ARL2_HUMAN
ID ARL2_HUMAN Reviewed; 184 AA.
AC P36404; G3V184; Q9BUK8;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 4.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=ADP-ribosylation factor-like protein 2;
GN Name=ARL2;
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] (ISOFORM 1), AND VARIANT ALA-141.
RX PubMed=8415637; DOI=10.1073/pnas.90.19.8952;
RA Clark J., Moore L., Krasinskas A., Way J., Battey J.F., Tamkun J.W.,
RA Kahn R.A.;
RT "Selective amplification of additional members of the ADP-ribosylation
RT factor (ARF) family: cloning of additional human and Drosophila ARF-like
RT genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:8952-8956(1993).
RN [2]
RP SEQUENCE REVISION TO 11.
RA Kahn R.A.;
RL Submitted (NOV-1997) to UniProtKB.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-141.
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT ALA-141.
RX PubMed=15146197; DOI=10.1038/nbt971;
RA Brandenberger R., Wei H., Zhang S., Lei S., Murage J., Fisk G.J., Li Y.,
RA Xu C., Fang R., Guegler K., Rao M.S., Mandalam R., Lebkowski J.,
RA Stanton L.W.;
RT "Transcriptome characterization elucidates signaling networks that control
RT human ES cell growth and differentiation.";
RL Nat. Biotechnol. 22:707-716(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [8]
RP INTERACTION WITH ARL2BP.
RX PubMed=10488091; DOI=10.1074/jbc.274.39.27553;
RA Sharer J.D., Kahn R.A.;
RT "The ARF-like 2 (ARL2)-binding protein, BART. Purification, cloning, and
RT initial characterization.";
RL J. Biol. Chem. 274:27553-27561(1999).
RN [9]
RP FUNCTION, INTERACTION WITH TBCD, AND MUTAGENESIS OF THR-30; THR-47; PHE-50
RP AND GLN-70.
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 [10]
RP INTERACTION WITH ARL2BP AND PDE6D, AND MUTAGENESIS OF GLN-70.
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 [11]
RP INTERACTION WITH ARL2BP.
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 SUBCELLULAR LOCATION, AND LACK OF N-MYRISTOYLATION.
RX PubMed=11809823; DOI=10.1091/mbc.01-05-0245;
RA Sharer J.D., Shern J.F., Van Valkenburgh H., Wallace D.C., Kahn R.A.;
RT "ARL2 and BART enter mitochondria and bind the adenine nucleotide
RT transporter.";
RL Mol. Biol. Cell 13:71-83(2002).
RN [13]
RP FUNCTION, MUTAGENESIS OF GLN-70, AND SUBCELLULAR LOCATION.
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 ELMOD2.
RX PubMed=17452337; DOI=10.1074/jbc.m701347200;
RA Bowzard J.B., Cheng D., Peng J., Kahn R.A.;
RT "ELMOD2 is an Arl2 GTPase-activating protein that also acts on Arfs.";
RL J. Biol. Chem. 282:17568-17580(2007).
RN [15]
RP FUNCTION, AND GTP/GDP BINDING.
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 FUNCTION, INTERACTION WITH ARL2BP, MUTAGENESIS OF THR-30 AND GLN-70, AND
RP SUBCELLULAR LOCATION.
RX PubMed=18234692; DOI=10.1093/intimm/dxm154;
RA Muromoto R., Sekine Y., Imoto S., Ikeda O., Okayama T., Sato N.,
RA Matsuda T.;
RT "BART is essential for nuclear retention of STAT3.";
RL Int. Immunol. 20:395-403(2008).
RN [17]
RP INTERACTION WITH ARL2BP.
RX PubMed=18981177; DOI=10.1074/jbc.m806167200;
RA Bailey L.K., Campbell L.J., Evetts K.A., Littlefield K., Rajendra E.,
RA Nietlispach D., Owen D., Mott H.R.;
RT "The structure of binder of Arl2 (BART) reveals a novel G protein binding
RT domain: implications for function.";
RL J. Biol. Chem. 284:992-999(2009).
RN [18]
RP FUNCTION.
RX PubMed=20740604; DOI=10.1002/cm.20480;
RA Tian G., Thomas S., Cowan N.J.;
RT "Effect of TBCD and its regulatory interactor Arl2 on tubulin and
RT microtubule integrity.";
RL Cytoskeleton 67:706-714(2010).
RN [19]
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 [20]
RP INTERACTION WITH TBCD.
RX PubMed=27666374; DOI=10.1016/j.ajhg.2016.08.005;
RA Miyake N., Fukai R., Ohba C., Chihara T., Miura M., Shimizu H., Kakita A.,
RA Imagawa E., Shiina M., Ogata K., Okuno-Yuguchi J., Fueki N., Ogiso Y.,
RA Suzumura H., Watabe Y., Imataka G., Leong H.Y., Fattal-Valevski A.,
RA Kramer U., Miyatake S., Kato M., Okamoto N., Sato Y., Mitsuhashi S.,
RA Nishino I., Kaneko N., Nishiyama A., Tamura T., Mizuguchi T., Nakashima M.,
RA Tanaka F., Saitsu H., Matsumoto N.;
RT "Biallelic TBCD mutations cause early-onset neurodegenerative
RT encephalopathy.";
RL Am. J. Hum. Genet. 99:950-961(2016).
RN [21]
RP INVOLVEMENT IN MRCS1, VARIANT MRCS1 LEU-15, CHARACTERIZATION OF VARIANT
RP MRCS1 LEU-15, FUNCTION, INTERACTION WITH UNC119, INTERACTION WITH ARL2BP,
RP AND SUBCELLULAR LOCATION.
RX PubMed=30945270; DOI=10.1111/cge.13541;
RA Cai X.B., Wu K.C., Zhang X., Lv J.N., Jin G.H., Xiang L., Chen J.,
RA Huang X.F., Pan D., Lu B., Lu F., Qu J., Jin Z.B.;
RT "Whole-exome sequencing identified ARL2 as a novel candidate gene for MRCS
RT (microcornea, rod-cone dystrophy, cataract, and posterior staphyloma)
RT syndrome.";
RL Clin. Genet. 96:61-71(2019).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-184 IN A COMPLEX WITH ARL2BP;
RP GTP AND MAGNESIUM IONS, INTERACTION WITH ARL2BP, AND MUTAGENESIS OF LEU-3;
RP LEU-4; ILE-6; LEU-7; PHE-50; TYR-76 AND TYR-80.
RX PubMed=19368893; DOI=10.1016/j.str.2009.01.014;
RA Zhang T., Li S., Zhang Y., Zhong C., Lai Z., Ding J.;
RT "Crystal structure of the ARL2-GTP-BART complex reveals a novel recognition
RT and binding mode of small GTPase with effector.";
RL Structure 17:602-610(2009).
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). GTP-binding protein that does not act as an
CC allosteric activator of the cholera toxin catalytic subunit. Regulates
CC formation of new microtubules and centrosome integrity. Prevents the
CC TBCD-induced microtubule destruction. Participates in association with
CC TBCD, in the disassembly of the apical junction complexes. Antagonizes
CC the effect of TBCD on epithelial cell detachment and tight and adherens
CC junctions disassembly. Together with ARL2, plays a role in the nuclear
CC translocation, retention and transcriptional activity of STAT3.
CC Component of a regulated secretory pathway involved in Ca(2+)-dependent
CC release of acetylcholine. Required for normal progress through the cell
CC cycle (PubMed:10831612, PubMed:16525022, PubMed:18234692,
CC PubMed:18588884, PubMed:20740604). Also regulates mitochondrial
CC integrity and function (PubMed:30945270). {ECO:0000269|PubMed:10831612,
CC ECO:0000269|PubMed:16525022, ECO:0000269|PubMed:18234692,
CC ECO:0000269|PubMed:18588884, ECO:0000269|PubMed:20740604,
CC ECO:0000269|PubMed:30945270}.
CC -!- SUBUNIT: Found in a complex with ARL2, ARL2BP and SLC25A6
CC (PubMed:30945270). Found in a complex with at least ARL2, PPP2CB,
CC PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Found in a complex with ARL2,
CC ARL2BP and SLC25A4. The GTP-bound form interacts with PDE6D. Interacts
CC with ELMOD2. The GTP-bound form interacts with ARL2BP. Interacts,
CC preferentially in its GDP-bound state, with TBCD (PubMed:10488091,
CC PubMed:10831612, PubMed:11303027, PubMed:11847227, PubMed:17452337,
CC PubMed:18234692, PubMed:18981177, PubMed:19368893, PubMed:27666374).
CC Interacts with UNC119. {ECO:0000269|PubMed:10488091,
CC ECO:0000269|PubMed:10831612, ECO:0000269|PubMed:11303027,
CC ECO:0000269|PubMed:11847227, ECO:0000269|PubMed:17452337,
CC ECO:0000269|PubMed:18234692, ECO:0000269|PubMed:18981177,
CC ECO:0000269|PubMed:19368893, ECO:0000269|PubMed:27666374,
CC ECO:0000269|PubMed:30945270}.
CC -!- INTERACTION:
CC P36404; Q9Y2Y0: ARL2BP; NbExp=24; IntAct=EBI-752365, EBI-3449344;
CC P36404; Q969G2: LHX4; NbExp=3; IntAct=EBI-752365, EBI-2865388;
CC P36404; O43924: PDE6D; NbExp=18; IntAct=EBI-752365, EBI-712685;
CC P36404; Q9BZK7: TBL1XR1; NbExp=4; IntAct=EBI-752365, EBI-765729;
CC P36404; Q13432: UNC119; NbExp=11; IntAct=EBI-752365, EBI-711260;
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000305|PubMed:30945270}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Nucleus. Cytoplasm. Note=The complex
CC formed with ARL2BP, ARL2 and SLC25A6 is expressed in mitochondria. The
CC complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in
CC mitochondria (By similarity). Not detected in the Golgi, nucleus and on
CC the mitotic spindle. Centrosome-associated throughout the cell cycle.
CC Not detected to interphase microtubules.
CC {ECO:0000250|UniProtKB:O08697}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P36404-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P36404-2; Sequence=VSP_047278;
CC -!- PTM: Not N-myristoylated.
CC -!- DISEASE: Microcornea, rod-cone dystrophy, cataract, and posterior
CC staphyloma 1 (MRCS1) [MIM:619082]: An autosomal dominant ocular
CC disorder characterized by poor visual acuity in early childhood, due to
CC congenital cataract and microcornea followed by rod-cone dystrophy,
CC with later development of posterior staphyloma.
CC {ECO:0000269|PubMed:30945270}. Note=The disease is caused by variants
CC 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; L13687; AAC37606.1; -; mRNA.
DR EMBL; AF493888; AAM12602.1; -; mRNA.
DR EMBL; CN338497; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AP000436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW74333.1; -; Genomic_DNA.
DR EMBL; BC002530; AAH02530.1; -; mRNA.
DR CCDS; CCDS55770.1; -. [P36404-2]
DR CCDS; CCDS8088.1; -. [P36404-1]
DR PIR; A48259; A48259.
DR RefSeq; NP_001186674.1; NM_001199745.1. [P36404-2]
DR RefSeq; NP_001658.2; NM_001667.3. [P36404-1]
DR PDB; 3DOE; X-ray; 2.25 A; A=1-184.
DR PDB; 3DOF; X-ray; 3.30 A; A=1-184.
DR PDBsum; 3DOE; -.
DR PDBsum; 3DOF; -.
DR AlphaFoldDB; P36404; -.
DR SMR; P36404; -.
DR BioGRID; 106895; 99.
DR CORUM; P36404; -.
DR DIP; DIP-47535N; -.
DR IntAct; P36404; 28.
DR MINT; P36404; -.
DR STRING; 9606.ENSP00000246747; -.
DR ChEMBL; CHEMBL4295751; -.
DR DrugBank; DB14731; Tagraxofusp.
DR iPTMnet; P36404; -.
DR PhosphoSitePlus; P36404; -.
DR BioMuta; ARL2; -.
DR DMDM; 116241255; -.
DR EPD; P36404; -.
DR jPOST; P36404; -.
DR MassIVE; P36404; -.
DR MaxQB; P36404; -.
DR PaxDb; P36404; -.
DR PeptideAtlas; P36404; -.
DR PRIDE; P36404; -.
DR ProteomicsDB; 32289; -.
DR ProteomicsDB; 55198; -. [P36404-1]
DR Antibodypedia; 29583; 373 antibodies from 31 providers.
DR DNASU; 402; -.
DR Ensembl; ENST00000246747.9; ENSP00000246747.4; ENSG00000213465.8. [P36404-1]
DR Ensembl; ENST00000529384.5; ENSP00000436021.1; ENSG00000213465.8. [P36404-1]
DR Ensembl; ENST00000533729.1; ENSP00000432971.1; ENSG00000213465.8. [P36404-2]
DR GeneID; 402; -.
DR KEGG; hsa:402; -.
DR MANE-Select; ENST00000246747.9; ENSP00000246747.4; NM_001667.4; NP_001658.2.
DR UCSC; uc021qlc.2; human. [P36404-1]
DR CTD; 402; -.
DR DisGeNET; 402; -.
DR GeneCards; ARL2; -.
DR HGNC; HGNC:693; ARL2.
DR HPA; ENSG00000213465; Low tissue specificity.
DR MalaCards; ARL2; -.
DR MIM; 601175; gene.
DR MIM; 619082; phenotype.
DR neXtProt; NX_P36404; -.
DR OpenTargets; ENSG00000213465; -.
DR PharmGKB; PA24986; -.
DR VEuPathDB; HostDB:ENSG00000213465; -.
DR eggNOG; KOG0073; Eukaryota.
DR GeneTree; ENSGT00940000157941; -.
DR HOGENOM; CLU_040729_12_3_1; -.
DR InParanoid; P36404; -.
DR OMA; TTCVKKF; -.
DR PhylomeDB; P36404; -.
DR TreeFam; TF105462; -.
DR BRENDA; 3.6.5.2; 2681.
DR PathwayCommons; P36404; -.
DR Reactome; R-HSA-389977; Post-chaperonin tubulin folding pathway.
DR Reactome; R-HSA-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR Reactome; R-HSA-9648002; RAS processing.
DR SignaLink; P36404; -.
DR BioGRID-ORCS; 402; 778 hits in 1073 CRISPR screens.
DR EvolutionaryTrace; P36404; -.
DR GeneWiki; ARL2; -.
DR GenomeRNAi; 402; -.
DR Pharos; P36404; Tbio.
DR PRO; PR:P36404; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P36404; protein.
DR Bgee; ENSG00000213465; Expressed in C1 segment of cervical spinal cord and 193 other tissues.
DR ExpressionAtlas; P36404; baseline and differential.
DR Genevisible; P36404; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019003; F:GDP binding; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IMP:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IMP:UniProtKB.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISS:UniProtKB.
DR GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; IDA:UniProtKB.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISS:UniProtKB.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:1903715; P:regulation of aerobic respiration; IMP:UniProtKB.
DR GO; GO:0006110; P:regulation of glycolytic process; IMP:UniProtKB.
DR GO; GO:0031113; P:regulation of microtubule polymerization; IMP:UniProtKB.
DR CDD; cd04154; Arl2; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR045873; Arl2.
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 3D-structure; Alternative splicing; Cataract; Cell cycle; Cytoplasm;
KW Cytoskeleton; Disease variant; GTP-binding; Isopeptide bond; Lipoprotein;
KW Mitochondrion; Myristate; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..184
FT /note="ADP-ribosylation factor-like protein 2"
FT /id="PRO_0000207453"
FT BINDING 23..30
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 66..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 125..128
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0J4"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT CROSSLNK 71
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT VAR_SEQ 113..139
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15146197"
FT /id="VSP_047278"
FT VARIANT 15
FT /note="R -> L (in MRCS1; decreased interaction with UNC119;
FT decreased interaction with ARL2BP; changed cellular
FT respiration; decreased ATP production)"
FT /evidence="ECO:0000269|PubMed:30945270"
FT /id="VAR_085165"
FT VARIANT 141
FT /note="V -> A (in dbSNP:rs664226)"
FT /evidence="ECO:0000269|PubMed:15146197,
FT ECO:0000269|PubMed:8415637, ECO:0000269|Ref.3"
FT /id="VAR_028056"
FT MUTAGEN 3
FT /note="L->A: Reduces interaction with ARL2BP."
FT /evidence="ECO:0000269|PubMed:19368893"
FT MUTAGEN 3
FT /note="L->D: Reduces interaction with ARL2BP."
FT /evidence="ECO:0000269|PubMed:19368893"
FT MUTAGEN 4
FT /note="L->A: Does not reduce interaction with ARL2BP."
FT /evidence="ECO:0000269|PubMed:19368893"
FT MUTAGEN 4
FT /note="L->D: Reduces interaction with ARL2BP."
FT /evidence="ECO:0000269|PubMed:19368893"
FT MUTAGEN 6
FT /note="I->R: Reduces interaction with ARL2BP."
FT /evidence="ECO:0000269|PubMed:19368893"
FT MUTAGEN 7
FT /note="L->A: Does not reduce interaction with ARL2BP."
FT /evidence="ECO:0000269|PubMed:19368893"
FT MUTAGEN 7
FT /note="L->D: Reduces interaction with ARL2BP."
FT /evidence="ECO:0000269|PubMed:19368893"
FT MUTAGEN 30
FT /note="T->N: Does not inhibit the interaction with TBCD and
FT rescues the TBCD-induced microtubule destruction. Reduces
FT interaction with ARL2BP. Inhibits accumulation of STAT3 in
FT the nucleus."
FT /evidence="ECO:0000269|PubMed:10831612,
FT ECO:0000269|PubMed:18234692"
FT MUTAGEN 47
FT /note="T->A: Does not inhibit the interaction with TBCD and
FT rescues the TBCD-induced microtubule destruction."
FT /evidence="ECO:0000269|PubMed:10831612"
FT MUTAGEN 50
FT /note="F->A: Reduces interaction with ARL2BP. Inhibits the
FT interaction with TBCD and rescues the TBCD-induced
FT microtubule destruction."
FT /evidence="ECO:0000269|PubMed:10831612,
FT ECO:0000269|PubMed:19368893"
FT MUTAGEN 70
FT /note="Q->L: Induces cell cycle arrest, reduces ability to
FT form microtubules and centrosome fragmentation. Inhibits
FT the interaction with TBCD and does not rescue the TBCD-
FT induced microtubule destruction. Interacts with ARL2BP and
FT PDE6D."
FT /evidence="ECO:0000269|PubMed:10831612,
FT ECO:0000269|PubMed:11303027, ECO:0000269|PubMed:16525022,
FT ECO:0000269|PubMed:18234692"
FT MUTAGEN 76
FT /note="Y->A: Does not reduce interaction with ARL2BP."
FT /evidence="ECO:0000269|PubMed:19368893"
FT MUTAGEN 80
FT /note="Y->A: Reduces interaction with ARL2BP."
FT /evidence="ECO:0000269|PubMed:19368893"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:3DOE"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:3DOE"
FT HELIX 29..37
FT /evidence="ECO:0007829|PDB:3DOE"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:3DOE"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:3DOE"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:3DOE"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:3DOE"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:3DOE"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:3DOE"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:3DOE"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:3DOE"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:3DOE"
FT HELIX 141..146
FT /evidence="ECO:0007829|PDB:3DOE"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:3DOE"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:3DOE"
FT HELIX 165..184
FT /evidence="ECO:0007829|PDB:3DOE"
SQ SEQUENCE 184 AA; 20878 MW; 0823F005719C17F9 CRC64;
MGLLTILKKM KQKERELRLL MLGLDNAGKT TILKKFNGED IDTISPTLGF NIKTLEHRGF
KLNIWDVGGQ KSLRSYWRNY FESTDGLIWV VDSADRQRMQ DCQRELQSLL VEERLAGATL
LIFANKQDLP GALSSNAIRE VLELDSIRSH HWCIQGCSAV TGENLLPGID WLLDDISSRI
FTAD
