ARL3_HUMAN
ID ARL3_HUMAN Reviewed; 182 AA.
AC P36405; B2R6C7; Q53X83; Q5JSM2;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=ADP-ribosylation factor-like protein 3;
GN Name=ARL3; Synonyms=ARFL3;
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 [MRNA].
RX PubMed=8034651; DOI=10.1016/s0021-9258(17)32257-3;
RA Cavenagh M.A., Breiner M., Schurmann A., Rosenwald A.G., Terui T.,
RA Zhang C.-J., Randoazzo P.A., Adams M., Joost H.-G., Kahn R.A.;
RT "ADP-ribosylation factor (ARF)-like 3, a new member of the ARF family of
RT GTP-binding proteins cloned from human and rat tissues.";
RL J. Biol. Chem. 269:18937-18942(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-34.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [7]
RP PROTEIN SEQUENCE OF 80-97 AND 128-149, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP LACK OF INTERACTION WITH TBCC.
RX PubMed=10831612; DOI=10.1083/jcb.149.5.1087;
RA Bhamidipati A., Lewis S.A., Cowan N.J.;
RT "ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of
RT tubulin-folding cofactor D with native tubulin.";
RL J. Cell Biol. 149:1087-1096(2000).
RN [9]
RP INTERACTION WITH ARL2BP; GOLGA4; PDE6D AND UNC119, AND MUTAGENESIS OF
RP GLN-71.
RX PubMed=11303027; DOI=10.1074/jbc.m102359200;
RA Van Valkenburgh H., Shern J.F., Sharer J.D., Zhu X., Kahn R.A.;
RT "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific
RT and shared effectors: characterizing ARL1-binding proteins.";
RL J. Biol. Chem. 276:22826-22837(2001).
RN [10]
RP ASSOCIATION WITH MICROTUBULES, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12417528; DOI=10.1093/hmg/11.24.3065;
RA Grayson C., Bartolini F., Chapple J.P., Willison K.R., Bhamidipati A.,
RA Lewis S.A., Luthert P.J., Hardcastle A.J., Cowan N.J., Cheetham M.E.;
RT "Localization in the human retina of the X-linked retinitis pigmentosa
RT protein RP2, its homologue cofactor C and the RP2 interacting protein
RT Arl3.";
RL Hum. Mol. Genet. 11:3065-3074(2002).
RN [11]
RP INTERACTION WITH RP2 AND ARL2BP, AND MUTAGENESIS OF THR-31 AND GLN-71.
RX PubMed=11847227; DOI=10.1074/jbc.m200128200;
RA Bartolini F., Bhamidipati A., Thomas S., Schwahn U., Lewis S.A.,
RA Cowan N.J.;
RT "Functional overlap between retinitis pigmentosa 2 protein and the tubulin-
RT specific chaperone cofactor C.";
RL J. Biol. Chem. 277:14629-14634(2002).
RN [12]
RP INTERACTION WITH SYS1, AND SUBCELLULAR LOCATION.
RX PubMed=15077113; DOI=10.1038/ncb1120;
RA Behnia R., Panic B., Whyte J.R.C., Munro S.;
RT "Targeting of the Arf-like GTPase Arl3p to the Golgi requires N-terminal
RT acetylation and the membrane protein Sys1p.";
RL Nat. Cell Biol. 6:405-413(2004).
RN [13]
RP FUNCTION, MUTAGENESIS OF GLN-71, SUBCELLULAR LOCATION, AND
RP MICROTUBULE-ASSOCIATED.
RX PubMed=16525022; DOI=10.1091/mbc.e05-10-0929;
RA Zhou C., Cunningham L., Marcus A.I., Li Y., Kahn R.A.;
RT "Arl2 and Arl3 regulate different microtubule-dependent processes.";
RL Mol. Biol. Cell 17:2476-2487(2006).
RN [14]
RP INTERACTION WITH RP2.
RX PubMed=16472755; DOI=10.1016/j.str.2005.11.008;
RA Kuehnel K., Veltel S., Schlichting I., Wittinghofer A.;
RT "Crystal structure of the human retinitis pigmentosa 2 protein and its
RT interaction with Arl3.";
RL Structure 14:367-378(2006).
RN [15]
RP FUNCTION, GTP/GDP BINDING, IDENTIFICATION IN A COMPLEX WITH UNC119 AND RP2,
RP AND SUBCELLULAR LOCATION.
RX PubMed=18588884; DOI=10.1016/j.febslet.2008.05.053;
RA Veltel S., Kravchenko A., Ismail S., Wittinghofer A.;
RT "Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3-effector-
RT GAP complex.";
RL FEBS Lett. 582:2501-2507(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
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 [18]
RP FUNCTION, MUTAGENESIS OF THR-31 AND GLN-71, AND INTERACTION WITH DNAAF9.
RX PubMed=22085962; DOI=10.1101/gad.173443.111;
RA Wright K.J., Baye L.M., Olivier-Mason A., Mukhopadhyay S., Sang L.,
RA Kwong M., Wang W., Pretorius P.R., Sheffield V.C., Sengupta P.,
RA Slusarski D.C., Jackson P.K.;
RT "An ARL3-UNC119-RP2 GTPase cycle targets myristoylated NPHP3 to the primary
RT cilium.";
RL Genes Dev. 25:2347-2360(2011).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [21]
RP INVOLVEMENT IN RP83, AND VARIANT RP83 CYS-90.
RX PubMed=26964041; DOI=10.1371/journal.pone.0150944;
RA Strom S.P., Clark M.J., Martinez A., Garcia S., Abelazeem A.A., Matynia A.,
RA Parikh S., Sullivan L.S., Bowne S.J., Daiger S.P., Gorin M.B.;
RT "De novo occurrence of a variant in ARL3 and apparent autosomal dominant
RT transmission of retinitis pigmentosa.";
RL PLoS ONE 11:E0150944-E0150944(2016).
RN [22]
RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN JBTS35, VARIANTS JBTS35
RP CYS-149 AND HIS-149, AND CHARACTERIZATION OF VARIANT JBTS35 HIS-149.
RX PubMed=30269812; DOI=10.1016/j.ajhg.2018.08.015;
RA Alkanderi S., Molinari E., Shaheen R., Elmaghloob Y., Stephen L.A.,
RA Sammut V., Ramsbottom S.A., Srivastava S., Cairns G., Edwards N.,
RA Rice S.J., Ewida N., Alhashem A., White K., Miles C.G., Steel D.H.,
RA Alkuraya F.S., Ismail S., Sayer J.A.;
RT "ARL3 Mutations Cause Joubert Syndrome by Disrupting Ciliary Protein
RT Composition.";
RL Am. J. Hum. Genet. 103:612-620(2018).
CC -!- FUNCTION: Small GTP-binding protein which cycles between an inactive
CC GDP-bound and an active GTP-bound form, and the rate of cycling is
CC regulated by guanine nucleotide exchange factors (GEF) and GTPase-
CC activating proteins (GAP) (PubMed:16525022, PubMed:18588884). Required
CC for normal cytokinesis and cilia signaling (PubMed:22085962). Requires
CC assistance from GTPase-activating proteins (GAPs) like RP2 and PDE6D,
CC in order to cycle between inactive GDP-bound and active GTP-bound
CC forms. Required for targeting proteins to the cilium, including
CC myristoylated NPHP3 and prenylated INPP5E (PubMed:30269812). Targets
CC NPHP3 to the ciliary membrane by releasing myristoylated NPHP3 from
CC UNC119B cargo adapter into the cilium (PubMed:22085962). Required for
CC PKD1:PKD2 complex targeting from the trans-Golgi network to the cilium
CC (By similarity). {ECO:0000250|UniProtKB:Q9WUL7,
CC ECO:0000269|PubMed:16525022, ECO:0000269|PubMed:18588884,
CC ECO:0000269|PubMed:22085962}.
CC -!- SUBUNIT: Found in a complex with ARL3, RP2 and UNC119 (or UNC119B); RP2
CC induces hydrolysis of GTP ARL3 in the complex, leading to the release
CC of UNC119 (or UNC119B) (PubMed:11303027, PubMed:11847227,
CC PubMed:18588884). Interacts with RP2; interaction is direct and
CC stimulated with the activated GTP-bound form of ARL3 (PubMed:16472755).
CC Interacts with SYS1 (PubMed:11303027, PubMed:11847227,
CC PubMed:15077113). The GTP-bound form interacts with ARL2BP and PDE6D
CC (PubMed:11303027, PubMed:11847227). Microtubule-associated protein
CC (PubMed:11303027, PubMed:16525022). May interact with GOLGA4
CC (PubMed:11303027). Interacts with GGA1; the interaction recruits
CC PKD1:PKD2 complex to trans-Golgi network and is required for ciliary
CC targeting of PKD1:PKD2 complex (By similarity). Interacts with DNAAF9
CC (PubMed:22085962). {ECO:0000250|UniProtKB:Q9WUL7,
CC ECO:0000269|PubMed:11303027, ECO:0000269|PubMed:11847227,
CC ECO:0000269|PubMed:15077113, ECO:0000269|PubMed:16472755,
CC ECO:0000269|PubMed:16525022, ECO:0000269|PubMed:18588884,
CC ECO:0000269|PubMed:22085962}.
CC -!- INTERACTION:
CC P36405; Q9Y2Y0: ARL2BP; NbExp=6; IntAct=EBI-712710, EBI-3449344;
CC P36405; O43924: PDE6D; NbExp=8; IntAct=EBI-712710, EBI-712685;
CC P36405; O60907: TBL1X; NbExp=3; IntAct=EBI-712710, EBI-3505105;
CC P36405; Q13432: UNC119; NbExp=15; IntAct=EBI-712710, EBI-711260;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane
CC protein; Cytoplasmic side. Cytoplasm, cytoskeleton, spindle. Nucleus.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
CC Cytoplasm. Cell projection, cilium {ECO:0000269|PubMed:30269812}.
CC Note=Detected predominantly in the photoreceptor connecting cilium.
CC Present on the mitotic spindle. Centrosome-associated throughout the
CC cell cycle. Not detected to interphase microtubules.
CC -!- TISSUE SPECIFICITY: Expressed in the retina. Strongly expressed in
CC connecting cilium, the myoid region of the inner segments (IS) and in
CC cone photoreceptors (at protein level). {ECO:0000269|PubMed:12417528}.
CC -!- DISEASE: Joubert syndrome 35 (JBTS35) [MIM:618161]: A form of Joubert
CC syndrome, a disorder presenting with cerebellar ataxia, oculomotor
CC apraxia, hypotonia, neonatal breathing abnormalities and psychomotor
CC delay. Neuroradiologically, it is characterized by cerebellar vermian
CC hypoplasia/aplasia, thickened and reoriented superior cerebellar
CC peduncles, and an abnormally large interpeduncular fossa, giving the
CC appearance of a molar tooth on transaxial slices (molar tooth sign).
CC Additional variable features include retinal dystrophy, renal disease,
CC liver fibrosis, and polydactyly. JBTS35 inheritance is autosomal
CC recessive. {ECO:0000269|PubMed:30269812}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Retinitis pigmentosa 83 (RP83) [MIM:618173]: An autosomal
CC dominant form of retinitis pigmentosa, a retinal dystrophy belonging to
CC the group of pigmentary retinopathies. Retinitis pigmentosa is
CC characterized by retinal pigment deposits visible on fundus examination
CC and primary loss of rod photoreceptor cells followed by secondary loss
CC of cone photoreceptors. Patients typically have night vision blindness
CC and loss of midperipheral visual field. As their condition progresses,
CC they lose their far peripheral visual field and eventually central
CC vision as well. {ECO:0000269|PubMed:26964041}. Note=The disease may be
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; U07151; AAA21654.1; -; mRNA.
DR EMBL; AF493889; AAM12603.1; -; mRNA.
DR EMBL; AK312525; BAG35424.1; -; mRNA.
DR EMBL; CR407637; CAG28565.1; -; mRNA.
DR EMBL; AL391121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009841; AAH09841.1; -; mRNA.
DR CCDS; CCDS7538.1; -.
DR PIR; A54869; A54869.
DR RefSeq; NP_004302.1; NM_004311.3.
DR RefSeq; XP_016871749.1; XM_017016260.1.
DR AlphaFoldDB; P36405; -.
DR SMR; P36405; -.
DR BioGRID; 106896; 28.
DR DIP; DIP-47537N; -.
DR IntAct; P36405; 29.
DR MINT; P36405; -.
DR STRING; 9606.ENSP00000260746; -.
DR DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR GlyGen; P36405; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P36405; -.
DR PhosphoSitePlus; P36405; -.
DR BioMuta; ARL3; -.
DR DMDM; 543851; -.
DR REPRODUCTION-2DPAGE; IPI00003327; -.
DR UCD-2DPAGE; P36405; -.
DR EPD; P36405; -.
DR jPOST; P36405; -.
DR MassIVE; P36405; -.
DR MaxQB; P36405; -.
DR PaxDb; P36405; -.
DR PeptideAtlas; P36405; -.
DR PRIDE; P36405; -.
DR ProteomicsDB; 55199; -.
DR Antibodypedia; 31479; 430 antibodies from 29 providers.
DR DNASU; 403; -.
DR Ensembl; ENST00000260746.6; ENSP00000260746.4; ENSG00000138175.9.
DR GeneID; 403; -.
DR KEGG; hsa:403; -.
DR MANE-Select; ENST00000260746.6; ENSP00000260746.4; NM_004311.4; NP_004302.1.
DR UCSC; uc001kwa.4; human.
DR CTD; 403; -.
DR DisGeNET; 403; -.
DR GeneCards; ARL3; -.
DR HGNC; HGNC:694; ARL3.
DR HPA; ENSG00000138175; Tissue enhanced (retina).
DR MalaCards; ARL3; -.
DR MIM; 604695; gene.
DR MIM; 618161; phenotype.
DR MIM; 618173; phenotype.
DR neXtProt; NX_P36405; -.
DR OpenTargets; ENSG00000138175; -.
DR Orphanet; 475; Joubert syndrome.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA24987; -.
DR VEuPathDB; HostDB:ENSG00000138175; -.
DR eggNOG; KOG0074; Eukaryota.
DR GeneTree; ENSGT00940000155737; -.
DR HOGENOM; CLU_040729_12_0_1; -.
DR InParanoid; P36405; -.
DR OMA; ASEDITQ; -.
DR OrthoDB; 1271528at2759; -.
DR PhylomeDB; P36405; -.
DR TreeFam; TF105463; -.
DR PathwayCommons; P36405; -.
DR Reactome; R-HSA-5624138; Trafficking of myristoylated proteins to the cilium.
DR SignaLink; P36405; -.
DR BioGRID-ORCS; 403; 24 hits in 1088 CRISPR screens.
DR ChiTaRS; ARL3; human.
DR GeneWiki; ARL3; -.
DR GenomeRNAi; 403; -.
DR Pharos; P36405; Tbio.
DR PRO; PR:P36405; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P36405; protein.
DR Bgee; ENSG00000138175; Expressed in bronchial epithelial cell and 212 other tissues.
DR Genevisible; P36405; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0032794; F:GTPase activating protein binding; IEA:Ensembl.
DR GO; GO:0003924; F:GTPase activity; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; ISS:UniProtKB.
DR GO; GO:0042073; P:intraciliary transport; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; ISS:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
DR GO; GO:0042461; P:photoreceptor cell development; ISS:UniProtKB.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IMP:MGI.
DR GO; GO:1903441; P:protein localization to ciliary membrane; ISS:UniProtKB.
DR GO; GO:0061512; P:protein localization to cilium; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:UniProtKB.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR044612; ARL2/3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR PANTHER; PTHR45697; PTHR45697; 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 Cell cycle; Cell division; Cell projection; Ciliopathy; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Disease variant; Golgi apparatus;
KW GTP-binding; Joubert syndrome; Lipoprotein; Magnesium; Membrane;
KW Metal-binding; Myristate; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..182
FT /note="ADP-ribosylation factor-like protein 3"
FT /id="PRO_0000207456"
FT BINDING 24..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 31
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 67..71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 159..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT VARIANT 34
FT /note="L -> M (in dbSNP:rs1141895)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_014869"
FT VARIANT 90
FT /note="Y -> C (in RP83; unknown pathological significance;
FT dbSNP:rs1564730440)"
FT /evidence="ECO:0000269|PubMed:26964041"
FT /id="VAR_081340"
FT VARIANT 149
FT /note="R -> C (in JBTS35; dbSNP:rs776901858)"
FT /evidence="ECO:0000269|PubMed:30269812"
FT /id="VAR_081202"
FT VARIANT 149
FT /note="R -> H (in JBTS35; decreased release of NPHP3 and
FT INPP5E cargos to the cilium; dbSNP:rs770782663)"
FT /evidence="ECO:0000269|PubMed:30269812"
FT /id="VAR_081203"
FT MUTAGEN 31
FT /note="T->N: Enhances the interaction with RP2."
FT /evidence="ECO:0000269|PubMed:11847227,
FT ECO:0000269|PubMed:22085962"
FT MUTAGEN 71
FT /note="Q->L: Enhances the interaction with RP2. Does not
FT induce a mitotic arrest resulting from the loss of the
FT microtubule-based mitotic spindle. Induces release of
FT myristoylated proteins from UNC119. Interacts with ARL2BP,
FT GOLGA4, PDE6D and UNC119."
FT /evidence="ECO:0000269|PubMed:11303027,
FT ECO:0000269|PubMed:11847227, ECO:0000269|PubMed:16525022,
FT ECO:0000269|PubMed:22085962"
SQ SEQUENCE 182 AA; 20456 MW; E5C1ACAD0BD55537 CRC64;
MGLLSILRKL KSAPDQEVRI LLLGLDNAGK TTLLKQLASE DISHITPTQG FNIKSVQSQG
FKLNVWDIGG QRKIRPYWKN YFENTDILIY VIDSADRKRF EETGQELAEL LEEEKLSCVP
VLIFANKQDL LTAAPASEIA EGLNLHTIRD RVWQIQSCSA LTGEGVQDGM NWVCKNVNAK
KK
