RAB21_BOVIN
ID RAB21_BOVIN Reviewed; 222 AA.
AC Q17R06;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Ras-related protein Rab-21;
DE Flags: Precursor;
GN Name=RAB21;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). 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:Q6AXT5,
CC ECO:0000250|UniProtKB:Q9UL25}.
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:Q9UL25}; Lipid-anchor {ECO:0000305}. Golgi
CC apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9UL25}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:Q9UL25}. Early endosome
CC membrane {ECO:0000250|UniProtKB:Q9UL25}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q9UL25}. Cleavage furrow
CC {ECO:0000250|UniProtKB:Q9UL25}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:P35282}. Note=Colocalizes with ANKRD27 and VAMP7
CC in neurites (By similarity). In nonpolarized epithelial Caco-2 cells,
CC found in the endoplasmic reticulum; in polarized cells, observed in
CC vesicles in the apical cytoplasm. During mitosis, in mid-telophase,
CC localized in the ingressing cleavage furrow. In late telophase,
CC detected at the opposite poles of the daughter cells, in vesicles at
CC the base of lamellipodia formed by the separating daughter cells (By
CC similarity). {ECO:0000250|UniProtKB:P35282,
CC ECO:0000250|UniProtKB:Q9UL25}.
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; BC118088; AAI18089.1; -; mRNA.
DR RefSeq; NP_001068785.1; NM_001075317.1.
DR AlphaFoldDB; Q17R06; -.
DR SMR; Q17R06; -.
DR PaxDb; Q17R06; -.
DR PeptideAtlas; Q17R06; -.
DR PRIDE; Q17R06; -.
DR Ensembl; ENSBTAT00000086555; ENSBTAP00000062568; ENSBTAG00000053598.
DR GeneID; 507488; -.
DR KEGG; bta:507488; -.
DR CTD; 23011; -.
DR VEuPathDB; HostDB:ENSBTAG00000053598; -.
DR eggNOG; KOG0088; Eukaryota.
DR GeneTree; ENSGT00940000156786; -.
DR InParanoid; Q17R06; -.
DR OMA; DICLCIA; -.
DR OrthoDB; 1226895at2759; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000053598; Expressed in oocyte and 103 other tissues.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
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:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0032482; P:Rab protein signal transduction; IEA:InterPro.
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..219
FT /note="Ras-related protein Rab-21"
FT /id="PRO_0000283074"
FT PROPEP 220..222
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370766"
FT MOTIF 45..53
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 23..31
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 159..161
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"
SQ SEQUENCE 222 AA; 24146 MW; C43549CCF7EAF20C CRC64;
MAAAGGGGAA AGRTYSFKVV LLGEGCVGKT SLVLRYCENK FNDKHITTLQ ASFLTKKLNI
GGKRVNLAIW DTAGQERFHA LGPIYYRDSN GAILVYDITD EDSFQKVKNW VKELRKMLGN
EICLCIVGNK VDLEKERHVS IQEAESYAES VGAKHYHTSA KQNKGIEELF LDLCKRMIET
AQVDERAKGN GSSQPGAARR GVQIIDDEPQ AQSVGGGCCS SG
