RAB43_MOUSE
ID RAB43_MOUSE Reviewed; 210 AA.
AC Q8CG50;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Ras-related protein Rab-43;
GN Name=Rab43;
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=KM; TISSUE=Liver;
RA Guo J.H., Yu L.;
RT "Cloning, expression pattern and homology modeling of novel human and mouse
RT RAB genes.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, 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 [4]
RP PHOSPHORYLATION AT THR-80.
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).
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 set of downstream effectors directly responsible for vesicle
CC formation, movement, tethering and fusion. The low intrinsic GTPase
CC activity of RAB43 is activated by USP6NL. Involved in retrograde
CC transport from the endocytic pathway to the Golgi apparatus. Involved
CC in the transport of Shiga toxin from early and recycling endosomes to
CC the trans-Golgi network. Required for the structural integrity of the
CC Golgi complex. Plays a role in the maturation of phagosomes that engulf
CC pathogens, such as S.aureus and Mycobacterium.
CC -!- SUBUNIT: Interacts with GDI1, GDI2, CHM and CHML; phosphorylation at
CC Thr-80 disrupts these interactions. {ECO:0000250|UniProtKB:Q86YS6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome
CC {ECO:0000250|UniProtKB:Q86YS6}. Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}. Golgi apparatus {ECO:0000250|UniProtKB:Q86YS6}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}. Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:Q86YS6}. Note=Recruited to phagosomes containing
CC S.aureus or M.tuberculosis. {ECO:0000250|UniProtKB:Q86YS6}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AJ534465; CAD58914.1; -; mRNA.
DR CCDS; CCDS20329.1; -.
DR RefSeq; NP_001034483.1; NM_001039394.1.
DR AlphaFoldDB; Q8CG50; -.
DR SMR; Q8CG50; -.
DR BioGRID; 213709; 1.
DR IntAct; Q8CG50; 2.
DR STRING; 10090.ENSMUSP00000077716; -.
DR iPTMnet; Q8CG50; -.
DR PhosphoSitePlus; Q8CG50; -.
DR EPD; Q8CG50; -.
DR jPOST; Q8CG50; -.
DR MaxQB; Q8CG50; -.
DR PaxDb; Q8CG50; -.
DR PRIDE; Q8CG50; -.
DR ProteomicsDB; 255067; -.
DR Antibodypedia; 34842; 103 antibodies from 24 providers.
DR DNASU; 69834; -.
DR Ensembl; ENSMUST00000078647; ENSMUSP00000077716; ENSMUSG00000030055.
DR GeneID; 69834; -.
DR KEGG; mmu:69834; -.
DR UCSC; uc009ctx.1; mouse.
DR CTD; 339122; -.
DR MGI; MGI:1917084; Rab43.
DR VEuPathDB; HostDB:ENSMUSG00000030055; -.
DR eggNOG; KOG0084; Eukaryota.
DR GeneTree; ENSGT00940000161980; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; Q8CG50; -.
DR OMA; MFVMETS; -.
DR OrthoDB; 1149105at2759; -.
DR PhylomeDB; Q8CG50; -.
DR TreeFam; TF300097; -.
DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR BioGRID-ORCS; 69834; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Rab43; mouse.
DR PRO; PR:Q8CG50; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8CG50; protein.
DR Bgee; ENSMUSG00000030055; Expressed in granulocyte and 132 other tissues.
DR ExpressionAtlas; Q8CG50; baseline and differential.
DR Genevisible; Q8CG50; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0090382; P:phagosome maturation; ISS:UniProtKB.
DR GO; GO:0035526; P:retrograde transport, plasma membrane to Golgi; ISS:UniProtKB.
DR GO; GO:1901998; P:toxin transport; IMP:MGI.
DR GO; GO:0019068; P:virion assembly; ISO:MGI.
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 Cytoplasmic vesicle; Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Reference proteome.
FT CHAIN 1..210
FT /note="Ras-related protein Rab-43"
FT /id="PRO_0000244616"
FT MOTIF 45..53
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 23..30
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 71..75
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 129..132
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 161..162
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 80
FT /note="Phosphothreonine; by LRRK2"
FT /evidence="ECO:0000269|PubMed:29125462"
FT MOD_RES 210
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 208
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 210
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 210 AA; 23263 MW; 4D7DF82526A6ED02 CRC64;
MAGPGPGDQD EHYDFLFKLV LVGDASVGKT CVVQRFKTGA FSARQGSTIG VDFTMKTLEI
QGKRVKLQIW DTAGQERFRT ITQSYYRSAN GAILAYDISK RSTFLSVPHW IEDVRKYAGS
NIVQLLIGNK SDLADFREVP LAEAQSLAEH YDILCAIETS AKDSSNVEEA FTRVATELIM
RHGGPMFSEK NTDHIQLDSK DIAESWGCGC
