RAB24_MOUSE
ID RAB24_MOUSE Reviewed; 203 AA.
AC P35290;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Ras-related protein Rab-24;
DE AltName: Full=Rab-16;
GN Name=Rab24;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=8126105; DOI=10.1242/jcs.106.4.1249;
RA Olkkonen V.M., Dupree P., Killisch I., Luetcke A., Simons K., Zerial M.;
RT "Molecular cloning and subcellular localization of three GTP-binding
RT proteins of the rab subfamily.";
RL J. Cell Sci. 106:1249-1261(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary gland;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-68.
RC TISSUE=Kidney;
RX PubMed=1555775; DOI=10.1016/0378-1119(92)90387-5;
RA Chavrier P., Simons K., Zerial M.;
RT "The complexity of the Rab and Rho GTP-binding protein subfamilies revealed
RT by a PCR cloning approach.";
RL Gene 112:261-264(1992).
RN [4]
RP SUBCELLULAR LOCATION, ISOPRENYLATION, LACK OF INTERACTION WITH ARHGDIA AND
RP ARHGDIB, AND MUTAGENESIS OF SER-67.
RX PubMed=10660536; DOI=10.1074/jbc.275.6.3848;
RA Erdman R.A., Shellenberger K.E., Overmeyer J.H., Maltese W.A.;
RT "Rab24 is an atypical member of the Rab GTPase family. Deficient GTPase
RT activity, GDP dissociation inhibitor interaction, and prenylation of Rab24
RT expressed in cultured cells.";
RL J. Biol. Chem. 275:3848-3856(2000).
RN [5]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-22; THR-120 AND ASP-123.
RX PubMed=12323076; DOI=10.1186/1471-2121-3-25;
RA Maltese W.A., Soule G., Gunning W., Calomeni E., Alexander B.;
RT "Mutant Rab24 GTPase is targeted to nuclear inclusions.";
RL BMC Cell Biol. 3:25-25(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
CC -!- FUNCTION: May be involved in autophagy-related processes.
CC -!- SUBUNIT: Unlike other Rab family members, does not interact with GDP
CC dissociation inhibitors (GDIs), including ARHGDIA and ARHGDIB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10660536,
CC ECO:0000269|PubMed:12323076}. Membrane {ECO:0000269|PubMed:10660536,
CC ECO:0000269|PubMed:12323076}; Lipid-anchor {ECO:0000305}. Note=Only
CC about 20% is recovered in the particulate fraction.
CC {ECO:0000269|PubMed:10660536}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in brain.
CC {ECO:0000269|PubMed:8126105}.
CC -!- PTM: Isoprenylation is inefficient compared to other Rab family
CC members. {ECO:0000269|PubMed:10660536}.
CC -!- MISCELLANEOUS: The unusual Ser-67, instead of a conserved Gln in other
CC family members, is the cause of low GTPase activity. As a result, the
CC predominant nucleotide associated with the protein is GTP.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z22819; CAA80472.1; -; mRNA.
DR EMBL; BC019950; AAH19950.1; -; mRNA.
DR EMBL; BC054466; AAH54466.1; -; mRNA.
DR EMBL; BC055894; AAH55894.1; -; mRNA.
DR EMBL; M79306; AAK14830.1; -; mRNA.
DR CCDS; CCDS26541.1; -.
DR PIR; JH0646; JH0646.
DR PIR; S40235; S40235.
DR RefSeq; NP_033026.1; NM_009000.3.
DR AlphaFoldDB; P35290; -.
DR SMR; P35290; -.
DR IntAct; P35290; 4.
DR MINT; P35290; -.
DR STRING; 10090.ENSMUSP00000046188; -.
DR iPTMnet; P35290; -.
DR PhosphoSitePlus; P35290; -.
DR EPD; P35290; -.
DR jPOST; P35290; -.
DR PaxDb; P35290; -.
DR PeptideAtlas; P35290; -.
DR PRIDE; P35290; -.
DR ProteomicsDB; 300342; -.
DR Antibodypedia; 29222; 285 antibodies from 24 providers.
DR DNASU; 19336; -.
DR Ensembl; ENSMUST00000035242; ENSMUSP00000046188; ENSMUSG00000034789.
DR GeneID; 19336; -.
DR KEGG; mmu:19336; -.
DR UCSC; uc007qqk.1; mouse.
DR CTD; 53917; -.
DR MGI; MGI:105065; Rab24.
DR VEuPathDB; HostDB:ENSMUSG00000034789; -.
DR eggNOG; KOG0092; Eukaryota.
DR GeneTree; ENSGT00910000144316; -.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; P35290; -.
DR OMA; TAKYWIQ; -.
DR OrthoDB; 1340129at2759; -.
DR PhylomeDB; P35290; -.
DR TreeFam; TF300199; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR BioGRID-ORCS; 19336; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Rab24; mouse.
DR PRO; PR:P35290; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P35290; protein.
DR Bgee; ENSMUSG00000034789; Expressed in granulocyte and 267 other tissues.
DR ExpressionAtlas; P35290; baseline and differential.
DR Genevisible; P35290; MM.
DR GO; GO:0005776; C:autophagosome; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR CDD; cd04118; Rab24; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041828; Rab24.
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; Cytoplasm; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..203
FT /note="Ras-related protein Rab-24"
FT /id="PRO_0000121214"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 14..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 120..123
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 154..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 200
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 201
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 22
FT /note="S->N: Predominantly in the GTP-bound state. No
FT effect on subcellular location."
FT /evidence="ECO:0000269|PubMed:12323076"
FT MUTAGEN 67
FT /note="S->Q: Increase in GTPase activity. No effect neither
FT on prenylation, nor on subcellular location."
FT /evidence="ECO:0000269|PubMed:10660536"
FT MUTAGEN 120
FT /note="T->A,I: Accumulates in punctate structures in both
FT cytoplasmic and nuclear compartments."
FT /evidence="ECO:0000269|PubMed:12323076"
FT MUTAGEN 123
FT /note="D->I: Accumulates in punctate structures in both
FT cytoplasmic and nuclear compartments. Disrupts the
FT integrity of the nuclear envelope."
FT /evidence="ECO:0000269|PubMed:12323076"
FT CONFLICT 67
FT /note="S -> Q (in Ref. 3; AAK14830)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 203 AA; 23144 MW; 872EA5E2E7B5B0F0 CRC64;
MSGQRVDVKV VMLGKEYVGK TSLVERYVHD RFLVGPYQNT IGAAFVAKVM CVGDRTVTLG
IWDTAGSERY EAMSRIYYRG AKAAIVCYDL TDSSSFERAK FWVKELRSLE EGCQIYLCGT
KSDLLEEDRR RRRVDFHDVQ DYADNIKAQL FETSSKTGQS VDELFQKVAE DYVSVAAFQV
MTEDKGVDLS QKANPYFYSC CHH
