ID   ARL6_CAEEL              Reviewed;         190 AA.
AC   Q18510;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=ADP-ribosylation factor-like protein 6;
GN   Name=arl-6 {ECO:0000312|EMBL:CAA86319.1}; ORFNames=C38D4.8;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1] {ECO:0000312|EMBL:CAA86319.1}
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] {ECO:0000305}
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15314642; DOI=10.1038/ng1414;
RA   Fan Y., Esmail M.A., Ansley S.J., Blacque O.E., Boroevich K., Ross A.J.,
RA   Moore S.J., Badano J.L., May-Simera H., Compton D.S., Green J.S.,
RA   Lewis R.A., van Haelst M.M., Parfrey P.S., Baillie D.L., Beales P.L.,
RA   Katsanis N., Davidson W.S., Leroux M.R.;
RT   "Mutations in a member of the Ras superfamily of small GTP-binding proteins
RT   causes Bardet-Biedl syndrome.";
RL   Nat. Genet. 36:989-993(2004).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15314642}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in ciliated cells.
CC       {ECO:0000269|PubMed:15314642}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC       {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z46241; CAA86319.1; -; Genomic_DNA.
DR   PIR; T19826; T19826.
DR   RefSeq; NP_497993.1; NM_065592.1.
DR   AlphaFoldDB; Q18510; -.
DR   SMR; Q18510; -.
DR   BioGRID; 48141; 1.
DR   STRING; 6239.C38D4.8; -.
DR   EPD; Q18510; -.
DR   PaxDb; Q18510; -.
DR   EnsemblMetazoa; C38D4.8.1; C38D4.8.1; WBGene00000193.
DR   GeneID; 183311; -.
DR   KEGG; cel:CELE_C38D4.8; -.
DR   UCSC; C38D4.8; c. elegans.
DR   CTD; 183311; -.
DR   WormBase; C38D4.8; CE00921; WBGene00000193; arl-6.
DR   eggNOG; KOG0070; Eukaryota.
DR   GeneTree; ENSGT00940000156459; -.
DR   HOGENOM; CLU_040729_9_1_1; -.
DR   InParanoid; Q18510; -.
DR   OMA; TLLNHPX; -.
DR   OrthoDB; 1271528at2759; -.
DR   PhylomeDB; Q18510; -.
DR   Reactome; R-CEL-5620922; BBSome-mediated cargo-targeting to cilium.
DR   PRO; PR:Q18510; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00000193; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0005930; C:axoneme; IDA:WormBase.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0030425; C:dendrite; IDA:WormBase.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IDA:WormBase.
DR   GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0046907; P:intracellular transport; IDA:WormBase.
DR   GO; GO:0061512; P:protein localization to cilium; IBA:GO_Central.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   CDD; cd04157; Arl6; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR041839; Arl6.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR024156; Small_GTPase_ARF.
DR   InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR   PANTHER; PTHR11711; PTHR11711; 1.
DR   Pfam; PF00025; Arf; 1.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00178; SAR; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51417; ARF; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; GTP-binding; Lipoprotein; Myristate; Nucleotide-binding;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..190
FT                   /note="ADP-ribosylation factor-like protein 6"
FT                   /id="PRO_0000262959"
FT   BINDING         24..31
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         69..73
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         130..133
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D0J4"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   190 AA;  21031 MW;  D37C12A5AB509B81 CRC64;
     MGFFSSLSSL FGLGKKDVNI VVVGLDNSGK TTILNQLKTP ETRSQQIVPT VGHVVTNFST
     QNLSFHAFDM AGQMKYRSTW ESYFHSSQGV IFVLDSSDRL RMELLKDELM MVMEHKDVVS
     RGIPIVILAN KMDIPGAMTA SDITVALGLN LYRSGTWSIH STCALTGDGL DKAMQQLSAE
     ITKYMESRRT