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   27-MAR-2024, entry version 190.
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,
RC   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).
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}.
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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; 10090-ENSMUSP00000046188; -.
DR   PeptideAtlas; P35290; -.
DR   ProteomicsDB; 300342; -.
DR   Pumba; P35290; -.
DR   Antibodypedia; 29222; 320 antibodies from 24 providers.
DR   DNASU; 19336; -.
DR   Ensembl; ENSMUST00000035242.9; ENSMUSP00000046188.8; ENSMUSG00000034789.9.
DR   GeneID; 19336; -.
DR   KEGG; mmu:19336; -.
DR   UCSC; uc007qqk.1; mouse.
DR   AGR; MGI:105065; -.
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; RFRAGPY; -.
DR   OrthoDB; 2915497at2759; -.
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 78 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 271 other cell types or tissues.
DR   ExpressionAtlas; P35290; baseline and differential.
DR   GO; GO:0005776; C:autophagosome; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0012505; C:endomembrane system; 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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR041828; Rab24.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR47978; -; 1.
DR   PANTHER; PTHR47978:SF71; RAB24, MEMBER RAS ONCOGENE FAMILY; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00176; RAN; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51419; RAB; 1.
DR   Genevisible; P35290; MM.
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
//