RAB21_CANLF
ID RAB21_CANLF Reviewed; 223 AA.
AC P55745;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Ras-related protein Rab-21;
DE Flags: Precursor;
GN Name=RAB21;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RA Chavrier P.;
RT "Rab21.";
RL (In) Zerial M., Huber L.A. (eds.);
RL Guidebook to the small GTPases, pp.365-366, Oxford University Press, Oxford
RL (1995).
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. As a result, may regulate cell adhesion and migration. During
CC the mitosis of adherent cells, controls the endosomal trafficking of
CC integrins which is required for the successful completion of
CC cytokinesis (By similarity). Involved in neurite growth (By
CC similarity). Modulates protein levels of the cargo receptors TMED2 and
CC TMED10, and required for appropriate Golgi localization of TMED10 (By
CC similarity). {ECO:0000250, 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. Interacts with ANKRD27 (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, ECO:0000250|UniProtKB:Q96NW4,
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}.
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DR AlphaFoldDB; P55745; -.
DR SMR; P55745; -.
DR STRING; 9612.ENSCAFP00000000675; -.
DR PaxDb; P55745; -.
DR Ensembl; ENSCAFT00000100886; ENSCAFP00000070287; ENSCAFG00000000458.
DR Ensembl; ENSCAFT00030009177; ENSCAFP00030008046; ENSCAFG00030004923.
DR Ensembl; ENSCAFT00040022225; ENSCAFP00040019274; ENSCAFG00040011919.
DR Ensembl; ENSCAFT00845041845; ENSCAFP00845032823; ENSCAFG00845023570.
DR VEuPathDB; HostDB:ENSCAFG00845023570; -.
DR VGNC; VGNC:45261; RAB21.
DR eggNOG; KOG0088; Eukaryota.
DR GeneTree; ENSGT00390000017998; -.
DR InParanoid; P55745; -.
DR Proteomes; UP000002254; Chromosome 10.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
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:0005886; C:plasma membrane; IBA:GO_Central.
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:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032482; P:Rab protein signal transduction; IEA:InterPro.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
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 3: Inferred from homology;
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_0000121204"
FT PROPEP 221..223
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370767"
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; 24161 MW; B9D198C48442294D CRC64;
MAAAGGGGGG AAGRAYSFKV VLLGEGCVGK TSLVLRYCEN KFNDKHITTL QASFLTKKLN
IGGKRVNLAI WDTAGQERFH ALGPIYYRDS NGAILVYDIT DEDSFQKVKN WVKELRKMLG
NEICLCIVGN KIDLEKERHV SIQEAESYAE SVGAKHYHTS AKQNKGIEEL FLDLCKRMIE
TAQVDERAKG NGSSQPGAAR RGVQIIDDEP QAQSSGGGCC SSG
