RAB10_CAEEL
ID RAB10_CAEEL Reviewed; 201 AA.
AC Q94148; I7FXD6;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Ras-related protein Rab-10 {ECO:0000305};
DE Short=Rab-10 {ECO:0000303|PubMed:16394106};
DE EC=3.6.5.2 {ECO:0000269|PubMed:26633194};
GN Name=rab-10 {ECO:0000303|PubMed:16394106, ECO:0000312|EMBL:CCD70773.1,
GN ECO:0000312|WormBase:T23H2.5};
GN ORFNames=T23H2.5 {ECO:0000312|WormBase:T23H2.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:CCD70773.1};
RN [1] {ECO:0000312|EMBL:CCD70773.1, ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD70773.1,
RC ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000312|EMBL:AFP33152.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-201, MUTAGENESIS OF THR-23 AND GLN-68, AND
RP PHYLOGENETIC ANALYSIS.
RX PubMed=23185324; DOI=10.1371/journal.pone.0049387;
RA Gallegos M.E., Balakrishnan S., Chandramouli P., Arora S., Azameera A.,
RA Babushekar A., Bargoma E., Bokhari A., Chava S.K., Das P., Desai M.,
RA Decena D., Saramma S.D., Dey B., Doss A.L., Gor N., Gudiputi L., Guo C.,
RA Hande S., Jensen M., Jones S., Jones N., Jorgens D., Karamchedu P.,
RA Kamrani K., Kolora L.D., Kristensen L., Kwan K., Lau H., Maharaj P.,
RA Mander N., Mangipudi K., Menakuru H., Mody V., Mohanty S., Mukkamala S.,
RA Mundra S.A., Nagaraju S., Narayanaswamy R., Ndungu-Case C., Noorbakhsh M.,
RA Patel J., Patel P., Pendem S.V., Ponakala A., Rath M., Robles M.C.,
RA Rokkam D., Roth C., Sasidharan P., Shah S., Tandon S., Suprai J.,
RA Truong T.Q., Uthayaruban R., Varma A., Ved U., Wang Z., Yu Z.;
RT "The C. elegans Rab family: Identification, classification and toolkit
RT construction.";
RL PLoS ONE 7:E49387-E49387(2012).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF THR-23 AND GLN-68.
RX PubMed=16394106; DOI=10.1091/mbc.e05-08-0787;
RA Chen C.C., Schweinsberg P.J., Vashist S., Mareiniss D.P., Lambie E.J.,
RA Grant B.D.;
RT "RAB-10 is required for endocytic recycling in the Caenorhabditis elegans
RT intestine.";
RL Mol. Biol. Cell 17:1286-1297(2006).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17761527; DOI=10.1091/mbc.e07-05-0486;
RA Glodowski D.R., Chen C.C., Schaefer H., Grant B.D., Rongo C.;
RT "RAB-10 regulates glutamate receptor recycling in a cholesterol-dependent
RT endocytosis pathway.";
RL Mol. Biol. Cell 18:4387-4396(2007).
RN [5]
RP INTERACTION WITH EHBP-1, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF THR-23 AND GLN-68.
RX PubMed=20573983; DOI=10.1091/mbc.e10-02-0149;
RA Shi A., Chen C.C., Banerjee R., Glodowski D., Audhya A., Rongo C.,
RA Grant B.D.;
RT "EHBP-1 functions with RAB-10 during endocytic recycling in Caenorhabditis
RT elegans.";
RL Mol. Biol. Cell 21:2930-2943(2010).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH TBC-2, SUBCELLULAR
RP LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF THR-23 AND GLN-68.
RX PubMed=23100538; DOI=10.1073/pnas.1203306109;
RA Sasidharan N., Sumakovic M., Hannemann M., Hegermann J., Liewald J.F.,
RA Olendrowitz C., Koenig S., Grant B.D., Rizzoli S.O., Gottschalk A.,
RA Eimer S.;
RT "RAB-5 and RAB-10 cooperate to regulate neuropeptide release in
RT Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:18944-18949(2012).
RN [7]
RP FUNCTION, INTERACTION WITH CNT-1 AND EHBP-1, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=22869721; DOI=10.1073/pnas.1205278109;
RA Shi A., Liu O., Koenig S., Banerjee R., Chen C.C., Eimer S., Grant B.D.;
RT "RAB-10-GTPase-mediated regulation of endosomal phosphatidylinositol-4,5-
RT bisphosphate.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E2306-E2315(2012).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP THR-23 AND GLN-68.
RX PubMed=25301900; DOI=10.1073/pnas.1408327111;
RA Chen S., Li L., Li J., Liu B., Zhu X., Zheng L., Zhang R., Xu T.;
RT "SEC-10 and RAB-10 coordinate basolateral recycling of clathrin-independent
RT cargo through endosomal tubules in Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:15432-15437(2014).
RN [9]
RP FUNCTION, INTERACTION WITH AMPH-1 AND TBC-2, SUBCELLULAR LOCATION,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLN-68.
RX PubMed=26393361; DOI=10.1371/journal.pgen.1005514;
RA Liu O., Grant B.D.;
RT "Basolateral endocytic recycling requires RAB-10 and AMPH-1 mediated
RT recruitment of RAB-5 GAP TBC-2 to endosomes.";
RL PLoS Genet. 11:E1005514-E1005514(2015).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP THR-23 AND GLN-68.
RX PubMed=26394140; DOI=10.1371/journal.pgen.1005484;
RA Zou W., Yadav S., DeVault L., Nung Jan Y., Sherwood D.R.;
RT "RAB-10-dependent membrane transport is required for dendrite
RT arborization.";
RL PLoS Genet. 11:E1005484-E1005484(2015).
RN [11]
RP FUNCTION, ACTIVITY REGULATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP THR-23 AND GLN-68.
RX PubMed=26633194; DOI=10.1371/journal.pgen.1005695;
RA Taylor C.A., Yan J., Howell A.S., Dong X., Shen K.;
RT "RAB-10 regulates dendritic branching by balancing dendritic transport.";
RL PLoS Genet. 11:E1005695-E1005695(2015).
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 (PubMed:23100538,
CC PubMed:26394140, PubMed:26633194). Required for basolateral endocytic
CC recycling, the return of macromolecules and fluid from endosomes to the
CC plasma membrane, in polarized epithelial cells of the intestine
CC upstream of rme-1 (PubMed:16394106). Involved in the formation of the
CC endosomal tubular network that is required for basolateral recycling of
CC clathrin-independent endocytic cargo such as daf-4 in the intestine
CC (PubMed:25301900). Required for the recruitment of cnt-1 effector to
CC endosomal membranes in the intestinal epithelium, which is important
CC for the regulation of levels of endosomal phosphatidylinositol-4,5-
CC bisphosphate, a key phosphoinositide in membrane traffic, and for the
CC recruitment of endosomal membrane-bending proteins, rme-1 and sdpn-1
CC (PubMed:22869721). Recruits the rab-5 GTPase-activating protein tbc-2
CC to endosomes where it then inactivates rab-5 resulting in removal of
CC rab-5 from membranes, which is necessary for cargo transport from early
CC endosomes to recycling endosomes in the basolateral intestine
CC (PubMed:26393361). Regulates recycling of synaptic membrane AMPA
CC glutamate receptor, glr-1, from intracellular endosomal compartments
CC back to synapses in a cholesterol-dependent endocytosis pathway
CC functioning after clathrin-independent endocytosis in command
CC interneurons (PubMed:17761527). Regulates neuropeptide release from
CC dense core vesicles (DCVs) of cholinergic motoneurons in cooperation
CC with rab-5. They reciprocally recruit each other's inactivating GAP
CC molecule leading to local exclusion of one or the other rab protein at
CC the Golgi-endosomal interphase at an essential stage during DCV sorting
CC (PubMed:23100538). Regulates membrane trafficking of membranes and
CC dendrite proteins from the Golgi and/or endosomal compartments to
CC plasma membrane during dendrite morphogenesis together with the exocyst
CC complex in the multi-dendritic PVD sensory neurons acting in a cell-
CC autonomous manner and requiring its GTPase activity (PubMed:26394140).
CC Functions cell-autonomously together with the exocyst complex to
CC regulate dendrite morphogenesis and anterior-posterior patterning of
CC the PVD neurons dendritic arbor by balancing the anterograde and
CC retrograde transport via molecular motors unc-116 (kinesin heavy chain)
CC and dhc-1 (dynein heavy chain) to appropriately transport branching
CC factors, such as dma-1, to the specific subcellular regions of the
CC developing dendrite in its GTPase activity-dependent manner
CC (PubMed:26633194). {ECO:0000269|PubMed:16394106,
CC ECO:0000269|PubMed:17761527, ECO:0000269|PubMed:22869721,
CC ECO:0000269|PubMed:23100538, ECO:0000269|PubMed:25301900,
CC ECO:0000269|PubMed:26393361, ECO:0000269|PubMed:26394140,
CC ECO:0000269|PubMed:26633194}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000269|PubMed:26633194};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000305|PubMed:26633194};
CC -!- ACTIVITY REGULATION: Rab activation is generally mediated by a guanine
CC exchange factor (GEF), while inactivation through hydrolysis of bound
CC GTP is catalyzed by a GTPase activating protein (GAP) (By similarity).
CC Tbc-4 is a likely GAP of this rab (PubMed:23100538). Denn-4 is a
CC putative GEF of this rab (PubMed:26633194).
CC {ECO:0000250|UniProtKB:Q15286, ECO:0000269|PubMed:23100538,
CC ECO:0000269|PubMed:26633194}.
CC -!- SUBUNIT: Interacts (GTP-bound form) with ehbp-1 (via C-terminal coiled
CC coil) (PubMed:20573983, PubMed:22869721). Interacts (GTP-bound form)
CC with cnt-1 (via C-terminal ankyrin repeat) (PubMed:22869721). Interacts
CC (GTP-bound form) with rab-5 GAP, tbc-2 (via putative coiled coil
CC domain) (PubMed:23100538, PubMed:26393361). Interacts (GTP-bound form)
CC with amph-1 (PubMed:26393361). {ECO:0000269|PubMed:20573983,
CC ECO:0000269|PubMed:22869721, ECO:0000269|PubMed:23100538,
CC ECO:0000269|PubMed:26393361}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000269|PubMed:16394106, ECO:0000269|PubMed:26394140}; Lipid-
CC anchor {ECO:0000250|UniProtKB:P62491}. Late endosome membrane
CC {ECO:0000269|PubMed:16394106}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P62491}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:16394106, ECO:0000269|PubMed:26394140}; Lipid-
CC anchor {ECO:0000250|UniProtKB:P62491}. Endosome membrane
CC {ECO:0000269|PubMed:20573983, ECO:0000269|PubMed:26393361}; Lipid-
CC anchor {ECO:0000250|UniProtKB:P62491}. Note=Colocalizes with cnt-1 on
CC recycling endosomes in the intestinal epithelium in vivo
CC (PubMed:22869721). Colocalizes with cnt-1, tbc-2 and amph-1 on
CC endosomes in the intestinal epithelium (PubMed:26393361). Localizes at
CC tips of the growing basolateral endosomal tubules of the intestine
CC (PubMed:25301900). Present in cell bodies as well as throughout the
CC ventral nerve cord of sensory interneurons (PubMed:17761527). The
CC localization on endosomal structures of the intestine and interneurons
CC is regulated by ehbp-1 (PubMed:20573983). Localizes to the medial
CC Golgi, endosomes and immature dense core vesicles (DCVs) in ventral
CC nerve cord (VNC) neurons. Also enriched in axons at dorsal nerve cord
CC (DNC) synapses and localizes with synaptic vesicles and DCVs. Some
CC localize with DCV in neuronal cell bodies. Colocalizes with tbc-4 in
CC the cell body near the Golgi in VNC neurons (PubMed:23100538).
CC Localizes to the Golgi and the early endosomes in the PVD sensory
CC neurons. Localizes to the transport vesicles moving bi-directionally
CC along PVD dendrites. Colocalizes with exoc-8 on intracellular vesicles
CC in the PVD dendrites (PubMed:26394140). {ECO:0000269|PubMed:16394106,
CC ECO:0000269|PubMed:17761527, ECO:0000269|PubMed:20573983,
CC ECO:0000269|PubMed:22869721, ECO:0000269|PubMed:23100538,
CC ECO:0000269|PubMed:25301900, ECO:0000269|PubMed:26393361,
CC ECO:0000269|PubMed:26394140}.
CC -!- TISSUE SPECIFICITY: Almost ubiquitously expressed. Expressed in
CC intestine, hypodermis, seam cells, body-wall muscles, many neurons,
CC oviduct sheath cell, spermatheca, coelomocytes and pharyngeal and nerve
CC ring. {ECO:0000269|PubMed:16394106}.
CC -!- DISRUPTION PHENOTYPE: Intestinal cells exhibit abnormally abundant rab-
CC 5 and rab-7 positive enlarged early endosomes, which accumulate
CC basolaterally recycling transmembrane cargo molecules and fluid
CC indicating a block in basolateral transport (PubMed:16394106,
CC PubMed:20573983). On the other hand, rme-1 positive recycling endosomes
CC are missing. No endocytic trafficking defects in oocytes or
CC coelomocytes (PubMed:16394106). Almost complete loss of cnt-1 endosomal
CC localization in the intestinal epithelium. Overaccumulation of
CC endosomal phosphatidylinositol-4,5-bisphosphate (PubMed:22869721).
CC Nearly complete loss of basolateral endosomal tubule extensions of the
CC intestine (PubMed:25301900). The endosomal localization of tbc-2 is
CC strongly reduced leading to increased rab-5 association with membranes
CC in the intestinal epithelia (PubMed:26393361). Cholesterol-dependent
CC accumulation of glr-1 in large accretions running along the length of
CC the ventral cord neurite bundle while synapses don't have general
CC formation defects. Animals display a decreased frequency of
CC locomotional reversals and significantly reduced response to nose-touch
CC suggesting reduced glr-1 signaling (PubMed:17761527, PubMed:20573983).
CC Rab-10 lin-10 double mutant displays additive glr-1 trafficking defects
CC indicating that they both regulate endocytic recycling of AMPA
CC receptors to synapses, but most probably along distinct regulatory
CC pathways (PubMed:17761527). Complete loss of dense core vesicles (DCVs)
CC secretion of neuropeptides from DA/DB motoneurons, while synaptic
CC ultrastructure and synaptic vesicles (SV) exocytosis as well as
CC coelomocyte function are unaffected (PubMed:23100538). Severely reduced
CC proximal dendritic arborization in multi-dendritic PVD sensory neurons,
CC but minimal effect on dendritic branching and growth on the distal area
CC of the PVD. The growth of PVD axon is normal. Reduced dendritic growth
CC of the multi-dendritic FLP neurons, but no effect on the dendritic
CC growth of unbranched dendrites of the OLL, AWB and AWC neurons.
CC Accumulates dendritic membrane proteins dma-1 and hpo-30 within
CC intracellular vesicles within the growing PVD dendrites and have
CC decreased dendrite membrane localization of these proteins. Rab-10 rab-
CC 8 double deletion mutant has enhanced dendritic arborization defects
CC than rab-10 deletion alone in PVD neurons (PubMed:26394140). PVD
CC dendritic branches are reduced in the posterior region of the cell, but
CC are excessive in the distal anterior region of the cell. Dma-1 fails to
CC localize to the plasma membrane in the posterior dendrite
CC (PubMed:26633194). Rab-10 rab-8 double deletion mutant has disrupted
CC transport of membrane proteins to the plasma membrane of the
CC nonpolarized germline cells (PubMed:20573983).
CC {ECO:0000269|PubMed:16394106, ECO:0000269|PubMed:17761527,
CC ECO:0000269|PubMed:20573983, ECO:0000269|PubMed:22869721,
CC ECO:0000269|PubMed:23100538, ECO:0000269|PubMed:25301900,
CC ECO:0000269|PubMed:26393361, ECO:0000269|PubMed:26394140,
CC ECO:0000269|PubMed:26633194}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; BX284601; CCD70773.1; -; Genomic_DNA.
DR EMBL; JQ235188; AFP33152.1; -; mRNA.
DR PIR; T28971; T28971.
DR RefSeq; NP_491857.1; NM_059456.4.
DR AlphaFoldDB; Q94148; -.
DR SMR; Q94148; -.
DR IntAct; Q94148; 1.
DR STRING; 6239.T23H2.5.2; -.
DR EPD; Q94148; -.
DR PaxDb; Q94148; -.
DR EnsemblMetazoa; T23H2.5.1; T23H2.5.1; WBGene00004273.
DR GeneID; 266836; -.
DR KEGG; cel:CELE_T23H2.5; -.
DR UCSC; T23H2.5.1; c. elegans.
DR CTD; 266836; -.
DR WormBase; T23H2.5; CE14114; WBGene00004273; rab-10.
DR eggNOG; KOG0078; Eukaryota.
DR GeneTree; ENSGT00940000165742; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; Q94148; -.
DR OMA; HKMLIGN; -.
DR OrthoDB; 1426655at2759; -.
DR PhylomeDB; Q94148; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-8873719; RAB geranylgeranylation.
DR Reactome; R-CEL-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:Q94148; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004273; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0031045; C:dense core granule; IDA:WormBase.
DR GO; GO:0005769; C:early endosome; IDA:WormBase.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:WormBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:WormBase.
DR GO; GO:0005797; C:Golgi medial cisterna; IDA:WormBase.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032593; C:insulin-responsive compartment; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IDA:WormBase.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0071532; F:ankyrin repeat binding; IMP:UniProtKB.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0032794; F:GTPase activating protein binding; IPI:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IBA:GO_Central.
DR GO; GO:0032456; P:endocytic recycling; IMP:WormBase.
DR GO; GO:1902647; P:negative regulation of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate biosynthetic process; IMP:UniProtKB.
DR GO; GO:1904951; P:positive regulation of establishment of protein localization; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0001881; P:receptor recycling; IMP:WormBase.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
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.
PE 1: Evidence at protein level;
KW Endosome; Golgi apparatus; GTP-binding; Hydrolase; Lipoprotein; Membrane;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..201
FT /note="Ras-related protein Rab-10"
FT /id="PRO_0000438074"
FT REGION 175..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 38..46
FT /note="Effector region"
FT /evidence="ECO:0000305"
FT COMPBIAS 181..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 16..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P07560"
FT BINDING 64..68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P07560"
FT BINDING 122..125
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT BINDING 152..154
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT LIPID 200
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT LIPID 201
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT MUTAGEN 23
FT /note="T->N: Dominant-negative mutant. Mislocalizes to the
FT cytoplasm instead of membranes. Hardly any basolateral
FT endosomal tubules of the intestine. No interaction with
FT catalytically inactive tbc-4 A-155 mutant. Does not rescue
FT rab-10 null mutant, and fails to rescue the proximal PVD
FT defects in rab-10 deletion mutants, but also disrupts the
FT distal dendrite arbor and further reduces branch complexity
FT in the anterior region in wild-type animals."
FT /evidence="ECO:0000269|PubMed:16394106,
FT ECO:0000269|PubMed:20573983, ECO:0000269|PubMed:23100538,
FT ECO:0000269|PubMed:23185324, ECO:0000269|PubMed:25301900,
FT ECO:0000269|PubMed:26394140, ECO:0000269|PubMed:26633194"
FT MUTAGEN 68
FT /note="Q->L: Constitutively active mutant unable to
FT hydrolyze GTP. Associates correctly with membranes.
FT Displays more extensive network of basolateral endosomal
FT tubules of the intestine. Strongly reduced DCV secretion in
FT dorsally projecting cholinergic DA/DB motoneurons.
FT Interacts with the catalytically inactive tbc-4 A-155
FT mutant, but not with the catalytically active tbc-4.
FT Partially rescues rab-10 null mutant and fully rescues the
FT PVD dendrite morphogenesis defects in rab-10 deletion
FT mutants."
FT /evidence="ECO:0000269|PubMed:16394106,
FT ECO:0000269|PubMed:20573983, ECO:0000269|PubMed:23100538,
FT ECO:0000269|PubMed:23185324, ECO:0000269|PubMed:25301900,
FT ECO:0000269|PubMed:26393361, ECO:0000269|PubMed:26394140,
FT ECO:0000269|PubMed:26633194"
SQ SEQUENCE 201 AA; 22712 MW; 2D205ABF751EBF1A CRC64;
MARRPYDMLF KLLLIGDSGV GKTCILYRFS DDAFNTTFIS TIGIDFKIKT IELKGKKIKL
QIWDTAGQER FHTITTSYYR GAMGIMLVYD ITNAKSFDNI AKWLRNIDEH ASEDVVKMIL
GNKCDMSDRR VVSRERGEKI AQDHGISFHE TSAKLNVHVD TAFYDLAEAI LAKMPDSTDE
QSRDTVNPVQ PQRQSSSGGC C
