RAB21_RAT
ID RAB21_RAT Reviewed; 223 AA.
AC Q6AXT5;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Ras-related protein Rab-21;
DE Flags: Precursor;
GN Name=Rab21;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 FUNCTION, AND 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).
CC -!- FUNCTION: Small GTPase involved in membrane trafficking control (By
CC similarity). Regulates integrin internalization and recycling, but does
CC not influence the traffic of endosomally translocated receptors in
CC general (By similarity). As a result, may regulate cell adhesion and
CC migration (By similarity). During the mitosis of adherent cells,
CC controls the endosomal trafficking of integrins which is required for
CC the successful completion of cytokinesis (By similarity). Involved in
CC neurite growth (PubMed:19745841). Following SBF2/MTMT13-mediated
CC activation in response to starvation-induced autophagy, binds to and
CC regulates SNARE protein VAMP8 endolysosomal transport required for
CC SNARE-mediated autophagosome-lysosome fusion (By similarity). Modulates
CC protein levels of the cargo receptors TMED2 and TMED10, and required
CC for appropriate Golgi localization of TMED10 (By similarity).
CC {ECO:0000250|UniProtKB:P35282, ECO:0000250|UniProtKB:Q9UL25,
CC ECO:0000269|PubMed:19745841}.
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 (By similarity). Interacts with RABGEF1 (via VPS9 domain)
CC (By similarity). Interacts with ANKRD27 (By similarity). Interacts (in
CC GTP-bound form) with VAMP8 in response to starvation; the interaction
CC probably regulates VAMP8 endolysosomal trafficking (By similarity).
CC Interacts (active GTP-bound form) with TMED10; the interaction is
CC indirect and regulates TMED10 abundance and localization at the Golgi
CC (By similarity). {ECO:0000250|UniProtKB:P35282,
CC ECO:0000250|UniProtKB:Q9UL25}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P35282}; Lipid-anchor {ECO:0000305}. Golgi
CC apparatus, trans-Golgi network {ECO:0000269|PubMed:19745841}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:P35282}. Early endosome
CC membrane {ECO:0000250|UniProtKB:P35282}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P35282}. Cleavage furrow
CC {ECO:0000250|UniProtKB:P35282}. 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 (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:P35282,
CC ECO:0000269|PubMed:19745841}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; BC079323; AAH79323.1; -; mRNA.
DR RefSeq; NP_001004238.1; NM_001004238.1.
DR AlphaFoldDB; Q6AXT5; -.
DR SMR; Q6AXT5; -.
DR STRING; 10116.ENSRNOP00000005258; -.
DR iPTMnet; Q6AXT5; -.
DR PhosphoSitePlus; Q6AXT5; -.
DR jPOST; Q6AXT5; -.
DR PaxDb; Q6AXT5; -.
DR PRIDE; Q6AXT5; -.
DR Ensembl; ENSRNOT00000005258; ENSRNOP00000005258; ENSRNOG00000003923.
DR GeneID; 299799; -.
DR KEGG; rno:299799; -.
DR UCSC; RGD:1303150; rat.
DR CTD; 23011; -.
DR RGD; 1303150; Rab21.
DR eggNOG; KOG0088; Eukaryota.
DR GeneTree; ENSGT00940000156786; -.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; Q6AXT5; -.
DR OMA; DICLCIA; -.
DR OrthoDB; 1226895at2759; -.
DR PhylomeDB; Q6AXT5; -.
DR TreeFam; TF300199; -.
DR Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR Reactome; R-RNO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:Q6AXT5; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000003923; Expressed in esophagus and 19 other tissues.
DR Genevisible; Q6AXT5; RN.
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:RGD.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:RGD.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032580; C:Golgi cisterna membrane; ISO:RGD.
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; IDA:SynGO.
DR GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
DR GO; GO:0012506; C:vesicle membrane; ISO:RGD.
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; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISO:RGD.
DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; ISO:RGD.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISO:RGD.
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; IDA:UniProtKB.
DR GO; GO:0017157; P:regulation of exocytosis; ISO:RGD.
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 2: Evidence at transcript level;
KW Acetylation; Cell projection; Cytoplasmic vesicle; Endoplasmic reticulum;
KW Endosome; 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..220
FT /note="Ras-related protein Rab-21"
FT /id="PRO_0000312571"
FT PROPEP 221..223
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370770"
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 220
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 219
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 220
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 223 AA; 24163 MW; BCF6701EC2884D74 CRC64;
MAAAGGGAAA AAGRAYSFKV VLLGEGCVGK TSLVLRYCEN KFNDKHITTL QASFLTKKLN
IGGKRVNLAI WDTAGQERFH ALGPIYYRDS NGAILVYDVT DEDSFQKVKN WVKELRKMLG
NEICLCIVGN KIDLEKERHV SIQEAESYAE SVGAKHYHTS AKQNKGIEEL FLDLCKRMIE
TAQVDERAKG NGSSQAGAAR RGVQIIDDEP QAQSGSGGCC SSG
