ARL6_PONAB
ID ARL6_PONAB Reviewed; 186 AA.
AC Q5R4G5; Q5R400;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=ADP-ribosylation factor-like protein 6;
GN Name=ARL6;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in membrane protein trafficking at the base of the
CC ciliary organelle. Mediates recruitment onto plasma membrane of the
CC BBSome complex which would constitute a coat complex required for
CC sorting of specific membrane proteins to the primary cilia. Together
CC with the BBSome complex and LTZL1, controls SMO ciliary trafficking and
CC contributes to the sonic hedgehog (SHH) pathway regulation. May
CC regulate cilia assembly and disassembly and subsequent ciliary
CC signaling events such as the Wnt signaling cascade. Isoform 2 may be
CC required for proper retinal function and organization (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SEC61B, ARL6IP1, ARL6IP2, ARL6IP3, ARL6IP4
CC ARL6IP5 and ARL6IP6. Interacts (GTP-bound form) with the BBSome a
CC complex that contains BBS1, BBS2, BBS4, BBS5, BBS7, BBS8/TTC8, BBS9 and
CC BBIP10. Interacts (GTP-free form) with IFT27.
CC {ECO:0000250|UniProtKB:Q9H0F7}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250}.
CC Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. Note=Appears
CC in a pattern of punctae flanking the microtubule axoneme that likely
CC correspond to small membrane-associated patches. Localizes to the so-
CC called ciliary gate where vesicles carrying ciliary cargo fuse with the
CC membrane (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; CR861283; CAH93351.1; -; mRNA.
DR EMBL; CR861460; CAH93516.1; -; mRNA.
DR RefSeq; NP_001127054.1; NM_001133582.1.
DR AlphaFoldDB; Q5R4G5; -.
DR SMR; Q5R4G5; -.
DR Ensembl; ENSPPYT00000015837; ENSPPYP00000015230; ENSPPYG00000013623.
DR GeneID; 100174082; -.
DR KEGG; pon:100174082; -.
DR CTD; 84100; -.
DR GeneTree; ENSGT00940000156459; -.
DR InParanoid; Q5R4G5; -.
DR OrthoDB; 1271528at2759; -.
DR Proteomes; UP000001595; Chromosome 3.
DR GO; GO:0005879; C:axonemal microtubule; ISS:UniProtKB.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030117; C:membrane coat; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IEA:Ensembl.
DR GO; GO:0061512; P:protein localization to cilium; IEA:Ensembl.
DR GO; GO:0051258; P:protein polymerization; ISS:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:Ensembl.
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 Cell membrane; Cell projection; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; GTP-binding; Lipoprotein; Magnesium; Membrane; Metal-binding;
KW Myristate; Nucleotide-binding; Protein transport; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..186
FT /note="ADP-ribosylation factor-like protein 6"
FT /id="PRO_0000207474"
FT BINDING 24..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 69..73
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 72
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"
FT BINDING 164
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT CONFLICT 74
FT /note="G -> E (in Ref. 1; CAH93516)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="V -> A (in Ref. 1; CAH93516)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 186 AA; 21112 MW; 4DEB74A23DC95037 CRC64;
MGLLDRLSIL LGLKKKEVHV LCLGLDNSGK TTIINKLKPS NAQSQNILPT IGFSIEKFKS
SSLSFTVFDM SGQGRYRNLW EHYYKEGQAI IFVIDSSDRL RMVVAKEELD TLLNHPDIKH
RRIPILFFAN KMDLRDAVTS VKVSQLLCLE NIKDKPWHIC ASDAIKGEGL QEGVDWLQDQ
IQTVKT
