RAB21_MOUSE
ID RAB21_MOUSE Reviewed; 222 AA.
AC P35282; Q7TPN7;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Ras-related protein Rab-21;
DE AltName: Full=Rab-12;
DE Flags: Precursor;
GN Name=Rab21 {ECO:0000312|MGI:MGI:894308};
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 [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-77.
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 [3]
RP PROTEIN SEQUENCE OF 178-187, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP FUNCTION, INTERACTION WITH ITGA1; ITGA2; ITGA5; ITGA6; ITGA11 AND ITGB1,
RP MUTAGENESIS OF THR-31 AND GLN-76, AND SUBCELLULAR LOCATION.
RX PubMed=16754960; DOI=10.1083/jcb.200509019;
RA Pellinen T., Arjonen A., Vuoriluoto K., Kallio K., Fransen J.A.M.,
RA Ivaska J.;
RT "Small GTPase Rab21 regulates cell adhesion and controls endosomal traffic
RT of beta1-integrins.";
RL J. Cell Biol. 173:767-780(2006).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18804435; DOI=10.1016/j.devcel.2008.08.001;
RA Pellinen T., Tuomi S., Arjonen A., Wolf M., Edgren H., Meyer H., Grosse R.,
RA Kitzing T., Rantala J.K., Kallioniemi O., Faessler R., Kallio M.,
RA Ivaska J.;
RT "Integrin trafficking regulated by Rab21 is necessary for cytokinesis.";
RL Dev. Cell 15:371-385(2008).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=19745841; DOI=10.1038/embor.2009.186;
RA Burgo A., Sotirakis E., Simmler M.C., Verraes A., Chamot C., Simpson J.C.,
RA Lanzetti L., Proux-Gillardeaux V., Galli T.;
RT "Role of Varp, a Rab21 exchange factor and TI-VAMP/VAMP7 partner, in
RT neurite growth.";
RL EMBO Rep. 10:1117-1124(2009).
RN [7]
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: Small GTPase involved in membrane trafficking control
CC (PubMed:16754960, PubMed:18804435). Regulates integrin internalization
CC and recycling, but does not influence the traffic of endosomally
CC translocated receptors in general (PubMed:16754960). As a result, may
CC regulate cell adhesion and migration (PubMed:16754960). During the
CC mitosis of adherent cells, controls the endosomal trafficking of
CC integrins which is required for the successful completion of
CC cytokinesis (PubMed:18804435). Involved in neurite growth (By
CC similarity). Following SBF2/MTMT13-mediated activation in response to
CC starvation-induced autophagy, binds to and regulates SNARE protein
CC VAMP8 endolysosomal transport required for SNARE-mediated
CC autophagosome-lysosome fusion (By similarity). Modulates protein levels
CC of the cargo receptors TMED2 and TMED10, and required for appropriate
CC Golgi localization of TMED10 (By similarity).
CC {ECO:0000250|UniProtKB:Q6AXT5, ECO:0000250|UniProtKB:Q9UL25,
CC ECO:0000269|PubMed:16754960, ECO:0000269|PubMed:18804435}.
CC -!- SUBUNIT: Interacts with the cytoplasmic tail of integrins ITGA1, ITGA2,
CC ITGA5, ITGA6, ITGA11 and ITGB1; this interaction is dependent upon its
CC GDP/GTP cycle (PubMed:16754960). Interacts with RABGEF1 (via VPS9
CC domain) (By similarity). Interacts with ANKRD27 (By similarity).
CC Interacts with VAMP7 (By similarity). Interacts (in GTP-bound form)
CC with VAMP8 in response to starvation; the interaction probably
CC regulates VAMP8 endolysosomal trafficking (By similarity). Interacts
CC (active GTP-bound form) with TMED10; the interaction is indirect and
CC regulates TMED10 abundance and localization at the Golgi (By
CC similarity). {ECO:0000250|UniProtKB:Q9UL25,
CC ECO:0000269|PubMed:16754960}.
CC -!- INTERACTION:
CC P35282; P17301: ITGA2; Xeno; NbExp=7; IntAct=EBI-1993555, EBI-702960;
CC P35282; P05556: ITGB1; Xeno; NbExp=3; IntAct=EBI-1993555, EBI-703066;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16754960}; Lipid-anchor {ECO:0000305}. Golgi
CC apparatus, trans-Golgi network {ECO:0000269|PubMed:19745841}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:16754960}. Early endosome
CC membrane {ECO:0000269|PubMed:16754960}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:16754960}. Cleavage furrow
CC {ECO:0000269|PubMed:18804435}. Cell projection, neuron projection
CC {ECO:0000269|PubMed:19745841}. Note=Colocalizes with ANKRD27 and VAMP7
CC in neurites (PubMed:19745841). During mitosis, in mid-telophase,
CC localized in the ingressing cleavage furrow (PubMed:18804435). In late
CC telophase, detected at the opposite poles of the daughter cells, in
CC vesicles at the base of lamellipodia formed by the separating daughter
CC cells (PubMed:18804435). {ECO:0000269|PubMed:18804435,
CC ECO:0000269|PubMed:19745841}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; BC055042; AAH55042.1; -; mRNA.
DR EMBL; M79302; AAK14826.1; -; mRNA.
DR CCDS; CCDS24177.1; -.
DR PIR; A38879; A38879.
DR RefSeq; NP_077774.1; NM_024454.1.
DR AlphaFoldDB; P35282; -.
DR SMR; P35282; -.
DR BioGRID; 229733; 4.
DR IntAct; P35282; 35.
DR MINT; P35282; -.
DR STRING; 10090.ENSMUSP00000020343; -.
DR iPTMnet; P35282; -.
DR PhosphoSitePlus; P35282; -.
DR SwissPalm; P35282; -.
DR EPD; P35282; -.
DR jPOST; P35282; -.
DR PaxDb; P35282; -.
DR PeptideAtlas; P35282; -.
DR PRIDE; P35282; -.
DR ProteomicsDB; 300341; -.
DR Antibodypedia; 1484; 426 antibodies from 30 providers.
DR DNASU; 216344; -.
DR Ensembl; ENSMUST00000020343; ENSMUSP00000020343; ENSMUSG00000020132.
DR GeneID; 216344; -.
DR KEGG; mmu:216344; -.
DR UCSC; uc007haz.1; mouse.
DR CTD; 23011; -.
DR MGI; MGI:894308; Rab21.
DR VEuPathDB; HostDB:ENSMUSG00000020132; -.
DR eggNOG; KOG0088; Eukaryota.
DR GeneTree; ENSGT00940000156786; -.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; P35282; -.
DR OMA; DICLCIA; -.
DR OrthoDB; 1226895at2759; -.
DR PhylomeDB; P35282; -.
DR TreeFam; TF300199; -.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 216344; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Rab21; mouse.
DR PRO; PR:P35282; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P35282; protein.
DR Bgee; ENSMUSG00000020132; Expressed in aortic valve and 257 other tissues.
DR ExpressionAtlas; P35282; baseline and differential.
DR Genevisible; P35282; MM.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0098559; C:cytoplasmic side of early endosome membrane; ISO:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0032580; C:Golgi cisterna membrane; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0012506; C:vesicle membrane; ISO:MGI.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0008089; P:anterograde axonal transport; ISO:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:UniProtKB.
DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; ISO:MGI.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0032482; P:Rab protein signal transduction; IEA:InterPro.
DR GO; GO:0030516; P:regulation of axon extension; ISO:MGI.
DR GO; GO:0017157; P:regulation of exocytosis; ISO:MGI.
DR CDD; cd04123; Rab21; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041833; Rab21.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR020849; Small_GTPase_Ras-type.
DR PANTHER; PTHR24070; PTHR24070; 1.
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; Cytoplasmic vesicle;
KW Direct protein sequencing; Endoplasmic reticulum; Endosome;
KW Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UL25"
FT CHAIN 2..219
FT /note="Ras-related protein Rab-21"
FT /id="PRO_0000121206"
FT PROPEP 220..222
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370769"
FT MOTIF 46..54
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 24..32
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 72..76
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 130..133
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 160..162
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UL25"
FT MOD_RES 219
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 218
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 219
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 31
FT /note="T->N: Defects in GTP-binding. Decrease in integrin-
FT binding."
FT /evidence="ECO:0000269|PubMed:16754960"
FT MUTAGEN 76
FT /note="Q->L: Defects in GTP hydrolysis. Increase in
FT integrin-binding."
FT /evidence="ECO:0000269|PubMed:16754960"
SQ SEQUENCE 222 AA; 24106 MW; 7FB005C28E8D6954 CRC64;
MAAAGGGAAA AAGRAYSFKV VLLGEGCVGK TSLVLRYCEN KFNDKHITTL QASFLTKKLN
IGGKRVNLAI WDTAGQERFH ALGPIYYRDS NGAILVYDVT DEDSFQKVKN WVKELRKMLG
NEICLCIVGN KIDLEKERHV SIQEAESYAE SVGAKHYHTS AKQNKGIEEL FLDLCKRMIE
TAQVDERAKG NGSSQAGAAR RGVQIIDDEP QAQSSGGCCS SG
