; mRNA.
DR EMBL; AK292969; BAF85658.1; -; mRNA.
DR EMBL; CH471065; EAW67100.1; -; Genomic_DNA.
DR EMBL; BC028064; AAH28064.1; -; mRNA.
DR CCDS; CCDS8338.1; -.
DR RefSeq; NP_059986.1; NM_017516.2.
DR AlphaFoldDB; Q14964; -.
DR SMR; Q14964; -.
DR BioGRID; 120117; 20.
DR DIP; DIP-60521N; -.
DR IntAct; Q14964; 17.
DR STRING; 9606.ENSP00000322594; -.
DR iPTMnet; Q14964; -.
DR PhosphoSitePlus; Q14964; -.
DR BioMuta; RAB39A; -.
DR DMDM; 46577701; -.
DR EPD; Q14964; -.
DR jPOST; Q14964; -.
DR MassIVE; Q14964; -.
DR MaxQB; Q14964; -.
DR PaxDb; Q14964; -.
DR PeptideAtlas; Q14964; -.
DR PRIDE; Q14964; -.
DR ProteomicsDB; 60261; -.
DR Antibodypedia; 31924; 115 antibodies from 26 providers.
DR DNASU; 54734; -.
DR Ensembl; ENST00000320578.3; ENSP00000322594.2; ENSG00000179331.3.
DR GeneID; 54734; -.
DR KEGG; hsa:54734; -.
DR MANE-Select; ENST00000320578.3; ENSP00000322594.2; NM_017516.3; NP_059986.1.
DR UCSC; uc001pjt.4; human.
DR CTD; 54734; -.
DR DisGeNET; 54734; -.
DR GeneCards; RAB39A; -.
DR HGNC; HGNC:16521; RAB39A.
DR HPA; ENSG00000179331; Tissue enhanced (brain, lymphoid tissue).
DR MIM; 619558; gene.
DR neXtProt; NX_Q14964; -.
DR OpenTargets; ENSG00000179331; -.
DR PharmGKB; PA34130; -.
DR VEuPathDB; HostDB:ENSG00000179331; -.
DR eggNOG; KOG0091; Eukaryota.
DR GeneTree; ENSGT00940000159933; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; Q14964; -.
DR OMA; NEAFHMI; -.
DR OrthoDB; 1416096at2759; -.
DR PhylomeDB; Q14964; -.
DR TreeFam; TF300032; -.
DR PathwayCommons; Q14964; -.
DR Reactome; R-HSA-6811438; Intra-Golgi traffic.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q14964; -.
DR BioGRID-ORCS; 54734; 13 hits in 1067 CRISPR screens.
DR ChiTaRS; RAB39A; human.
DR GenomeRNAi; 54734; -.
DR Pharos; Q14964; Tbio.
DR PRO; PR:Q14964; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q14964; protein.
DR Bgee; ENSG00000179331; Expressed in monocyte and 96 other tissues.
DR Genevisible; Q14964; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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; IDA: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; IMP:UniProtKB.
DR GO; GO:0090385; P:phagosome-lysosome fusion; IMP: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_0000121253"
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"
FT MUTAGEN 34..41
FT /note="PGLRSPAC->AQVS: Disrupts interaction with BECN1."
FT /evidence="ECO:0000269|PubMed:24349490"
FT CONFLICT 152
FT /note="K -> M (in Ref. 1; CAA68227)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="F -> S (in Ref. 1; CAA68227)"
FT /evidence="ECO:0000305"
FT CONFLICT 176..177
FT /note="YE -> FD (in Ref. 1; CAA68227)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="S -> P (in Ref. 1; CAA68227)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="F -> S (in Ref. 1; CAA68227)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 217 AA; 25007 MW; ABD121649354D7F5 CRC64;
METIWIYQFR LIVIGDSTVG KSCLLHRFTQ GRFPGLRSPA CDPTVGVDFF SRLLEIEPGK
RIKLQLWDTA GQERFRSITR SYYRNSVGGF LVFDITNRRS FEHVKDWLEE AKMYVQPFRI
VFLLVGHKCD LASQRQVTRE EAEKLSADCG MKYIETSAKD ATNVEESFTI LTRDIYELIK
KGEICIQDGW EGVKSGFVPN TVHSSEEAVK PRKECFC
