ID RB22A_MOUSE Reviewed; 194 AA.
AC P35285; Q3UCA7; Q91VD4;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 27-MAR-2024, entry version 190.
DE RecName: Full=Ras-related protein Rab-22A;
DE Short=Rab-22;
DE AltName: Full=Rab-14;
GN Name=Rab22a; Synonyms=Rab22;
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 [MRNA].
RA Kussmann S., Worch S., Hansmann I., Schlote D.;
RT "Mapping and characterization of mouse Rab22a gene.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-65.
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 [5]
RP TISSUE SPECIFICITY.
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RABGEF1.
RX PubMed=19759177; DOI=10.1091/mbc.e09-06-0453;
RA Zhu H., Liang Z., Li G.;
RT "Rabex-5 is a Rab22 effector and mediates a Rab22-Rab5 signaling cascade in
RT endocytosis.";
RL Mol. Biol. Cell 20:4720-4729(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).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLN-64.
RX PubMed=27718357; DOI=10.7554/elife.20417;
RA Qu F., Lorenzo D.N., King S.J., Brooks R., Bear J.E., Bennett V.;
RT "Ankyrin-B is a PI3P effector that promotes polarized alpha5beta1-integrin
RT recycling via recruiting RabGAP1L to early endosomes.";
RL Elife 5:0-0(2016).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) OF 2-169 IN COMPLEX WITH GTP ANALOG
RP AND ZFYVE20, AND INTERACTION WITH ZFYVE20.
RX PubMed=16034420; DOI=10.1038/nature03798;
RA Eathiraj S., Pan X., Ritacco C., Lambright D.G.;
RT "Structural basis of family-wide Rab GTPase recognition by rabenosyn-5.";
RL Nature 436:415-419(2005).
CC -!- FUNCTION: Plays a role in endocytosis and intracellular protein
CC transport (PubMed:19759177, PubMed:27718357). Mediates trafficking of
CC TF from early endosomes to recycling endosomes. Required for NGF-
CC mediated endocytosis of NTRK1, and subsequent neurite outgrowth. Binds
CC GTP and GDP and has low GTPase activity. Alternates between a GTP-bound
CC active form and a GDP-bound inactive form (By similarity).
CC {ECO:0000250|UniProtKB:Q9UL26, ECO:0000269|PubMed:19759177,
CC ECO:0000269|PubMed:27718357}.
CC -!- SUBUNIT: Binds EEA1 (By similarity). Interacts (in its GTP-bound form)
CC with RINL (By similarity). Interacts directly with ZFYVE20
CC (PubMed:16034420). Interacts (in its GTP-bound form) with RABGEF1
CC (PubMed:19759177). {ECO:0000250|UniProtKB:P51154,
CC ECO:0000250|UniProtKB:Q9UL26, ECO:0000269|PubMed:16034420,
CC ECO:0000269|PubMed:19759177}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:27718357};
CC Lipid-anchor {ECO:0000305}. Cell membrane
CC {ECO:0000250|UniProtKB:P51154}; Lipid-anchor {ECO:0000305}. Early
CC endosome {ECO:0000269|PubMed:19759177, ECO:0000269|PubMed:27718357}.
CC Late endosome {ECO:0000250|UniProtKB:P51154}. Cell projection, ruffle
CC {ECO:0000250|UniProtKB:Q9UL26}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:27718357}. 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 M.tuberculosis. {ECO:0000250|UniProtKB:Q9UL26}.
CC -!- TISSUE SPECIFICITY: Detected in brain and heart, and at lower levels in
CC lung and spleen. {ECO:0000269|PubMed:8126105}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AJ311124; CAC41378.1; -; mRNA.
DR EMBL; AK031667; BAC27501.1; -; mRNA.
DR EMBL; AK146594; BAE27289.1; -; mRNA.
DR EMBL; AK150617; BAE29707.1; -; mRNA.
DR EMBL; BC006596; AAH06596.1; -; mRNA.
DR EMBL; M79304; AAK14828.1; -; mRNA.
DR CCDS; CCDS38352.1; -.
DR PIR; JH0644; JH0644.
DR RefSeq; NP_077756.2; NM_024436.3.
DR PDB; 1YVD; X-ray; 1.93 A; A=3-169.
DR PDB; 1Z0J; X-ray; 1.32 A; A=2-169.
DR PDBsum; 1YVD; -.
DR PDBsum; 1Z0J; -.
DR AlphaFoldDB; P35285; -.
DR SMR; P35285; -.
DR BioGRID; 202539; 1.
DR DIP; DIP-60516N; -.
DR IntAct; P35285; 33.
DR STRING; 10090.ENSMUSP00000029024; -.
DR GlyGen; P35285; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P35285; -.
DR PhosphoSitePlus; P35285; -.
DR SwissPalm; P35285; -.
DR EPD; P35285; -.
DR PaxDb; 10090-ENSMUSP00000029024; -.
DR PeptideAtlas; P35285; -.
DR ProteomicsDB; 300246; -.
DR Pumba; P35285; -.
DR Antibodypedia; 29093; 176 antibodies from 30 providers.
DR DNASU; 19334; -.
DR Ensembl; ENSMUST00000029024.10; ENSMUSP00000029024.4; ENSMUSG00000027519.11.
DR GeneID; 19334; -.
DR KEGG; mmu:19334; -.
DR UCSC; uc008oed.1; mouse.
DR AGR; MGI:105072; -.
DR CTD; 57403; -.
DR MGI; MGI:105072; Rab22a.
DR VEuPathDB; HostDB:ENSMUSG00000027519; -.
DR eggNOG; KOG0092; Eukaryota.
DR GeneTree; ENSGT00940000157009; -.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; P35285; -.
DR OMA; CDLNDAR; -.
DR OrthoDB; 5483572at2759; -.
DR PhylomeDB; P35285; -.
DR TreeFam; TF331262; -.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR BioGRID-ORCS; 19334; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Rab22a; mouse.
DR EvolutionaryTrace; P35285; -.
DR PRO; PR:P35285; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P35285; Protein.
DR Bgee; ENSMUSG00000027519; Expressed in humerus cartilage element and 254 other cell types or tissues.
DR ExpressionAtlas; P35285; baseline and differential.
DR Genevisible; P35285; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0012505; C:endomembrane system; 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; ISO:MGI.
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; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0006897; P:endocytosis; ISO:MGI.
DR GO; GO:0007032; P:endosome organization; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0097494; P:regulation of vesicle size; ISO:MGI.
DR CDD; cd01860; Rab5_related; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR47977; RAS-RELATED PROTEIN RAB; 1.
DR PANTHER; PTHR47977:SF13; RAS-RELATED PROTEIN RAB-31 ISOFORM X1; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00176; RAN; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Cytoplasmic vesicle;
KW Endocytosis; Endosome; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..194
FT /note="Ras-related protein Rab-22A"
FT /id="PRO_0000121210"
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 BINDING 60..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 118..121
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 148..150
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
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: Constitutively active. Disrupts general
FT recycling of receptors in embryonic fibroblasts."
FT /evidence="ECO:0000269|PubMed:27718357"
FT CONFLICT 54
FT /note="H -> R (in Ref. 4; AAK14828)"
FT /evidence="ECO:0000305"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:1Z0J"
FT HELIX 18..27
FT /evidence="ECO:0007829|PDB:1Z0J"
FT STRAND 39..49
FT /evidence="ECO:0007829|PDB:1Z0J"
FT STRAND 52..61
FT /evidence="ECO:0007829|PDB:1Z0J"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:1Z0J"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:1Z0J"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:1Z0J"
FT HELIX 90..106
FT /evidence="ECO:0007829|PDB:1Z0J"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:1Z0J"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:1Z0J"
FT HELIX 130..139
FT /evidence="ECO:0007829|PDB:1Z0J"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:1Z0J"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:1Z0J"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:1Z0J"
SQ SEQUENCE 194 AA; 21802 MW; 1799B676CA9091F7 CRC64;
MALRELKVCL LGDTGVGKSS IVWRFVEDSF DPNINPTIGA SFMTKTVQYQ NELHKFLIWD
TAGQERFRAL APMYYRGSAA AIIVYDITKE ETFSTLKNWV RELRQHGPPS IVVAIAGNKC
DLTDVREVME RDAKDYADSI HAIFVETSAK NAININELFI EISRRIPSTD ANPASGGKGF
KLRRQPSEPK RSCC
//
