ARL2_MOUSE
ID ARL2_MOUSE Reviewed; 184 AA.
AC Q9D0J4; Q9WUM1;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=ADP-ribosylation factor-like protein 2;
GN Name=Arl2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Linari M., Hanzal-Bayer M., Becker J.;
RT "Identification of Mus musculus arf like protein 2 (ARL2).";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP IDENTIFICATION IN A COMPLEX WITH SLC25A4 AND ARL2BP, AND TISSUE
RP SPECIFICITY.
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 [5]
RP INTERACTION WITH PDE6D, GTP/GDP-BINDING, AND MUTAGENESIS OF THR-30 AND
RP GLN-70.
RX PubMed=15979089; DOI=10.1016/j.jmb.2005.05.036;
RA Hanzal-Bayer M., Linari M., Wittinghofer A.;
RT "Properties of the interaction of Arf-like protein 2 with PDEdelta.";
RL J. Mol. Biol. 350:1074-1082(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH HUMAN PDE6D AND GTP.
RX PubMed=11980706; DOI=10.1093/emboj/21.9.2095;
RA Hanzal-Bayer M., Renault L., Roversi P., Wittinghofer A., Hillig R.C.;
RT "The complex of Arl2-GTP and PDE delta: from structure to function.";
RL EMBO J. 21:2095-2106(2002).
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.
CC -!- SUBUNIT: Found in a complex with ARL2, ARL2BP and SLC25A6. Found in a
CC complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD.
CC Interacts with ELMOD2. The GTP-bound form interacts with ARL2BP.
CC Interacts with TBCD; the GDP-bound form interacts preferentially with
CC TBCD. Interacts with UNC119 (By similarity). Found in a complex with
CC ARL2, ARL2BP and SLC25A4. The GTP-bound form interacts with PDE6D.
CC {ECO:0000250, ECO:0000269|PubMed:11809823, ECO:0000269|PubMed:11980706,
CC ECO:0000269|PubMed:15979089}.
CC -!- INTERACTION:
CC Q9D0J4; O43924: PDE6D; Xeno; NbExp=6; IntAct=EBI-1033319, EBI-712685;
CC Q9D0J4; Q13432: UNC119; Xeno; NbExp=2; IntAct=EBI-1033319, EBI-711260;
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome. Nucleus.
CC Cytoplasm. Note=The complex formed with ARL2BP, ARL2 and SLC25A6 is
CC expressed in mitochondria. Not detected in the Golgi, nucleus and on
CC the mitotic spindle. Centrosome-associated throughout the cell cycle.
CC Not detected to interphase microtubules (By similarity). The complex
CC formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, lung, cerebellum, liver,
CC kidney, hippocampus, spleen, cortex and heart (at protein level).
CC {ECO:0000269|PubMed:11809823}.
CC -!- PTM: Not N-myristoylated.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; AF143680; AAD33908.1; -; mRNA.
DR EMBL; AK011366; BAB27572.1; -; mRNA.
DR EMBL; BC060259; AAH60259.1; -; mRNA.
DR CCDS; CCDS29496.1; -.
DR RefSeq; NP_062696.2; NM_019722.3.
DR PDB; 1KSG; X-ray; 2.30 A; A=1-184.
DR PDB; 1KSH; X-ray; 1.80 A; A=1-184.
DR PDB; 1KSJ; X-ray; 2.60 A; A=1-184.
DR PDB; 4GOK; X-ray; 2.60 A; A/B=17-184.
DR PDBsum; 1KSG; -.
DR PDBsum; 1KSH; -.
DR PDBsum; 1KSJ; -.
DR PDBsum; 4GOK; -.
DR AlphaFoldDB; Q9D0J4; -.
DR SMR; Q9D0J4; -.
DR BioGRID; 207906; 7.
DR DIP; DIP-36659N; -.
DR IntAct; Q9D0J4; 9.
DR MINT; Q9D0J4; -.
DR STRING; 10090.ENSMUSP00000025893; -.
DR iPTMnet; Q9D0J4; -.
DR PhosphoSitePlus; Q9D0J4; -.
DR EPD; Q9D0J4; -.
DR jPOST; Q9D0J4; -.
DR MaxQB; Q9D0J4; -.
DR PaxDb; Q9D0J4; -.
DR PeptideAtlas; Q9D0J4; -.
DR PRIDE; Q9D0J4; -.
DR ProteomicsDB; 282019; -.
DR Antibodypedia; 29583; 373 antibodies from 31 providers.
DR DNASU; 56327; -.
DR Ensembl; ENSMUST00000025893; ENSMUSP00000025893; ENSMUSG00000024944.
DR GeneID; 56327; -.
DR KEGG; mmu:56327; -.
DR UCSC; uc008gho.1; mouse.
DR CTD; 402; -.
DR MGI; MGI:1928393; Arl2.
DR VEuPathDB; HostDB:ENSMUSG00000024944; -.
DR eggNOG; KOG0073; Eukaryota.
DR GeneTree; ENSGT00940000157941; -.
DR HOGENOM; CLU_040729_12_3_1; -.
DR InParanoid; Q9D0J4; -.
DR OMA; EHRGYKL; -.
DR OrthoDB; 1271528at2759; -.
DR PhylomeDB; Q9D0J4; -.
DR TreeFam; TF105462; -.
DR Reactome; R-MMU-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR Reactome; R-MMU-9648002; RAS processing.
DR BioGRID-ORCS; 56327; 28 hits in 76 CRISPR screens.
DR ChiTaRS; Arl2; mouse.
DR EvolutionaryTrace; Q9D0J4; -.
DR PRO; PR:Q9D0J4; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9D0J4; protein.
DR Bgee; ENSMUSG00000024944; Expressed in embryonic brain and 254 other tissues.
DR Genevisible; Q9D0J4; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0015870; P:acetylcholine transport; ISO:MGI.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISS:UniProtKB.
DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; ISS:UniProtKB.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISS:UniProtKB.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:1903715; P:regulation of aerobic respiration; ISS:UniProtKB.
DR GO; GO:0006110; P:regulation of glycolytic process; ISS:UniProtKB.
DR GO; GO:0031113; P:regulation of microtubule polymerization; ISS: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; Cell cycle; Cytoplasm; Cytoskeleton; GTP-binding;
KW Isopeptide bond; Lipoprotein; Mitochondrion; Myristate; Nucleotide-binding;
KW Nucleus; Phosphoprotein; 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_0000207454"
FT BINDING 23..30
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:11980706"
FT BINDING 66..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:11980706"
FT BINDING 68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:11980706"
FT BINDING 125..128
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:11980706"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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 /evidence="ECO:0000250|UniProtKB:P36404"
FT MUTAGEN 30
FT /note="T->L: Reduces affinity to GTP and GDP. Inhibits
FT interaction with PDE6D."
FT /evidence="ECO:0000269|PubMed:15979089"
FT MUTAGEN 70
FT /note="Q->L: Does not reduce affinity fo GTP and GDP.
FT Enhances interaction with PDE6D."
FT /evidence="ECO:0000269|PubMed:15979089"
FT CONFLICT 33
FT /note="L -> S (in Ref. 1; AAD33908)"
FT /evidence="ECO:0000305"
FT HELIX 2..12
FT /evidence="ECO:0007829|PDB:1KSG"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:1KSH"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:1KSH"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:1KSH"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:1KSH"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:1KSH"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:1KSH"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:1KSH"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1KSH"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:1KSH"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:1KSH"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:1KSH"
FT HELIX 135..141
FT /evidence="ECO:0007829|PDB:1KSH"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1KSH"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:1KSH"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:1KSH"
FT HELIX 165..177
FT /evidence="ECO:0007829|PDB:1KSH"
SQ SEQUENCE 184 AA; 20864 MW; 8B3741700BFED3F8 CRC64;
MGLLTILKKM KQKERELRLL MLGLDNAGKT TILKKFNGED VDTISPTLGF NIKTLEHRGF
KLNIWDVGGQ KSLRSYWRNY FESTDGLIWV VDSADRQRMQ DCQRELQSLL VEERLAGATL
LIFANKQDLP GALSCNAIQE ALELDSIRSH HWRIQGCSAV TGEDLLPGID WLLDDISSRV
FTAD
