RAB28_CAEEL
ID RAB28_CAEEL Reviewed; 248 AA.
AC Q9XWR6; I7EVL1;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Ras-related protein Rab-28 {ECO:0000250|UniProtKB:P51157};
GN Name=rab-28 {ECO:0000312|WormBase:Y11D7A.4};
GN ORFNames=Y11D7A.4 {ECO:0000312|WormBase:Y11D7A.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {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:AFP33158.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-24.
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] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF THR-49 AND GLN-95.
RX PubMed=27930654; DOI=10.1371/journal.pgen.1006469;
RA Jensen V.L., Carter S., Sanders A.A., Li C., Kennedy J., Timbers T.A.,
RA Cai J., Scheidel N., Kennedy B.N., Morin R.D., Leroux M.R., Blacque O.E.;
RT "Whole-organism developmental expression profiling identifies rab-28 as a
RT novel ciliary GTPase associated with the BBSome and intraflagellar
RT transport.";
RL PLoS Genet. 12:E1006469-E1006469(2016).
CC -!- FUNCTION: GTPase. Intraflagellar transport (IFT) cargo that undergoes
CC bidirectional IFT along the ciliary axoneme when in active GTP-bound
CC state in amphid and phasmid ciliated sensory neurons. Targeting and
CC function as IFT cargo may depend on the BBSome, an IFT cargo adapter.
CC Does not undergo IFT when in inactive GDP-bound state. May in turn play
CC a role in cilium structure and/or function in ciliated sensory neurons.
CC {ECO:0000269|PubMed:27930654}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC {ECO:0000269|PubMed:27930654}; Peripheral membrane protein
CC {ECO:0000269|PubMed:27930654}. Perikaryon
CC {ECO:0000269|PubMed:27930654}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:27930654}. Note=In active GTP-bound state, is
CC targeted to the periciliary membrane in a bbs-8-dependent manner. In
CC inactive GDP-bound state, is diffusely localized in the cilium.
CC {ECO:0000269|PubMed:27930654}.
CC -!- TISSUE SPECIFICITY: Expressed in amphid and phasmid ciliated sensory
CC neurons. {ECO:0000269|PubMed:27930654}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, with seemingly normal
CC ciliary structure, and normal transport and function of IFT proteins
CC such as osm-6. {ECO:0000269|PubMed:27930654}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; BX284604; CAA21582.1; -; Genomic_DNA.
DR EMBL; JQ235194; AFP33158.1; -; mRNA.
DR PIR; T26461; T26461.
DR RefSeq; NP_501609.1; NM_069208.1.
DR AlphaFoldDB; Q9XWR6; -.
DR SMR; Q9XWR6; -.
DR STRING; 6239.Y11D7A.4; -.
DR EPD; Q9XWR6; -.
DR PaxDb; Q9XWR6; -.
DR EnsemblMetazoa; Y11D7A.4.1; Y11D7A.4.1; WBGene00004281.
DR GeneID; 189429; -.
DR KEGG; cel:CELE_Y11D7A.4; -.
DR UCSC; Y11D7A.4; c. elegans.
DR CTD; 189429; -.
DR WormBase; Y11D7A.4; CE19030; WBGene00004281; rab-28.
DR eggNOG; KOG0078; Eukaryota.
DR GeneTree; ENSGT00940000164241; -.
DR HOGENOM; CLU_041217_10_4_1; -.
DR InParanoid; Q9XWR6; -.
DR OMA; YIYGSHA; -.
DR OrthoDB; 1144210at2759; -.
DR PhylomeDB; Q9XWR6; -.
DR PRO; PR:Q9XWR6; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004281; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0097546; C:ciliary base; IDA:UniProtKB.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035869; C:ciliary transition zone; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:1990075; C:periciliary membrane compartment; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0003386; P:amphid sensory organ development; IMP:UniProtKB.
DR GO; GO:0035082; P:axoneme assembly; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0035641; P:locomotory exploration behavior; IMP:UniProtKB.
DR GO; GO:1902017; P:regulation of cilium assembly; 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.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cilium; Cytoplasm; Cytoskeleton;
KW GTP-binding; Membrane; Nucleotide-binding; Reference proteome; Transport.
FT CHAIN 1..248
FT /note="Ras-related protein Rab-28"
FT /evidence="ECO:0000305"
FT /id="PRO_0000442189"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 64..72
FT /note="Effector region"
FT /evidence="ECO:0000305"
FT BINDING 42..50
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:27930654"
FT BINDING 91..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:27930654"
FT BINDING 152..155
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P51157"
FT BINDING 182..184
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P51157"
FT MUTAGEN 49
FT /note="T->N: Expected to give rise to an inactive GDP-bound
FT state. Cilia-related sensory abnormalities and failure to
FT undergo intraflagellar transport."
FT /evidence="ECO:0000269|PubMed:27930654"
FT MUTAGEN 95
FT /note="Q->L: Expected to give rise to a constitutively
FT active GTP-bound state. Cilia-related sensory
FT abnormalities, but undergoes intraflagellar transport, but
FT at a reduced frequency compared to wild-type."
FT /evidence="ECO:0000269|PubMed:27930654"
SQ SEQUENCE 248 AA; 27319 MW; 3F17527F9BC58EE2 CRC64;
MTTMGEDEAP ALPKKSPLPE KIDEADVDDD PDDKVIKIVV VGDGASGKTS ICQRFAKESF
DKSYHQTLGL DFFSRRITLP HEMQVLVQVW DIGGQSIAGE MIDKYLTGAN IVFLVYDVTN
SKSFENAVDW LSVVKKNTKS SETPVKLVLM GNKTDLEERR VVSVEAHKNF ATSNDMMPTY
VSAKTGDTVF LTFRQAVAEV LNVGLSRAEV EADIEIVQGS VIEQPKQSDA SYARRSDQSR
STSVCSIT
