ARL6_BOVIN
ID ARL6_BOVIN Reviewed; 186 AA.
AC Q0IIM2;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=ADP-ribosylation factor-like protein 6;
GN Name=ARL6;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH THE BBSOME.
RX PubMed=20603001; DOI=10.1016/j.cell.2010.05.015;
RA Jin H., White S.R., Shida T., Schulz S., Aguiar M., Gygi S.P., Bazan J.F.,
RA Nachury M.V.;
RT "The conserved Bardet-Biedl syndrome proteins assemble a coat that traffics
RT membrane proteins to cilia.";
RL Cell 141:1208-1219(2010).
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:0000269|PubMed:20603001}.
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; BC122575; AAI22576.1; -; mRNA.
DR RefSeq; NP_001069250.1; NM_001075782.1.
DR PDB; 6VBV; EM; 3.50 A; 3=1-186.
DR PDB; 6VOA; EM; 4.00 A; A=1-186.
DR PDBsum; 6VBV; -.
DR PDBsum; 6VOA; -.
DR AlphaFoldDB; Q0IIM2; -.
DR SMR; Q0IIM2; -.
DR STRING; 9913.ENSBTAP00000013306; -.
DR PaxDb; Q0IIM2; -.
DR PRIDE; Q0IIM2; -.
DR Ensembl; ENSBTAT00000013306; ENSBTAP00000013306; ENSBTAG00000010091.
DR GeneID; 519014; -.
DR KEGG; bta:519014; -.
DR CTD; 84100; -.
DR VEuPathDB; HostDB:ENSBTAG00000010091; -.
DR VGNC; VGNC:26149; ARL6.
DR eggNOG; KOG0070; Eukaryota.
DR GeneTree; ENSGT00940000156459; -.
DR HOGENOM; CLU_040729_9_1_1; -.
DR InParanoid; Q0IIM2; -.
DR OMA; WQIVPSN; -.
DR OrthoDB; 1271528at2759; -.
DR TreeFam; TF105466; -.
DR Reactome; R-BTA-5620922; BBSome-mediated cargo-targeting to cilium.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000010091; Expressed in oocyte and 102 other tissues.
DR GO; GO:0005879; C:axonemal microtubule; IDA:UniProtKB.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030117; C:membrane coat; IDA:UniProtKB.
DR GO; GO:0062063; F:BBSome binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; IDA:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0061512; P:protein localization to cilium; IBA:GO_Central.
DR GO; GO:0051258; P:protein polymerization; IDA:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IDA:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; GTP-binding;
KW Lipoprotein; Membrane; Myristate; Nucleotide-binding; Protein transport;
KW Reference proteome; 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_0000282338"
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"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:6VBV"
FT HELIX 30..35
FT /evidence="ECO:0007829|PDB:6VBV"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:6VBV"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:6VBV"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:6VBV"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:6VBV"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:6VBV"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:6VBV"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:6VBV"
FT TURN 116..120
FT /evidence="ECO:0007829|PDB:6VBV"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:6VBV"
FT HELIX 140..147
FT /evidence="ECO:0007829|PDB:6VBV"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:6VBV"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:6VBV"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:6VBV"
FT HELIX 170..182
FT /evidence="ECO:0007829|PDB:6VBV"
SQ SEQUENCE 186 AA; 21055 MW; FFF3D398E82E1C3E CRC64;
MGLLDRLSGL LGLKKKEVHV LCLGLDNSGK TTIINKLKPS NAQSQDIVPT IGFSIQKFKS
SSLSFTVFDM SGQGRYRNLW EHYYKEGQAI IFVIDSSDKL RMVVAKEELR TLLNHPDIKH
RRIPILFFAN KMDLRDALTS VKVSQLLCLE DIKDKPWHIC ASDAIKGEGL QEGVDWLQDQ
IQSVKT
