RBCC

Full text data of RAB21

RAB21 (KIAA0118) [Confidence: high (present in two of the MS resources)]
Ras-related protein Rab-21; Flags: Precursor

hRBCD IPI00007755
IPI00007755 Ras-related protein Rab-21 Ras-related protein Rab-21 membrane n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a 1 n/a n/a n/a n/a 2 n/a n/a cytoplasmic and membrane associated n/a expected molecular weight found in band between 98- 188 kDa

UniProt Q9UL25
ID RAB21_HUMAN Reviewed; 225 AA.
AC Q9UL25; Q14466; Q569H3;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 133.
DE RecName: Full=Ras-related protein Rab-21;
DE Flags: Precursor;
GN Name=RAB21; Synonyms=KIAA0118;
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], SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph, and Placenta;
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 [3]
RP PROTEIN SEQUENCE OF 2-16; 48-59; 91-109 AND 141-157, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-225.
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
RA Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III.
RT The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [5]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-33 AND GLN-78.
RX PubMed=15561770; DOI=10.1242/jcs.01560;
RA Simpson J.C., Griffiths G., Wessling-Resnick M., Fransen J.A.M.,
RA Bennett H., Jones A.T.;
RT "A role for the small GTPase Rab21 in the early endocytic pathway.";
RL J. Cell Sci. 117:6297-6311(2004).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18804435; DOI=10.1016/j.devcel.2008.08.001;
RA Pellinen T., Tuomi S., Arjonen A., Wolf M., Edgren H., Meyer H.,
RA Grosse R., Kitzing T., Rantala J.K., Kallioniemi O., Faessler R.,
RA Kallio M., Ivaska J.;
RT "Integrin trafficking regulated by Rab21 is necessary for
RT cytokinesis.";
RL Dev. Cell 15:371-385(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 16-183 IN COMPLEX WITH GTP
RP ANALOG AND GDP.
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-
RT 5.";
RL Nature 436:415-419(2005).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 16-183 IN COMPLEX WITH
RP RABGEF1.
RX PubMed=17450153; DOI=10.1038/nsmb1232;
RA Delprato A., Lambright D.G.;
RT "Structural basis for Rab GTPase activation by VPS9 domain exchange
RT factors.";
RL Nat. Struct. Mol. Biol. 14:406-412(2007).
CC -!- FUNCTION: Regulates integrin internalization and recycling, but
CC does not influence the traffic of endosomally translocated
CC receptors in general. As a result, may regulate cell adhesion and
CC migration (By similarity). During the mitosis of adherent cells,
CC controls the endosomal trafficking of integrins which is required
CC for the successful completion of cytokinesis.
CC -!- SUBUNIT: Interacts with the cytoplasmic tail of integrins ITGA1,
CC ITGA2, ITGA5, ITGA6, ITGA11 and ITGB1 (By similarity). Interacts
CC with RABGEF1 (via VPS9 domain).
CC -!- INTERACTION:
CC Q9UKG1:APPL1; NbExp=10; IntAct=EBI-1056039, EBI-741243;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Lipid-anchor
CC (By similarity). Golgi apparatus membrane. Early endosome
CC membrane. Cytoplasmic vesicle membrane. Cleavage furrow. Note=In
CC nonpolarized epithelial Caco-2 cells, found in the endoplasmic
CC reticulum; in polarized cells, observed in vesicles in the apical
CC cytoplasm. During mitosis, in mid-telophase, localized in the
CC ingressing cleavage furrow. In late telophase, detected at the
CC opposite poles of the daughter cells, in vesicles at the base of
CC lamellipodia formed by the separating daughter cells.
CC -!- TISSUE SPECIFICITY: Widely expressed. In jejunal tissue,
CC predominantly expressed in the apical region of the epithelial
CC cell layer of the villi, weak expression, if any, in the crypt
CC epithelium. Capillary endothelium and some cell types in the
CC lamina propria also show expression.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR EMBL; AF091035; AAF00048.1; -; mRNA.
DR EMBL; BC021901; AAH21901.1; -; mRNA.
DR EMBL; BC092475; AAH92475.1; -; mRNA.
DR EMBL; D42087; BAA07682.1; -; mRNA.
DR RefSeq; NP_055814.1; NM_014999.2.
DR UniGene; Hs.524590; -.
DR PDB; 1YZT; X-ray; 2.05 A; A/B=16-183.
DR PDB; 1YZU; X-ray; 2.50 A; A/B=16-183.
DR PDB; 1Z08; X-ray; 1.80 A; A/B/C/D=16-183.
DR PDB; 1Z0I; X-ray; 2.33 A; A=16-183.
DR PDB; 2OT3; X-ray; 2.10 A; B=16-183.
DR PDBsum; 1YZT; -.
DR PDBsum; 1YZU; -.
DR PDBsum; 1Z08; -.
DR PDBsum; 1Z0I; -.
DR PDBsum; 2OT3; -.
DR ProteinModelPortal; Q9UL25; -.
DR SMR; Q9UL25; 17-181.
DR DIP; DIP-29349N; -.
DR IntAct; Q9UL25; 5.
DR MINT; MINT-3081967; -.
DR STRING; 9606.ENSP00000261263; -.
DR PhosphoSite; Q9UL25; -.
DR DMDM; 13633613; -.
DR PaxDb; Q9UL25; -.
DR PeptideAtlas; Q9UL25; -.
DR PRIDE; Q9UL25; -.
DR DNASU; 23011; -.
DR Ensembl; ENST00000261263; ENSP00000261263; ENSG00000080371.
DR GeneID; 23011; -.
DR KEGG; hsa:23011; -.
DR UCSC; uc001swt.3; human.
DR CTD; 23011; -.
DR GeneCards; GC12P072100; -.
DR HGNC; HGNC:18263; RAB21.
DR HPA; HPA016988; -.
DR MIM; 612398; gene.
DR neXtProt; NX_Q9UL25; -.
DR PharmGKB; PA34111; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233968; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; Q9UL25; -.
DR KO; K07890; -.
DR OMA; SHFFASA; -.
DR OrthoDB; EOG7RZ5QX; -.
DR PhylomeDB; Q9UL25; -.
DR BRENDA; 3.6.5.2; 2681.
DR ChiTaRS; RAB21; human.
DR EvolutionaryTrace; Q9UL25; -.
DR GeneWiki; RAB21; -.
DR GenomeRNAi; 23011; -.
DR NextBio; 43928; -.
DR PRO; PR:Q9UL25; -.
DR ArrayExpress; Q9UL25; -.
DR Bgee; Q9UL25; -.
DR CleanEx; HS_RAB21; -.
DR Genevestigator; Q9UL25; -.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; 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:0005768; C:endosome; IDA:LIFEdb.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA: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 3D-structure; Acetylation; Complete proteome; Cytoplasmic vesicle;
KW Direct protein sequencing; Endoplasmic reticulum; Endosome;
KW Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 222 Ras-related protein Rab-21.
FT /FTId=PRO_0000121205.
FT PROPEP 223 225 Removed in mature form (Potential).
FT /FTId=PRO_0000370768.
FT NP_BIND 26 34 GTP.
FT NP_BIND 74 78 GTP (By similarity).
FT NP_BIND 132 135 GTP.
FT NP_BIND 162 164 GTP.
FT MOTIF 48 56 Effector region (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 222 222 Cysteine methyl ester (Potential).
FT LIPID 221 221 S-geranylgeranyl cysteine (By
FT similarity).
FT LIPID 222 222 S-geranylgeranyl cysteine (By
FT similarity).
FT MUTAGEN 33 33 T->N: Defects in GTP-binding.
FT MUTAGEN 78 78 Q->L: Defects in GTP hydrolysis.
FT STRAND 18 25
FT HELIX 28 30
FT HELIX 32 41
FT STRAND 46 48
FT STRAND 55 65
FT STRAND 67 74
FT HELIX 79 84
FT HELIX 85 89
FT STRAND 93 100
FT HELIX 104 121
FT HELIX 122 124
FT STRAND 125 132
FT HELIX 134 139
FT HELIX 144 153
FT STRAND 157 162
FT TURN 163 166
FT HELIX 169 181
SQ SEQUENCE 225 AA; 24348 MW; 73CA2C127F0CBFD6 CRC64;
MAAAGGGGGG AAAAGRAYSF KVVLLGEGCV GKTSLVLRYC ENKFNDKHIT TLQASFLTKK
LNIGGKRVNL AIWDTAGQER FHALGPIYYR DSNGAILVYD ITDEDSFQKV KNWVKELRKM
LGNEICLCIV GNKIDLEKER HVSIQEAESY AESVGAKHYH TSAKQNKGIE ELFLDLCKRM
IETAQVDERA KGNGSSQPGT ARRGVQIIDD EPQAQTSGGG CCSSG
//

MIM 612398
*RECORD*
*FIELD* NO
612398
*FIELD* TI
*612398 RAB-ASSOCIATED PROTEIN RAB21; RAB21
;;KIAA0118
*FIELD* TX

DESCRIPTION

RAB21 belongs to the RAB family of small GTP-binding proteins that
read moreregulate intracellular vesicle targeting (Opdam et al., 2000).

CLONING

By sequencing clones obtained from a human immature myeloid cell line
cDNA library, Nagase et al. (1995) cloned RAB21, which they designated
KIAA0118. The transcript contains a repetitive element in its 3-prime
end, and the deduced protein shares significant similarity with slime
mold Rab-B. Northern blot analysis detected expression of RAB21 in all
human tissues and cell lines examined, with highest expression in heart
and skeletal muscle.

By RT-PCR of Caco2 human colon cancer cell RNA using degenerate primers
based on conserved regions of RAB family members, followed by screening
a Caco2 cDNA library, Opdam et al. (2000) obtained 2 RAB21 clones that
appeared to differ in their polyadenylation sites. The deduced 225-amino
acid RAB21 protein has a calculated molecular mass of 24.5 kD. Like
other RAB proteins, RAB21 contains 6 GTP-binding domains and C-terminal
cysteines required for prenylation. Northern blot analysis detected
transcripts of 1.8, 2.5, and 4.0 kb in lung, kidney, liver, esophagus,
stomach, jejunum, rectum, and all human cell lines examined.
Immunofluorescence analysis showed RAB21 associated with the endoplasmic
reticulum in nonpolarized Caco2 cells and with apical membranes and late
endosomes or lysosomes in differentiated, polarized Caco2 cells.
Immunohistochemical analysis of human jejunum revealed strongest RAB21
staining in the apical cytoplasmic region of epithelial cells. RAB21 was
also detected in capillary endothelial cells and in some cells of the
lamina propria.

GENE FUNCTION

Opdam et al. (2000) showed that recombinant human RAB21 bound
radiolabeled GTP.

Using human and rodent cell lines, Pellinen et al. (2008) showed that
integrins (see ITGB1; 135630) anchored the cleavage furrow to the matrix
during cytokinesis and that targeting of integrins to and from the
cleavage furrow was regulated by RAB21. RAB21 activity, integrin-RAB21
association, and integrin endocytosis were all necessary for normal
cytokinesis. Pellinen et al. (2008) found a deletion of the RAB21 gene
in 2 ovarian cancer cell lines and a prostate cancer tumor sample. Cells
harboring this deletion were multinucleated, and reintroduction of RAB21
into the ovarian cancer cell lines rescued the phenotype. Pellinen et
al. (2008) concluded that RAB21-regulated integrin trafficking is
essential for normal cell division and that defects in this trafficking
may contribute to multinucleation and genomic instability.

MAPPING

By radiation hybrid analysis, Nagase et al. (1995) mapped the RAB21 gene
to chromosome 12.

*FIELD* RF
1. Nagase, T; Miyajima, N; Tanaka, A.; Sazuka, T.; Seki, N.; Sato,
S.; Tabata, S.; Ishikawa, K.; Kawarabayashi, Y.; Kotani, H.; Nomura,
N.: Prediction of the coding sequences of unidentified human genes.
III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced
by analysis of cDNA clones from human cell line KG-1. DNA Res. 2:
37-43, 1995.

2. Opdam, F. J. M.; Kamps, G.; Croes, H.; van Bokhoven, H.; Ginsel,
L. A.; Fransen, J. A. M.: Expression of Rab small GTPases in epithelial
Caco-2 cells: Rab21 is an apically located GTP-binding protein in
polarised intestinal epithelial cells. Europ. J. Cell Biol. 79:
308-316, 2000.

3. Pellinen, T.; Tuomi, S.; Arjonen, A.; Wolf, M.; Edgren, H.; Meyer,
H.; Grosse, R.; Kitzing, T.; Rantala, J. K.; Kallioniemi O.; Fassler,
R.; Kallio, M.; Ivaska, J.: Integrin trafficking regulated by Rab21
is necessary for cytokinesis. Dev. Cell 15: 371-385, 2008.

*FIELD* CD
Patricia A. Hartz: 11/11/2008

*FIELD* ED
mgross: 11/11/2008

RBCC Red Blood Cell Collection

Full text data of RAB21