RAB23_MOUSE
ID RAB23_MOUSE Reviewed; 237 AA.
AC P35288;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Ras-related protein Rab-23;
DE AltName: Full=Protein open brain;
DE AltName: Full=Rab-15;
DE Flags: Precursor;
GN Name=Rab23; Synonyms=Opb;
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].
RC TISSUE=Kidney;
RX PubMed=8125302; DOI=10.1016/0378-1119(94)90809-5;
RA Olkkonen V.M., Peterson J.R., Dupree P., Lutcke A., Zerial M., Simons K.;
RT "Isolation of a mouse cDNA encoding Rab23, a small novel GTPase expressed
RT predominantly in the brain.";
RL Gene 138:207-211(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-69.
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 [4]
RP ROLE IN DISEASE.
RX PubMed=7720556; DOI=10.1242/dev.120.11.3119;
RA Gunther T., Struwe M., Aguzzi A., Schughart K.;
RT "Open brain, a new mouse mutant with severe neural tube defects, shows
RT altered gene expression patterns in the developing spinal cord.";
RL Development 120:3119-3130(1994).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=11071781; DOI=10.1006/dbio.2000.9918;
RA Eggenschwiler J.T., Anderson K.V.;
RT "Dorsal and lateral fates in the mouse neural tube require the cell-
RT autonomous activity of the open brain gene.";
RL Dev. Biol. 227:648-660(2000).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=11449277; DOI=10.1038/35084089;
RA Eggenschwiler J.T., Espinoza E., Anderson K.V.;
RT "Rab23 is an essential negative regulator of the mouse Sonic hedgehog
RT signalling pathway.";
RL Nature 412:194-198(2001).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14617350; DOI=10.1046/j.1600-0854.2003.00141.x;
RA Evans T.M., Ferguson C., Wainwright B.J., Parton R.G., Wicking C.;
RT "Rab23, a negative regulator of hedgehog signaling, localizes to the plasma
RT membrane and the endocytic pathway.";
RL Traffic 4:869-884(2003).
RN [8]
RP FUNCTION.
RX PubMed=16364285; DOI=10.1016/j.ydbio.2005.09.022;
RA Eggenschwiler J.T., Bulgakov O.V., Qin J., Li T., Anderson K.V.;
RT "Mouse Rab23 regulates hedgehog signaling from smoothened to Gli
RT proteins.";
RL Dev. Biol. 290:1-12(2006).
RN [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16463280; DOI=10.1002/jnr.20788;
RA Guo A., Wang T., Ng E.L., Aulia S., Chong K.H., Teng F.Y., Wang Y.,
RA Tang B.L.;
RT "Open brain gene product Rab23: expression pattern in the adult mouse brain
RT and functional characterization.";
RL J. Neurosci. Res. 83:1118-1127(2006).
RN [10]
RP FUNCTION.
RX PubMed=18218620; DOI=10.1074/jbc.m706795200;
RA Yang L., Clinton J.M., Blackburn M.L., Zhang Q., Zou J.,
RA Zielinska-Kwiatkowska A., Tang B.L., Chansky H.A.;
RT "Rab23 regulates differentiation of ATDC5 chondroprogenitor cells.";
RL J. Biol. Chem. 283:10649-10657(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, 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 [12]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 7-172.
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: The small GTPases Rab are key regulators of intracellular
CC membrane trafficking, from the formation of transport vesicles to their
CC fusion with membranes. Rabs cycle between an inactive GDP-bound form
CC and an active GTP-bound form that is able to recruit to membranes
CC different set of downstream effectors directly responsible for vesicle
CC formation, movement, tethering and fusion (By similarity). Plays a role
CC in autophagic vacuole assembly, and mediates defense against pathogens,
CC such as S.aureus, by promoting their capture by autophagosomes that
CC then merge with lysosomes (By similarity). Together with SUFU, prevents
CC nuclear import of GLI1, and thereby inhibits GLI1 transcription factor
CC activity. Regulates GLI1 in differentiating chondrocytes. Likewise,
CC regulates GLI3 proteolytic processing and modulates GLI2 and GLI3
CC transcription factor activity. {ECO:0000250,
CC ECO:0000269|PubMed:11071781, ECO:0000269|PubMed:11449277,
CC ECO:0000269|PubMed:16364285, ECO:0000269|PubMed:18218620,
CC ECO:0000269|PubMed:7720556}.
CC -!- SUBUNIT: Interacts with SUFU. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14617350};
CC Lipid-anchor {ECO:0000305}; Cytoplasmic side
CC {ECO:0000269|PubMed:14617350}. Cytoplasm {ECO:0000269|PubMed:14617350}.
CC Endosome membrane {ECO:0000269|PubMed:14617350}. Cytoplasmic vesicle,
CC autophagosome {ECO:0000250|UniProtKB:Q9ULC3}. Cytoplasmic vesicle,
CC phagosome {ECO:0000305}. 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:Q9ULC3}.
CC -!- TISSUE SPECIFICITY: Detected in brain neurons (at protein level).
CC Forebrain and midbrain. {ECO:0000269|PubMed:14617350,
CC ECO:0000269|PubMed:16463280}.
CC -!- DISEASE: Note=Defects in Rab23 are the cause of the open brain
CC phenotype. Mice suffer from exencephaly and severe malformations of the
CC spinal cord and the dorsal root ganglia, leading to complete embryonic
CC lethality. In addition, mice display poorly developed eyes and
CC polydactyly.
CC -!- DISRUPTION PHENOTYPE: Complete embryonic lethality, due to defects in
CC neural tube closure. Mice suffer from exencephaly and severe
CC malformations of the spinal cord and the dorsal root ganglia. In
CC addition, mice display poorly developed eyes and polydactyly.
CC {ECO:0000269|PubMed:11071781, ECO:0000269|PubMed:11449277}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; Z22821; CAA80474.1; -; mRNA.
DR EMBL; BC025578; AAH25578.1; -; mRNA.
DR EMBL; M79305; AAK14829.1; -; mRNA.
DR CCDS; CCDS35532.1; -.
DR PIR; I48729; S40244.
DR PIR; JH0645; JH0645.
DR PDB; 1Z22; X-ray; 2.06 A; A=7-172.
DR PDB; 1Z2A; X-ray; 1.90 A; A=7-172.
DR PDBsum; 1Z22; -.
DR PDBsum; 1Z2A; -.
DR AlphaFoldDB; P35288; -.
DR SMR; P35288; -.
DR DIP; DIP-60517N; -.
DR IntAct; P35288; 1.
DR STRING; 10090.ENSMUSP00000085625; -.
DR iPTMnet; P35288; -.
DR PhosphoSitePlus; P35288; -.
DR EPD; P35288; -.
DR jPOST; P35288; -.
DR MaxQB; P35288; -.
DR PaxDb; P35288; -.
DR PeptideAtlas; P35288; -.
DR PRIDE; P35288; -.
DR ProteomicsDB; 253143; -.
DR UCSC; uc007anv.1; mouse.
DR MGI; MGI:99833; Rab23.
DR eggNOG; KOG4252; Eukaryota.
DR InParanoid; P35288; -.
DR PhylomeDB; P35288; -.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR ChiTaRS; Rab23; mouse.
DR EvolutionaryTrace; P35288; -.
DR PRO; PR:P35288; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P35288; protein.
DR GO; GO:0005776; C:autophagosome; ISS:UniProtKB.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0006968; P:cellular defense response; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISO:MGI.
DR GO; GO:0097094; P:craniofacial suture morphogenesis; ISS:UniProtKB.
DR GO; GO:0021904; P:dorsal/ventral neural tube patterning; IMP:UniProtKB.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR GO; GO:0046039; P:GTP metabolic process; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0045861; P:negative regulation of proteolysis; IMP:MGI.
DR GO; GO:0007399; P:nervous system development; IMP:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IMP:MGI.
DR GO; GO:0008589; P:regulation of smoothened signaling pathway; IGI:MGI.
DR GO; GO:0007165; P:signal transduction; IMP:MGI.
DR GO; GO:0021513; P:spinal cord dorsal/ventral patterning; IMP:MGI.
DR CDD; cd04106; Rab23_like; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR034114; Rab23.
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 3D-structure; Cell membrane; Cytoplasm; Cytoplasmic vesicle;
KW Developmental protein; Endosome; GTP-binding; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..234
FT /note="Ras-related protein Rab-23"
FT /id="PRO_0000121212"
FT PROPEP 235..237
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370772"
FT REGION 204..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 38..46
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 16..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 64..68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULC3"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULC3"
FT MOD_RES 234
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 234
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:1Z2A"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:1Z2A"
FT STRAND 43..53
FT /evidence="ECO:0007829|PDB:1Z2A"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:1Z2A"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1Z2A"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:1Z2A"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:1Z2A"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:1Z2A"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:1Z2A"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:1Z2A"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:1Z2A"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:1Z2A"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:1Z2A"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:1Z2A"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:1Z2A"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:1Z2A"
SQ SEQUENCE 237 AA; 26678 MW; AA1F2B25BAECD3E6 CRC64;
MLEEDMEVAI KMVVVGNGAV GKSSMIQRYC KGIFTKDYKK TIGVDFLERQ IQVNDEDVRL
MLWDTAGQEE FDAITKAYYR GAQACVLVFS TTDRESFEAI SSWREKVVAE VGDIPTALVQ
NKIDLLDDSC IKNEEAEGLA KRLKLRFYRT SVKEDLNVSE VFKYLAEKHL QKLKQQITED
PEQTHSSSNK IGVFNASVGS HLGQNSSSLN GGDVINLRPN KQRTKRTRNP FSSCSVP
