ARL6_HUMAN
ID ARL6_HUMAN Reviewed; 186 AA.
AC Q9H0F7; A8KA93; D3DN31;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=ADP-ribosylation factor-like protein 6;
DE AltName: Full=Bardet-Biedl syndrome 3 protein;
GN Name=ARL6; Synonyms=BBS3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INVOLVEMENT IN BBS3.
RX PubMed=15258860; DOI=10.1086/423903;
RA Chiang A.P., Nishimura D., Searby C., Elbedour K., Carmi R., Ferguson A.L.,
RA Secrist J., Braun T., Casavant T., Stone E.M., Sheffield V.C.;
RT "Comparative genomic analysis identifies an ADP-ribosylation factor-like
RT gene as the cause of Bardet-Biedl Syndrome (BBS3).";
RL Am. J. Hum. Genet. 75:475-484(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND 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).
RN [8]
RP ALTERNATIVE SPLICING (ISOFORM 2).
RX PubMed=20333246; DOI=10.1371/journal.pgen.1000884;
RA Pretorius P.R., Baye L.M., Nishimura D.Y., Searby C.C., Bugge K., Yang B.,
RA Mullins R.F., Stone E.M., Sheffield V.C., Slusarski D.C.;
RT "Identification and functional analysis of the vision-specific BBS3 (ARL6)
RT long isoform.";
RL PLoS Genet. 6:E1000884-E1000884(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP FUNCTION.
RX PubMed=22072986; DOI=10.1371/journal.pgen.1002358;
RA Seo S., Zhang Q., Bugge K., Breslow D.K., Searby C.C., Nachury M.V.,
RA Sheffield V.C.;
RT "A novel protein LZTFL1 regulates ciliary trafficking of the BBSome and
RT Smoothened.";
RL PLoS Genet. 7:E1002358-E1002358(2011).
RN [11]
RP INTERACTION WITH IFT27.
RX PubMed=25443296; DOI=10.1016/j.devcel.2014.09.004;
RA Liew G.M., Ye F., Nager A.R., Murphy J.P., Lee J.S., Aguiar M.,
RA Breslow D.K., Gygi S.P., Nachury M.V.;
RT "The intraflagellar transport protein IFT27 promotes BBSome exit from cilia
RT through the GTPase ARL6/BBS3.";
RL Dev. Cell 31:265-278(2014).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 16-186 IN COMPLEX WITH GTP AND
RP MAGNESIUM, FUNCTION, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANTS
RP MET-31; ARG-31; ALA-169 AND TRP-170.
RX PubMed=20207729; DOI=10.1074/jbc.m109.070953;
RA Wiens C.J., Tong Y., Esmail M.A., Oh E., Gerdes J.M., Wang J., Tempel W.,
RA Rattner J.B., Katsanis N., Park H.W., Leroux M.R.;
RT "Bardet-Biedl syndrome-associated small GTPase ARL6 (BBS3) functions at or
RT near the ciliary gate and modulates Wnt signaling.";
RL J. Biol. Chem. 285:16218-16230(2010).
RN [13]
RP VARIANTS BBS3 ARG-31; MET-31; ALA-169 AND TRP-170.
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).
RN [14]
RP CHARACTERIZATION OF VARIANTS MET-31; ARG-31; ALA-169 AND TRP-170.
RX PubMed=19236846; DOI=10.1016/j.bbrc.2009.02.087;
RA Kobayashi T., Hori Y., Ueda N., Kajiho H., Muraoka S., Shima F.,
RA Kataoka T., Kontani K., Katada T.;
RT "Biochemical characterization of missense mutations in the Arf/Arl-family
RT small GTPase Arl6 causing Bardet-Biedl syndrome.";
RL Biochem. Biophys. Res. Commun. 381:439-442(2009).
RN [15]
RP VARIANT RP55 VAL-89.
RX PubMed=19956407;
RA Aldahmesh M.A., Safieh L.A., Alkuraya H., Al-Rajhi A., Shamseldin H.,
RA Hashem M., Alzahrani F., Khan A.O., Alqahtani F., Rahbeeni Z., Alowain M.,
RA Khalak H., Al-Hazzaa S., Meyer B.F., Alkuraya F.S.;
RT "Molecular characterization of retinitis pigmentosa in Saudi Arabia.";
RL Mol. Vis. 15:2464-2469(2009).
RN [16]
RP VARIANT BBS3 THR-94.
RX PubMed=23219996; DOI=10.1016/j.gene.2012.11.023;
RA Khan S., Ullah I., Irfanullah X., Touseef M., Basit S., Khan M.N.,
RA Ahmad W.;
RT "Novel homozygous mutations in the genes ARL6 and BBS10 underlying Bardet-
RT Biedl syndrome.";
RL Gene 515:84-88(2013).
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
CC (PubMed:20603001). Together with BBS1, is necessary for correct
CC trafficking of PKD1 to primary cilia (By similarity). Together with the
CC BBSome complex and LTZL1, controls SMO ciliary trafficking and
CC contributes to the sonic hedgehog (SHH) pathway regulation
CC (PubMed:22072986). May regulate cilia assembly and disassembly and
CC subsequent ciliary signaling events such as the Wnt signaling cascade
CC (PubMed:20207729). Isoform 2 may be required for proper retinal
CC function and organization (By similarity).
CC {ECO:0000250|UniProtKB:O88848, ECO:0000269|PubMed:20207729,
CC ECO:0000269|PubMed:20603001, ECO:0000269|PubMed:22072986}.
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:20207729, ECO:0000269|PubMed:20603001,
CC ECO:0000269|PubMed:25443296}.
CC -!- INTERACTION:
CC Q9H0F7; Q8NFJ9: BBS1; NbExp=4; IntAct=EBI-2891949, EBI-1805484;
CC Q9H0F7-1; Q8NFJ9: BBS1; NbExp=3; IntAct=EBI-16127759, EBI-1805484;
CC Q9H0F7-1; A8JEA1: BBS1; Xeno; NbExp=2; IntAct=EBI-16127759, EBI-16127672;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane; Peripheral
CC membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, cilium
CC axoneme. Cytoplasm, cytoskeleton, cilium basal body. Note=Appears in a
CC 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.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=BBS3;
CC IsoId=Q9H0F7-1; Sequence=Displayed;
CC Name=2; Synonyms=BBS3L;
CC IsoId=Q9H0F7-2; Sequence=VSP_040511;
CC -!- DISEASE: Bardet-Biedl syndrome 3 (BBS3) [MIM:600151]: A syndrome
CC characterized by usually severe pigmentary retinopathy, early-onset
CC obesity, polydactyly, hypogenitalism, renal malformation and
CC intellectual disability. Secondary features include diabetes mellitus,
CC hypertension and congenital heart disease. Bardet-Biedl syndrome
CC inheritance is autosomal recessive, but three mutated alleles (two at
CC one locus, and a third at a second locus) may be required for clinical
CC manifestation of some forms of the disease.
CC {ECO:0000269|PubMed:15258860, ECO:0000269|PubMed:15314642,
CC ECO:0000269|PubMed:23219996}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Retinitis pigmentosa 55 (RP55) [MIM:613575]: A retinal
CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis
CC pigmentosa is characterized by retinal pigment deposits visible on
CC fundus examination and primary loss of rod photoreceptor cells followed
CC by secondary loss of cone photoreceptors. Patients typically have night
CC vision blindness and loss of midperipheral visual field. As their
CC condition progresses, they lose their far peripheral visual field and
CC eventually central vision as well. {ECO:0000269|PubMed:19956407}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; AL136815; CAB66749.1; -; mRNA.
DR EMBL; AK292958; BAF85647.1; -; mRNA.
DR EMBL; AC110491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79880.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79881.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79882.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79883.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79884.1; -; Genomic_DNA.
DR EMBL; BC024239; AAH24239.1; -; mRNA.
DR CCDS; CCDS2928.1; -. [Q9H0F7-1]
DR RefSeq; NP_001265222.1; NM_001278293.2. [Q9H0F7-1]
DR RefSeq; NP_001310442.1; NM_001323513.1. [Q9H0F7-2]
DR RefSeq; NP_115522.1; NM_032146.5. [Q9H0F7-1]
DR RefSeq; NP_816931.1; NM_177976.3. [Q9H0F7-1]
DR RefSeq; XP_016862800.1; XM_017007311.1. [Q9H0F7-1]
DR PDB; 2H57; X-ray; 2.00 A; A/B/C=16-186.
DR PDBsum; 2H57; -.
DR AlphaFoldDB; Q9H0F7; -.
DR SMR; Q9H0F7; -.
DR BioGRID; 123889; 13.
DR DIP; DIP-61535N; -.
DR IntAct; Q9H0F7; 19.
DR STRING; 9606.ENSP00000337722; -.
DR iPTMnet; Q9H0F7; -.
DR PhosphoSitePlus; Q9H0F7; -.
DR BioMuta; ARL6; -.
DR DMDM; 14547903; -.
DR EPD; Q9H0F7; -.
DR jPOST; Q9H0F7; -.
DR MassIVE; Q9H0F7; -.
DR MaxQB; Q9H0F7; -.
DR PaxDb; Q9H0F7; -.
DR PeptideAtlas; Q9H0F7; -.
DR PRIDE; Q9H0F7; -.
DR ProteomicsDB; 80274; -. [Q9H0F7-1]
DR ProteomicsDB; 80275; -. [Q9H0F7-2]
DR ABCD; Q9H0F7; 1 sequenced antibody.
DR Antibodypedia; 15743; 140 antibodies from 30 providers.
DR DNASU; 84100; -.
DR Ensembl; ENST00000335979.6; ENSP00000337722.2; ENSG00000113966.10. [Q9H0F7-1]
DR Ensembl; ENST00000394206.5; ENSP00000377756.1; ENSG00000113966.10. [Q9H0F7-1]
DR Ensembl; ENST00000463745.6; ENSP00000419619.1; ENSG00000113966.10. [Q9H0F7-1]
DR Ensembl; ENST00000493990.5; ENSP00000418057.1; ENSG00000113966.10. [Q9H0F7-1]
DR GeneID; 84100; -.
DR KEGG; hsa:84100; -.
DR MANE-Select; ENST00000463745.6; ENSP00000419619.1; NM_001278293.3; NP_001265222.1.
DR UCSC; uc003dru.4; human. [Q9H0F7-1]
DR CTD; 84100; -.
DR DisGeNET; 84100; -.
DR GeneCards; ARL6; -.
DR GeneReviews; ARL6; -.
DR HGNC; HGNC:13210; ARL6.
DR HPA; ENSG00000113966; Tissue enhanced (retina).
DR MalaCards; ARL6; -.
DR MIM; 600151; phenotype.
DR MIM; 608845; gene.
DR MIM; 613575; phenotype.
DR neXtProt; NX_Q9H0F7; -.
DR OpenTargets; ENSG00000113966; -.
DR Orphanet; 110; Bardet-Biedl syndrome.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA134931939; -.
DR VEuPathDB; HostDB:ENSG00000113966; -.
DR eggNOG; KOG0070; Eukaryota.
DR GeneTree; ENSGT00940000156459; -.
DR HOGENOM; CLU_040729_9_1_1; -.
DR InParanoid; Q9H0F7; -.
DR OMA; WQIVPSN; -.
DR OrthoDB; 1271528at2759; -.
DR PhylomeDB; Q9H0F7; -.
DR TreeFam; TF105466; -.
DR PathwayCommons; Q9H0F7; -.
DR Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium.
DR SignaLink; Q9H0F7; -.
DR BioGRID-ORCS; 84100; 11 hits in 1072 CRISPR screens.
DR ChiTaRS; ARL6; human.
DR EvolutionaryTrace; Q9H0F7; -.
DR GeneWiki; ARL6; -.
DR GenomeRNAi; 84100; -.
DR Pharos; Q9H0F7; Tbio.
DR PRO; PR:Q9H0F7; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9H0F7; protein.
DR Bgee; ENSG00000113966; Expressed in oviduct epithelium and 164 other tissues.
DR ExpressionAtlas; Q9H0F7; baseline and differential.
DR Genevisible; Q9H0F7; HS.
DR GO; GO:0005879; C:axonemal microtubule; ISS:UniProtKB.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0030117; C:membrane coat; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
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; IMP:UniProtKB.
DR GO; GO:0007368; P:determination of left/right symmetry; ISS:BHF-UCL.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0032402; P:melanosome transport; ISS:BHF-UCL.
DR GO; GO:0061512; P:protein localization to cilium; IMP:MGI.
DR GO; GO:0051258; P:protein polymerization; ISS:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR GO; GO:0016055; P:Wnt signaling pathway; IMP:UniProtKB.
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; Alternative splicing; Bardet-Biedl syndrome; Cell membrane;
KW Cell projection; Ciliopathy; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Disease variant; GTP-binding; Intellectual disability;
KW Lipoprotein; Magnesium; Membrane; Metal-binding; Myristate;
KW Nucleotide-binding; Obesity; Protein transport; Reference proteome;
KW Retinitis pigmentosa; Sensory transduction; Transport; Vision.
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_0000207472"
FT BINDING 24..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:20207729"
FT BINDING 31
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:20207729"
FT BINDING 50
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:20207729"
FT BINDING 50
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:20207729"
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:0000269|PubMed:20207729"
FT BINDING 130..133
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:20207729"
FT BINDING 164
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:20207729"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 179..186
FT /note="DQIQTVKT -> EKTIQSDPDCEDMKR (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040511"
FT VARIANT 31
FT /note="T -> M (in BBS3; abrogates the GTP-binding ability
FT without affecting GDP-binding/dissociating properties;
FT increased proteasomal degradation; dbSNP:rs104893680)"
FT /evidence="ECO:0000269|PubMed:15314642,
FT ECO:0000269|PubMed:19236846, ECO:0000269|PubMed:20207729"
FT /id="VAR_027643"
FT VARIANT 31
FT /note="T -> R (in BBS3; locked in a GDP-bound state that
FT differs from its wild-type counterpart which is mainly GTP-
FT bound; increased proteasomal degradation;
FT dbSNP:rs104893680)"
FT /evidence="ECO:0000269|PubMed:15314642,
FT ECO:0000269|PubMed:19236846, ECO:0000269|PubMed:20207729"
FT /id="VAR_027644"
FT VARIANT 89
FT /note="A -> V (in RP55; dbSNP:rs587777805)"
FT /evidence="ECO:0000269|PubMed:19956407"
FT /id="VAR_064184"
FT VARIANT 94
FT /note="I -> T (in BBS3; dbSNP:rs771054395)"
FT /evidence="ECO:0000269|PubMed:23219996"
FT /id="VAR_071405"
FT VARIANT 169
FT /note="G -> A (in BBS3; abrogates the GTP-binding ability;
FT increased proteasomal degradation; dbSNP:rs104893679)"
FT /evidence="ECO:0000269|PubMed:15314642,
FT ECO:0000269|PubMed:19236846, ECO:0000269|PubMed:20207729"
FT /id="VAR_027645"
FT VARIANT 170
FT /note="L -> W (in BBS3; abrogates the GTP-binding ability;
FT increased proteasomal degradation; dbSNP:rs104893681)"
FT /evidence="ECO:0000269|PubMed:15314642,
FT ECO:0000269|PubMed:19236846, ECO:0000269|PubMed:20207729"
FT /id="VAR_027646"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:2H57"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:2H57"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2H57"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:2H57"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:2H57"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:2H57"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:2H57"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:2H57"
FT HELIX 99..114
FT /evidence="ECO:0007829|PDB:2H57"
FT TURN 116..120
FT /evidence="ECO:0007829|PDB:2H57"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:2H57"
FT HELIX 140..147
FT /evidence="ECO:0007829|PDB:2H57"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:2H57"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:2H57"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:2H57"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:2H57"
SQ SEQUENCE 186 AA; 21097 MW; 42E37FC7886BF1F0 CRC64;
MGLLDRLSVL LGLKKKEVHV LCLGLDNSGK TTIINKLKPS NAQSQNILPT IGFSIEKFKS
SSLSFTVFDM SGQGRYRNLW EHYYKEGQAI IFVIDSSDRL RMVVAKEELD TLLNHPDIKH
RRIPILFFAN KMDLRDAVTS VKVSQLLCLE NIKDKPWHIC ASDAIKGEGL QEGVDWLQDQ
IQTVKT
