RB22A_HUMAN
ID RB22A_HUMAN Reviewed; 194 AA.
AC Q9UL26; B3KR86; E1P605; Q8TF12; Q9H4E6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Ras-related protein Rab-22A;
DE Short=Rab-22;
GN Name=RAB22A; Synonyms=RAB22;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ding J.B., Yu L., Zhao S.Y.;
RT "Cloning of a novel human cDNA similar to Canis familiaris mRNA for Rab22
RT protein.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon carcinoma;
RX PubMed=10887961; DOI=10.1078/s0171-9335(04)70034-5;
RA Opdam F.J.M., Kamps G., Croes H., van Bokhoven H., Ginsel L.A.,
RA Fransen J.A.M.;
RT "Expression of Rab small GTPases in epithelial Caco-2 cells: Rab21 is an
RT apically located GTP-binding protein in polarised intestinal epithelial
RT cells.";
RL Eur. J. Cell Biol. 79:308-316(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kussmann S., Hansmann I., Schlote D.;
RT "Mapping and characterization of the human RAB22A gene.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Uterus;
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLN-64.
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).
RN [10]
RP INTERACTION WITH RINL, MUTAGENESIS OF SER-19 AND GLN-64, AND SUBCELLULAR
RP LOCATION.
RX PubMed=21419809; DOI=10.1016/j.bbamcr.2011.03.005;
RA Woller B., Luiskandl S., Popovic M., Prieler B.E., Ikonge G., Mutzl M.,
RA Rehmann H., Herbst R.;
RT "Rin-like, a novel regulator of endocytosis, acts as guanine nucleotide
RT exchange factor for Rab5a and Rab22.";
RL Biochim. Biophys. Acta 1813:1198-1210(2011).
RN [11]
RP FUNCTION, AND INTERACTION WITH RABGEF1.
RX PubMed=21849477; DOI=10.1091/mbc.e11-03-0277;
RA Wang L., Liang Z., Li G.;
RT "Rab22 controls NGF signaling and neurite outgrowth in PC12 cells.";
RL Mol. Biol. Cell 22:3853-3860(2011).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=21255211; DOI=10.1111/j.1600-0854.2011.01165.x;
RA Seto S., Tsujimura K., Koide Y.;
RT "Rab GTPases regulating phagosome maturation are differentially recruited
RT to mycobacterial phagosomes.";
RL Traffic 12:407-420(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Plays a role in endocytosis and intracellular protein
CC transport. Mediates trafficking of TF from early endosomes to recycling
CC endosomes (PubMed:16537905). Required for NGF-mediated endocytosis of
CC NTRK1, and subsequent neurite outgrowth (PubMed:21849477). Binds GTP
CC and GDP and has low GTPase activity. Alternates between a GTP-bound
CC active form and a GDP-bound inactive form (PubMed:16537905).
CC {ECO:0000269|PubMed:16537905, ECO:0000269|PubMed:21849477}.
CC -!- SUBUNIT: Interacts directly with ZFYVE20 (By similarity). Binds EEA1
CC (By similarity). Interacts (in its GTP-bound form) with RABGEF1
CC (PubMed:21849477). Interacts (in its GTP-bound form) with RINL
CC (PubMed:21419809). {ECO:0000250|UniProtKB:P35285,
CC ECO:0000250|UniProtKB:P51154, ECO:0000269|PubMed:21419809,
CC ECO:0000269|PubMed:21849477}.
CC -!- INTERACTION:
CC Q9UL26; Q60I27: ALS2CL; NbExp=3; IntAct=EBI-399456, EBI-12078276;
CC Q9UL26; Q8NEU8: APPL2; NbExp=8; IntAct=EBI-399456, EBI-741261;
CC Q9UL26; Q15075: EEA1; NbExp=3; IntAct=EBI-399456, EBI-298113;
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:P51154};
CC Lipid-anchor {ECO:0000305}. Cell membrane
CC {ECO:0000250|UniProtKB:P51154}; Lipid-anchor {ECO:0000305}. Early
CC endosome {ECO:0000269|PubMed:16537905}. Late endosome
CC {ECO:0000250|UniProtKB:P51154}. Cell projection, ruffle
CC {ECO:0000269|PubMed:21419809}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:21419809}. Cytoplasmic vesicle, phagosome
CC {ECO:0000269|PubMed:21255211}. 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:0000269|PubMed:21255211}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AF125104; AAL75941.1; -; mRNA.
DR EMBL; AF091034; AAF00047.2; -; mRNA.
DR EMBL; AJ276210; CAC10538.1; -; mRNA.
DR EMBL; BT007046; AAP35695.1; -; mRNA.
DR EMBL; AK091180; BAG52298.1; -; mRNA.
DR EMBL; AL035455; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75496.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75497.1; -; Genomic_DNA.
DR EMBL; BC015710; AAH15710.1; -; mRNA.
DR EMBL; BC063457; AAH63457.1; -; mRNA.
DR CCDS; CCDS33497.1; -.
DR RefSeq; NP_065724.1; NM_020673.2.
DR AlphaFoldDB; Q9UL26; -.
DR SMR; Q9UL26; -.
DR BioGRID; 121505; 21.
DR IntAct; Q9UL26; 9.
DR MINT; Q9UL26; -.
DR STRING; 9606.ENSP00000244040; -.
DR ChEMBL; CHEMBL4295981; -.
DR iPTMnet; Q9UL26; -.
DR PhosphoSitePlus; Q9UL26; -.
DR BioMuta; RAB22A; -.
DR DMDM; 13633614; -.
DR EPD; Q9UL26; -.
DR jPOST; Q9UL26; -.
DR MassIVE; Q9UL26; -.
DR MaxQB; Q9UL26; -.
DR PaxDb; Q9UL26; -.
DR PeptideAtlas; Q9UL26; -.
DR PRIDE; Q9UL26; -.
DR ProteomicsDB; 84935; -.
DR Antibodypedia; 29093; 160 antibodies from 30 providers.
DR DNASU; 57403; -.
DR Ensembl; ENST00000244040.4; ENSP00000244040.3; ENSG00000124209.4.
DR GeneID; 57403; -.
DR KEGG; hsa:57403; -.
DR MANE-Select; ENST00000244040.4; ENSP00000244040.3; NM_020673.3; NP_065724.1.
DR UCSC; uc002xyz.4; human.
DR CTD; 57403; -.
DR DisGeNET; 57403; -.
DR GeneCards; RAB22A; -.
DR HGNC; HGNC:9764; RAB22A.
DR HPA; ENSG00000124209; Low tissue specificity.
DR MIM; 612966; gene.
DR neXtProt; NX_Q9UL26; -.
DR OpenTargets; ENSG00000124209; -.
DR PharmGKB; PA34112; -.
DR VEuPathDB; HostDB:ENSG00000124209; -.
DR eggNOG; KOG0092; Eukaryota.
DR GeneTree; ENSGT00940000157009; -.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; Q9UL26; -.
DR OMA; SESHRTC; -.
DR OrthoDB; 1340129at2759; -.
DR PhylomeDB; Q9UL26; -.
DR TreeFam; TF331262; -.
DR PathwayCommons; Q9UL26; -.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR SignaLink; Q9UL26; -.
DR SIGNOR; Q9UL26; -.
DR BioGRID-ORCS; 57403; 8 hits in 1075 CRISPR screens.
DR ChiTaRS; RAB22A; human.
DR GeneWiki; RAB22A; -.
DR GenomeRNAi; 57403; -.
DR Pharos; Q9UL26; Tbio.
DR PRO; PR:Q9UL26; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9UL26; protein.
DR Bgee; ENSG00000124209; Expressed in middle temporal gyrus and 208 other tissues.
DR Genevisible; Q9UL26; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IMP:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IMP:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IDA:UniProtKB.
DR GO; GO:0007032; P:endosome organization; IEP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0097494; P:regulation of vesicle size; IMP:UniProtKB.
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_0000121209"
FT REGION 174..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 19
FT /note="S->L: Loss of GTPase activity."
FT /evidence="ECO:0000269|PubMed:21419809"
FT MUTAGEN 64
FT /note="Q->L: Constitutive GTPase activity. Impairs normal
FT protein trafficking through early endosomes."
FT /evidence="ECO:0000269|PubMed:16537905,
FT ECO:0000269|PubMed:21419809"
FT CONFLICT 184
FT /note="R -> K (in Ref. 3; CAC10538)"
FT /evidence="ECO:0000305"
FT CONFLICT 192..193
FT /note="SC -> TA (in Ref. 1; AAL75941)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 194 AA; 21855 MW; EBC84711DA3F839B CRC64;
MALRELKVCL LGDTGVGKSS IVWRFVEDSF DPNINPTIGA SFMTKTVQYQ NELHKFLIWD
TAGQERFRAL APMYYRGSAA AIIVYDITKE ETFSTLKNWV KELRQHGPPN IVVAIAGNKC
DLIDVREVME RDAKDYADSI HAIFVETSAK NAININELFI EISRRIPSTD ANLPSGGKGF
KLRRQPSEPK RSCC
