RB22A_CANLF
ID RB22A_CANLF Reviewed; 194 AA.
AC P51154;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Ras-related protein Rab-22A;
DE Short=Rab-22;
GN Name=RAB22A; Synonyms=RAB22;
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 [MRNA], AND SUBCELLULAR LOCATION.
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 SEQUENCE REVISION.
RA Olkkonen V.M.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, INTERACTION WITH EEA1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLN-64.
RX PubMed=11870209; DOI=10.1242/jcs.115.5.899;
RA Kauppi M., Simonsen A., Bremnes B., Vieira A., Callaghan J.M., Stenmark H.,
RA Olkkonen V.M.;
RT "The small GTPase Rab22 interacts with EEA1 and controls endosomal membrane
RT trafficking.";
RL J. Cell Sci. 115:899-911(2002).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16537905; DOI=10.1128/mcb.26.7.2595-2614.2006;
RA Magadan J.G., Barbieri M.A., Mesa R., Stahl P.D., Mayorga L.S.;
RT "Rab22a regulates the sorting of transferrin to recycling endosomes.";
RL Mol. Cell. Biol. 26:2595-2614(2006).
CC -!- FUNCTION: Plays a role in endocytosis and intracellular protein
CC transport (PubMed:11870209, PubMed:16537905). Mediates trafficking of
CC TF from early endosomes to recycling endosomes (PubMed:16537905).
CC Required for NGF-mediated endocytosis of NTRK1, and subsequent neurite
CC outgrowth (By similarity). Binds GTP and GDP and has low GTPase
CC activity. Alternates between a GTP-bound active form and a GDP-bound
CC inactive form (PubMed:11870209). {ECO:0000250|UniProtKB:Q9UL26,
CC ECO:0000269|PubMed:11870209, ECO:0000269|PubMed:16537905}.
CC -!- SUBUNIT: Interacts directly with ZFYVE20 (By similarity). Interacts (in
CC its GTP-bound form) with RINL and RABGEF1 (By similarity). Binds EEA1
CC (PubMed:11870209). {ECO:0000250|UniProtKB:P35285,
CC ECO:0000250|UniProtKB:Q9UL26, ECO:0000269|PubMed:11870209}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:8126105};
CC Lipid-anchor {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:11870209,
CC ECO:0000269|PubMed:8126105}; Lipid-anchor {ECO:0000305}. Early endosome
CC {ECO:0000269|PubMed:11870209, ECO:0000269|PubMed:16537905,
CC ECO:0000269|PubMed:8126105}. Late endosome
CC {ECO:0000269|PubMed:8126105}. Cell projection, ruffle
CC {ECO:0000250|UniProtKB:Q9UL26}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:8126105}. Cytoplasmic vesicle, phagosome
CC {ECO:0000250|UniProtKB:Q9UL26}. Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}. Note=Recruited to phagosomes containing S.aureus or
CC Mycobacterium. {ECO:0000250|UniProtKB:Q9UL26}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; Z22820; CAA80473.1; -; mRNA.
DR PIR; S40208; S40208.
DR RefSeq; NP_001003208.1; NM_001003208.1.
DR AlphaFoldDB; P51154; -.
DR SMR; P51154; -.
DR STRING; 9612.ENSCAFP00000017821; -.
DR PaxDb; P51154; -.
DR GeneID; 403864; -.
DR KEGG; cfa:403864; -.
DR CTD; 57403; -.
DR eggNOG; KOG0092; Eukaryota.
DR InParanoid; P51154; -.
DR OrthoDB; 1340129at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
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 Cell membrane; Cell projection; Cytoplasmic vesicle; Endocytosis; Endosome;
KW GTP-binding; Lipoprotein; Membrane; Nucleotide-binding; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..194
FT /note="Ras-related protein Rab-22A"
FT /id="PRO_0000121208"
FT REGION 170..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 34..42
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 12..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 60..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 118..121
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 148..150
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 193
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 194
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 64
FT /note="Q->L: Impairs normal protein trafficking through
FT early endosomes."
FT /evidence="ECO:0000269|PubMed:11870209"
SQ SEQUENCE 194 AA; 21724 MW; E5930F84CFCB9B0B CRC64;
MALRELKVCL LGDTGVGKSS IVWRFVEDSF DPNINPTIGA SFMTKTVQYQ NELHKFLIWD
TAGQEAFRAL APMYYRGSAA AIIVYDITKE ETFSTLKNWV KELRQHGPPN IVVAIAGNKC
DLIDVREVME RDAKDYADSI HAIFVETSAK NAININELFI EISRRIPSAD ANPPSGGKGF
KLRRQPSEPQ RSCC
