ARL13_CAEEL
ID ARL13_CAEEL Reviewed; 370 AA.
AC H2L0N8; Q2V075;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=ADP-ribosylation factor-like protein 13B;
DE AltName: Full=ADP-ribosylation factor-like protein 13;
GN Name=arl-13; ORFNames=Y37E3.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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]
RP FUNCTION, SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-12; CYS-13; CYS-14
RP AND CYS-15, AND MUTAGENESIS OF 12-CYS--CYS-15.
RX PubMed=20231383; DOI=10.1083/jcb.200908133;
RA Cevik S., Hori Y., Kaplan O.I., Kida K., Toivenon T., Foley-Fisher C.,
RA Cottell D., Katada T., Kontani K., Blacque O.E.;
RT "Joubert syndrome Arl13b functions at ciliary membranes and stabilizes
RT protein transport in Caenorhabditis elegans.";
RL J. Cell Biol. 188:953-969(2010).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20530210; DOI=10.1083/jcb.200912001;
RA Li Y., Wei Q., Zhang Y., Ling K., Hu J.;
RT "The small GTPases ARL-13 and ARL-3 coordinate intraflagellar transport and
RT ciliogenesis.";
RL J. Cell Biol. 189:1039-1051(2010).
RN [4]
RP SUMOYLATION AT LYS-239 AND LYS-331, AND MUTAGENESIS OF LYS-45; LYS-62;
RP LYS-230; LYS-239 AND LYS-331.
RX PubMed=23128241; DOI=10.1083/jcb.201203150;
RA Li Y., Zhang Q., Wei Q., Zhang Y., Ling K., Hu J.;
RT "SUMOylation of the small GTPase ARL-13 promotes ciliary targeting of
RT sensory receptors.";
RL J. Cell Biol. 199:589-598(2012).
RN [5]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-38 AND 366-ARG--PRO-369.
RX PubMed=24339792; DOI=10.1371/journal.pgen.1003977;
RA Cevik S., Sanders A.A., Van Wijk E., Boldt K., Clarke L., van Reeuwijk J.,
RA Hori Y., Horn N., Hetterschijt L., Wdowicz A., Mullins A., Kida K.,
RA Kaplan O.I., van Beersum S.E., Man Wu K., Letteboer S.J., Mans D.A.,
RA Katada T., Kontani K., Ueffing M., Roepman R., Kremer H., Blacque O.E.;
RT "Active transport and diffusion barriers restrict Joubert syndrome-
RT associated ARL13B/ARL-13 to an inv-like ciliary membrane subdomain.";
RL PLoS Genet. 9:E1003977-E1003977(2013).
CC -!- FUNCTION: Cilium-specific protein required to control the microtubule-
CC based, ciliary axoneme structure. Required for normal sensory cilium
CC function. May act by maintaining the association between IFT
CC subcomplexes A and B. {ECO:0000269|PubMed:20231383,
CC ECO:0000269|PubMed:20530210}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC {ECO:0000269|PubMed:20231383, ECO:0000269|PubMed:20530210,
CC ECO:0000269|PubMed:24339792}; Lipid-anchor
CC {ECO:0000269|PubMed:20231383, ECO:0000269|PubMed:20530210,
CC ECO:0000269|PubMed:24339792}. Note=Associates to the cilium membrane
CC via palmitoylation. Localizes to proximal ciliary membranes, to an
CC inversin-like subciliary membrane compartment, excluding the transition
CC zone.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=H2L0N8-1; Sequence=Displayed;
CC Name=b;
CC IsoId=H2L0N8-2; Sequence=VSP_053886;
CC -!- TISSUE SPECIFICITY: Specifically expressed in ciliated sensory neurons
CC throughout development in both hermaphrodites.
CC {ECO:0000269|PubMed:20530210}.
CC -!- DOMAIN: The RVVP region and palmitoylation sites are required for
CC compartmentalization inside cilium to prevent distal cilium and nuclear
CC targeting. {ECO:0000269|PubMed:24339792}.
CC -!- PTM: Sumoylation regulates the targeting of membrane sensory receptors
CC to the cilium. {ECO:0000269|PubMed:23128241}.
CC -!- DISRUPTION PHENOTYPE: Shortened cilia with various ultrastructural
CC deformities and a disrupted association between IFT subcomplexes A and
CC B. {ECO:0000269|PubMed:20530210}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; FO081769; CCD73425.1; -; Genomic_DNA.
DR EMBL; FO081769; CCD73426.1; -; Genomic_DNA.
DR RefSeq; NP_001032986.1; NM_001037897.1. [H2L0N8-1]
DR RefSeq; NP_001032987.1; NM_001037898.1. [H2L0N8-2]
DR AlphaFoldDB; H2L0N8; -.
DR SMR; H2L0N8; -.
DR BioGRID; 37252; 40.
DR STRING; 6239.Y37E3.5a; -.
DR PaxDb; H2L0N8; -.
DR EnsemblMetazoa; Y37E3.5a.1; Y37E3.5a.1; WBGene00021349. [H2L0N8-1]
DR EnsemblMetazoa; Y37E3.5b.1; Y37E3.5b.1; WBGene00021349. [H2L0N8-2]
DR GeneID; 171765; -.
DR KEGG; cel:CELE_Y37E3.5; -.
DR UCSC; Y37E3.5b; c. elegans.
DR CTD; 171765; -.
DR WormBase; Y37E3.5a; CE39044; WBGene00021349; arl-13. [H2L0N8-1]
DR WormBase; Y37E3.5b; CE39045; WBGene00021349; arl-13. [H2L0N8-2]
DR eggNOG; KOG0074; Eukaryota.
DR InParanoid; H2L0N8; -.
DR OMA; WFETIFC; -.
DR OrthoDB; 732329at2759; -.
DR PhylomeDB; H2L0N8; -.
DR Reactome; R-CEL-9646399; Aggrephagy.
DR PRO; PR:H2L0N8; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00021349; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; H2L0N8; baseline and differential.
DR GO; GO:0097543; C:ciliary inversin compartment; IDA:WormBase.
DR GO; GO:0060170; C:ciliary membrane; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0031528; C:microvillus membrane; IDA:WormBase.
DR GO; GO:0097730; C:non-motile cilium; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0042073; P:intraciliary transport; IMP:UniProtKB.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:WormBase.
DR GO; GO:0097500; P:receptor localization to non-motile cilium; IMP:WormBase.
DR GO; GO:0007606; P:sensory perception of chemical stimulus; IMP:WormBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR Pfam; PF00025; Arf; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51417; ARF; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cilium; GTP-binding;
KW Isopeptide bond; Lipoprotein; Membrane; Nucleotide-binding; Palmitate;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..370
FT /note="ADP-ribosylation factor-like protein 13B"
FT /id="PRO_0000425899"
FT REGION 255..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..369
FT /note="RVVP region"
FT COMPBIAS 258..272
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 31..38
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 75..79
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 134..137
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 12
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:20231383"
FT LIPID 13
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:20231383"
FT LIPID 14
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:20231383"
FT LIPID 15
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:20231383"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:23128241"
FT CROSSLNK 331
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:23128241"
FT VAR_SEQ 311..314
FT /note="NFCR -> K (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_053886"
FT MUTAGEN 12..15
FT /note="CCCC->ASAS: Abolishes palmitoylation and
FT localization to the cilium membrane."
FT /evidence="ECO:0000269|PubMed:20231383"
FT MUTAGEN 38
FT /note="T->N: Does not affect localization to cilia."
FT /evidence="ECO:0000269|PubMed:24339792"
FT MUTAGEN 45
FT /note="K->R: Does not affect sumoylation."
FT /evidence="ECO:0000269|PubMed:23128241"
FT MUTAGEN 62
FT /note="K->R: Does not affect sumoylation."
FT /evidence="ECO:0000269|PubMed:23128241"
FT MUTAGEN 230
FT /note="K->R: Does not affect sumoylation."
FT /evidence="ECO:0000269|PubMed:23128241"
FT MUTAGEN 239
FT /note="K->R: Decreaed sumoylation. Abolishes sumoylation;
FT when associated with R-331."
FT /evidence="ECO:0000269|PubMed:23128241"
FT MUTAGEN 331
FT /note="K->R: Decreaed sumoylation. Abolishes sumoylation;
FT when associated with R-239."
FT /evidence="ECO:0000269|PubMed:23128241"
FT MUTAGEN 366..369
FT /note="Missing: Amphid cilia are abnormally dispersed and
FT mis-positioned. Defects in intraflagellar transport."
FT /evidence="ECO:0000269|PubMed:24339792"
SQ SEQUENCE 370 AA; 42085 MW; 40609CA32001D2F4 CRC64;
MTEKSWFETI FCCCCHRTPI IRREIKLGCF GIGSAGKTTF LKVLKGEDPR DLLRTNGFST
VKMEYDETFH LTIYDVGGDK GIRGIWSNYY AEVHGIIYVI DYSTDETFTE SIEALHSLTS
NPHVQKKPIF LLLNNQNNRE FDDVEISNET KIQAGQHKIV LFSHFNKYNG YLDNIKSATL
TVMARAKKDR NEYQEQFVRF IDSISEHYVE LSEGVKTAEL ALRIRQEEAK EQRRLMQMKV
EHDALKADVA GLELRNQPPV QPPIPPDPPS DPKSASVHIE ESPPMSLASS TIPSDIIQST
PETGTPRDPV NFCRISQTST KPVSPESNSV KEEPTIILKD NYFLPPKAPG RQYSRIQRIQ
NVLNNRVVPK
