RAB34_MOUSE
ID RAB34_MOUSE Reviewed; 259 AA.
AC Q64008; Q8BHJ0; Q99P59; Q99P90;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Ras-related protein Rab-34;
DE AltName: Full=Ras-related homolog;
DE AltName: Full=Ras-related protein Rab-39;
DE AltName: Full=Ras-related protein Rah;
GN Name=Rab34; Synonyms=Rab39, Rah, Rah1;
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].
RC STRAIN=C57BL/6J;
RA Hong W.;
RT "Mouse Rab39 coding region (cDNA).";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Neuron;
RA Hari M., Morimoto B.H., Asai D.J.;
RT "Full length sequence of Rah, a novel member of the Rab family of small
RT GTPases.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sun P., Yamamoto H., Endo T.;
RT "Rah, a Rab family small GTPase.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Lung;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 52-259.
RC TISSUE=Neuron;
RX PubMed=1752434; DOI=10.1101/gad.5.12b.2386;
RA Morimoto B.H., Chuang C.-C., Koshland D.E. Jr.;
RT "Molecular cloning of a member of a new class of low-molecular-weight GTP-
RT binding proteins.";
RL Genes Dev. 5:2386-2391(1991).
RN [6]
RP FUNCTION IN LYSOSOME REDISTRIBUTION, INTERACTION WITH RILP, MUTAGENESIS OF
RP LYS-82, AND SUBCELLULAR LOCATION.
RX PubMed=12475955; DOI=10.1091/mbc.e02-05-0280;
RA Wang T., Hong W.;
RT "Interorganellar regulation of lysosome positioning by the Golgi apparatus
RT through Rab34 interaction with Rab-interacting lysosomal protein.";
RL Mol. Biol. Cell 13:4317-4332(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, 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 [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29290584; DOI=10.1016/j.devcel.2017.12.003;
RA Pusapati G.V., Kong J.H., Patel B.B., Krishnan A., Sagner A., Kinnebrew M.,
RA Briscoe J., Aravind L., Rohatgi R.;
RT "CRISPR screens uncover genes that regulate target cell sensitivity to the
RT morphogen sonic hedgehog.";
RL Dev. Cell 44:113-129(2018).
CC -!- FUNCTION: Transport protein involved in the redistribution of lysosomes
CC to the peri-Golgi region (PubMed:12475955). Plays a role in the
CC maturation of phagosomes that engulf pathogens, such as S.aureus and
CC M.tuberculosis (By similarity). Plays a role in the fusion of
CC phagosomes with lysosomes (By similarity). Acts also as a positive
CC regulator of hedgehog signaling and regulates ciliary function
CC (PubMed:29290584). {ECO:0000250|UniProtKB:Q9BZG1,
CC ECO:0000269|PubMed:12475955, ECO:0000269|PubMed:29290584}.
CC -!- SUBUNIT: Interacts with RILP. {ECO:0000269|PubMed:12475955}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12475955}. Golgi
CC apparatus {ECO:0000269|PubMed:12475955}. Cytoplasmic vesicle, phagosome
CC {ECO:0000250|UniProtKB:Q9BZG1}. Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000250|UniProtKB:Q9BZG1}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9BZG1}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9BZG1}. Cell projection, cilium
CC {ECO:0000269|PubMed:29290584}. Note=Recruited to phagosomes containing
CC S.aureus or Mycobacterium. {ECO:0000250|UniProtKB:Q9BZG1}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AF322068; AAK09398.1; -; mRNA.
DR EMBL; AF327929; AAK11241.1; -; mRNA.
DR EMBL; AB082927; BAC16803.1; -; mRNA.
DR EMBL; BC038638; AAH38638.1; -; mRNA.
DR EMBL; S72304; AAB20669.1; -; mRNA.
DR CCDS; CCDS25094.1; -.
DR PIR; A41636; A41636.
DR RefSeq; NP_001152954.1; NM_001159482.1.
DR RefSeq; NP_258436.2; NM_033475.3.
DR AlphaFoldDB; Q64008; -.
DR SMR; Q64008; -.
DR BioGRID; 202576; 6.
DR IntAct; Q64008; 7.
DR STRING; 10090.ENSMUSP00000103958; -.
DR iPTMnet; Q64008; -.
DR PhosphoSitePlus; Q64008; -.
DR SwissPalm; Q64008; -.
DR jPOST; Q64008; -.
DR MaxQB; Q64008; -.
DR PaxDb; Q64008; -.
DR PRIDE; Q64008; -.
DR ProteomicsDB; 300379; -.
DR DNASU; 19376; -.
DR GeneID; 19376; -.
DR KEGG; mmu:19376; -.
DR CTD; 83871; -.
DR MGI; MGI:104606; Rab34.
DR eggNOG; KOG0094; Eukaryota.
DR InParanoid; Q64008; -.
DR OrthoDB; 1048146at2759; -.
DR PhylomeDB; Q64008; -.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR BioGRID-ORCS; 19376; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Rab34; mouse.
DR PRO; PR:Q64008; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q64008; protein.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005769; C:early endosome; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031985; C:Golgi cisterna; ISO:MGI.
DR GO; GO:0005795; C:Golgi stack; ISO:MGI.
DR GO; GO:0005770; C:late endosome; IDA:ParkinsonsUK-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IDA:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0030742; F:GTP-dependent protein binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; IDA:MGI.
DR GO; GO:0019001; F:guanyl nucleotide binding; IDA:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0019882; P:antigen processing and presentation; ISO:MGI.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0006897; P:endocytosis; IDA:MGI.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IGI:UniProtKB.
DR GO; GO:0007041; P:lysosomal transport; IDA:ParkinsonsUK-UCL.
DR GO; GO:0032418; P:lysosome localization; ISO:MGI.
DR GO; GO:0090382; P:phagosome maturation; ISS:UniProtKB.
DR GO; GO:0090385; P:phagosome-lysosome fusion; IMP:ParkinsonsUK-UCL.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IDA:ParkinsonsUK-UCL.
DR GO; GO:1905171; P:positive regulation of protein localization to phagocytic vesicle; IMP:ParkinsonsUK-UCL.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
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 Acetylation; Cell projection; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoplasmic vesicle; Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..259
FT /note="Ras-related protein Rab-34"
FT /id="PRO_0000121244"
FT MOTIF 81..89
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 59..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 107..111
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 166..169
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZG1"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT LIPID 257
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 258
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000255"
FT MUTAGEN 82
FT /note="K->Q: Abolishes interaction with RILP and
FT localization to the peri-Golgi region."
FT /evidence="ECO:0000269|PubMed:12475955"
FT MUTAGEN 82
FT /note="K->Y: Does not abolish interaction with RILP and
FT localization to the peri-Golgi region."
FT /evidence="ECO:0000269|PubMed:12475955"
FT CONFLICT 52
FT /note="I -> N (in Ref. 5; AAB20669)"
FT /evidence="ECO:0000305"
FT CONFLICT 224..225
FT /note="DV -> EL (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 29101 MW; 158F5132F0DDE808 CRC64;
MNILAPVRRD RVLAELPQCL KKEAALHVRK DFHPRVTCAC QEHRTGTVGF KISKVIVVGD
LSVGKTCLIN RFCKDTFDKN YKATIGVDFE MERFEVLGVP FSLQLWDTAG QERFKCIAST
YYRGAQAIII VFNLNDVASL EHTKQWLTDA LKENDPSNVL LFLVGSKKDL STPAQYSLME
KDALKVAQEI KAEYWAVSSL TGENVREFFF RVAALTFEAN VLADVEKSGA RHIADVVRIN
SDDKNLYLTA SKKKATCCP
