RBCC

Full text data of RAB22A

RAB22A (RAB22) [Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Ras-related protein Rab-22A; Rab-22

UniProt Q9UL26
ID RB22A_HUMAN Reviewed; 194 AA.
AC Q9UL26; B3KR86; E1P605; Q8TF12; Q9H4E6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 2.
DT 22-JAN-2014, entry version 121.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT Rab22 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
RT an apically located GTP-binding protein in polarised intestinal
RT epithelial 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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA 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.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RP SUBCELLULAR LOCATION.
RX PubMed=21419809; DOI=10.1016/j.bbamcr.2011.03.005;
RA Woller B., Luiskandl S., Popovic M., Prieler B.E., Ikonge G.,
RA Mutzl M., Rehmann H., Herbst R.;
RT "Rin-like, a novel regulator of endocytosis, acts as guanine
RT nucleotide 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
RT recruited to mycobacterial phagosomes.";
RL Traffic 12:407-420(2011).
CC -!- FUNCTION: Plays a role in endocytosis and intracellular protein
CC transport. Mediates trafficking of TF from early endosomes to
CC recycling endosomes. Required for NGF-mediated endocytosis of
CC NTRK1, and subsequent neurite outgrowth. Binds GTP and GDP and has
CC low GTPase activity. Alternates between a GTP-bound active form
CC and a GDP-bound inactive form.
CC -!- SUBUNIT: Interacts directly with ZFYVE20 (By similarity). Binds
CC EEA1 (By similarity). Interacts (in its GTP-bound form) with
CC RABGEF1. Interacts (in its GTP-bound form) with RINL.
CC -!- INTERACTION:
CC Q15075:EEA1; NbExp=3; IntAct=EBI-399456, EBI-298113;
CC -!- SUBCELLULAR LOCATION: Endosome membrane; Lipid-anchor (By
CC similarity). Cell membrane; Lipid-anchor (By similarity). Early
CC endosome. Cell projection, ruffle. Cytoplasmic vesicle.
CC Cytoplasmic vesicle, phagosome. Cytoplasmic vesicle, phagosome
CC membrane; Lipid-anchor; Cytoplasmic side (By similarity).
CC Note=Recruited to phagosomes containing S.aureus or
CC M.tuberculosis.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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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; CAC15020.1; -; 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 RefSeq; NP_065724.1; NM_020673.2.
DR UniGene; Hs.529044; -.
DR ProteinModelPortal; Q9UL26; -.
DR SMR; Q9UL26; 2-167.
DR IntAct; Q9UL26; 4.
DR MINT; MINT-5003659; -.
DR STRING; 9606.ENSP00000244040; -.
DR PhosphoSite; Q9UL26; -.
DR DMDM; 13633614; -.
DR PaxDb; Q9UL26; -.
DR PRIDE; Q9UL26; -.
DR DNASU; 57403; -.
DR Ensembl; ENST00000244040; ENSP00000244040; ENSG00000124209.
DR GeneID; 57403; -.
DR KEGG; hsa:57403; -.
DR UCSC; uc002xyz.3; human.
DR CTD; 57403; -.
DR GeneCards; GC20P056884; -.
DR HGNC; HGNC:9764; RAB22A.
DR MIM; 612966; gene.
DR neXtProt; NX_Q9UL26; -.
DR PharmGKB; PA34112; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233968; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; Q9UL26; -.
DR KO; K07891; -.
DR OMA; KCDLSDA; -.
DR OrthoDB; EOG77DJ7M; -.
DR PhylomeDB; Q9UL26; -.
DR GeneWiki; RAB22A; -.
DR GenomeRNAi; 57403; -.
DR NextBio; 63508; -.
DR PRO; PR:Q9UL26; -.
DR ArrayExpress; Q9UL26; -.
DR Bgee; Q9UL26; -.
DR CleanEx; HS_RAB22A; -.
DR Genevestigator; Q9UL26; -.
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: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; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; TAS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IDA:UniProtKB.
DR GO; GO:0007032; P:endosome organization; IEP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003579; Small_GTPase_Rab_type.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 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; Complete proteome;
KW Cytoplasmic vesicle; Endosome; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1 194 Ras-related protein Rab-22A.
FT /FTId=PRO_0000121209.
FT NP_BIND 12 20 GTP (By similarity).
FT NP_BIND 60 64 GTP (By similarity).
FT NP_BIND 118 121 GTP (By similarity).
FT NP_BIND 148 150 GTP (By similarity).
FT MOTIF 34 42 Effector region (By similarity).
FT LIPID 193 193 S-geranylgeranyl cysteine (By
FT similarity).
FT LIPID 194 194 S-geranylgeranyl cysteine (By
FT similarity).
FT MUTAGEN 19 19 S->L: Loss of GTPase activity.
FT MUTAGEN 64 64 Q->L: Constitutive GTPase activity.
FT Impairs normal protein trafficking
FT through early endosomes.
FT CONFLICT 184 184 R -> K (in Ref. 3; CAC10538).
FT CONFLICT 192 193 SC -> TA (in Ref. 1; AAL75941).
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
//

MIM 612966
*RECORD*
*FIELD* NO
612966
*FIELD* TI
*612966 RAS-ASSOCIATED PROTEIN RAB22A; RAB22A
*FIELD* TX

DESCRIPTION

Small GTPases of the RAB family, such as RAB22A, are involved in the
read moretransport of macromolecules along endocytic and exocytic pathways
(Magadan et al., 2006).

CLONING

By searching databases for RAS family members, followed by PCR, He et
al. (2002) cloned RAB22A. The deduced 194-amino acid RAB22A protein
contains 4 highly conserved GTPase motifs. Northern blot analysis
detected a major transcript of about 2.4 kb in all tissues examined
except testis. Highest expression was in lung, followed by heart,
pancreas, and spleen.

Using canine Rab22 to probe a Northern blot of mouse tissues, Olkkonen
et al. (1993) detected widespread but variable expression of Rab22, with
highest levels in brain and heart.

GENE FUNCTION

Kauppi et al. (2002) found that overexpression of canine Rab22a in
hamster kidney cells caused formation of abnormally large early
endosomal vacuoles. Expression of a GTPase-deficient Rab22a mutant
caused accumulation of a fluid-phase marker and aspartylglucosaminidase
(AGA; 208400) into abnormal vacuole-like structures that contained both
early and late endosome markers. Overexpression of either wildtype or
mutant Rab22a in HeLa cells caused redistribution of transferrin (TF;
190000)-positive endosomes to the leading edges of the cells,
fragmentation of the Golgi complex, and reduced degradation of EGF
(131530).

Using immunohistochemical analysis, Weigert et al. (2004) showed that
endogenous HeLa cell RAB22A localized on tubular endosomes and vesicles
at the cell periphery, both of which contained major histocompatibility
complex class I (MHCI; see 142800), but not transferrin. Knockdown of
RAB22A in HeLa cells via small interfering RNA inhibited recycling of
MHCI to the plasma membrane, but it only slightly affected recycling of
transferrin. Internalization of MHCI and transferrin was not altered by
knockdown of RAB22A. Weigert et al. (2004) concluded that RAB22A
regulates the recycling of cargo proteins that enter the cell
independently of clathrin (see CLTC; 118955).

Magadan et al. (2006) found that overexpression of human RAB22A, but not
canine Rab22a, in HeLa cells affected the distribution of transferrin
receptor (TFRC; 190010) and altered transferrin recycling. Both wildtype
RAB22A and GTPase-deficient RAB22A mutants affected the morphology of
endosomes, inhibited transferrin recycling, and promoted redistribution
of TFRC to large RAB22A-containing vesicles.

GENE STRUCTURE

He et al. (2002) determined that the RAB22A gene contains 9 exons and
spans over 50.1 kb.

MAPPING

By radiation hybrid analysis, He et al. (2002) mapped the RAB22A gene to
chromosome 20q13.3.

*FIELD* RF
1. He, H.; Dai, F.; Yu, L.; She, X.; Zhao, Y.; Jiang, J.; Chen, X.;
Zhao, S.: Identification and characterization of nine novel human
small GTPases showing variable expressions in liver cancer tissues. Gene
Expr. 10: 231-242, 2002.

2. Kauppi, M.; Simonsen, A.; Bremnes, B.; Vieira, A.; Callaghan, J.;
Stenmark, H.; Olkkonen, V. M.: The small GTPase Rab22 interacts with
EEA1 and controls endosomal membrane trafficking. J. Cell Sci. 115:
899-911, 2002.

3. Magadan, J. G.; Barbieri, M. A.; Mesa, R.; Stahl, P. D.; Mayorga,
L. S.: Rab22a regulates the sorting of transferrin to recycling endosomes. Molec.
Cell. Biol. 26: 2595-2614, 2006.

4. Olkkonen, V. M.; Dupree, P.; Killisch, I.; Lutcke, A.; Zerial,
M.; Simons, K.: Molecular cloning and subcellular localization of
three GTP-binding proteins of the rab subfamily. J. Cell Sci. 106:
1249-1261, 1993.

5. Weigert, R.; Yeung, A. C.; Li, J.; Donaldson, J. G.: Rab22a regulates
the recycling of membrane proteins internalized independently of clathrin. Molec.
Biol. Cell 15: 3758-3770, 2004.

*FIELD* CD
Patricia A. Hartz: 8/18/2009

*FIELD* ED
mgross: 08/18/2009

RBCC Red Blood Cell Collection

Full text data of RAB22A