ARL2_RAT
ID ARL2_RAT Reviewed; 184 AA.
AC O08697;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=ADP-ribosylation factor-like protein 2;
GN Name=Arl2; Synonyms=Arl184;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=9208929; DOI=10.1111/j.1432-1033.1997.00388.x;
RA Icard-Liepkalns C., Ravassard P., Liepkalns V.A., Chatail F., Mallet J.;
RT "An ADP-ribosylation-factor(ARF)-like protein involved in regulated
RT secretion.";
RL Eur. J. Biochem. 246:388-393(1997).
RN [2]
RP SUBCELLULAR LOCATION, AND TISSUE 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 [3]
RP INTERACTION WITH UNC119, AND TISSUE SPECIFICITY.
RX PubMed=12527357; DOI=10.1016/s0014-5793(02)03766-3;
RA Kobayashi A., Kubota S., Mori N., McLaren M.J., Inana G.;
RT "Photoreceptor synaptic protein HRG4 (UNC119) interacts with ARL2 via a
RT putative conserved domain.";
RL FEBS Lett. 534:26-32(2003).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=12912990; DOI=10.1074/jbc.m308678200;
RA Shern J.F., Sharer J.D., Pallas D.C., Bartolini F., Cowan N.J., Reed M.S.,
RA Pohl J., Kahn R.A.;
RT "Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A.";
RL J. Biol. Chem. 278:40829-40836(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity). {ECO:0000250}.
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. The
CC GDP-bound form interacts preferentially with TBCD. Interacts with
CC UNC119. Found in a complex with ARL2, ARL2BP and SLC25A4. The GTP-bound
CC form interacts with PDE6D (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:11809823}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:11809823}. Nucleus
CC {ECO:0000269|PubMed:11809823}. Cytoplasm {ECO:0000269|PubMed:11809823}.
CC Note=The complex formed with ARL2BP, ARL2 and SLC25A6 is expressed in
CC mitochondria. Not detected in the Golgi, nucleus and on the mitotic
CC spindle. Centrosome-associated throughout the cell cycle. Not detected
CC to interphase microtubules. The complex formed with ARL2BP, ARL2 and
CC SLC25A4 is expressed in mitochondria (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, retina, lung, cerebellum,
CC liver, kidney, hippocampus, spleen, cortex and heart (at protein
CC level). {ECO:0000269|PubMed:11809823, ECO:0000269|PubMed:12527357,
CC ECO:0000269|PubMed:12912990}.
CC -!- PTM: Not N-myristoylated.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; Y12708; CAA73245.1; -; mRNA.
DR RefSeq; NP_113899.1; NM_031711.1.
DR AlphaFoldDB; O08697; -.
DR SMR; O08697; -.
DR BioGRID; 249263; 1.
DR IntAct; O08697; 4.
DR STRING; 10116.ENSRNOP00000028525; -.
DR iPTMnet; O08697; -.
DR PhosphoSitePlus; O08697; -.
DR jPOST; O08697; -.
DR PaxDb; O08697; -.
DR PRIDE; O08697; -.
DR GeneID; 65142; -.
DR KEGG; rno:65142; -.
DR UCSC; RGD:69326; rat.
DR CTD; 402; -.
DR RGD; 69326; Arl2.
DR eggNOG; KOG0073; Eukaryota.
DR InParanoid; O08697; -.
DR OrthoDB; 1271528at2759; -.
DR PhylomeDB; O08697; -.
DR Reactome; R-RNO-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR Reactome; R-RNO-9648002; RAS processing.
DR PRO; PR:O08697; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
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:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019003; F:GDP binding; ISO:RGD.
DR GO; GO:0005525; F:GTP binding; ISO:RGD.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0015870; P:acetylcholine transport; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0006110; P:regulation of glycolytic process; ISO:RGD.
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 Cell cycle; Cytoplasm; Cytoskeleton; GTP-binding; Isopeptide bond;
KW Lipoprotein; Mitochondrion; Myristate; Nucleotide-binding; Nucleus;
KW 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_0000207455"
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:0007744|PubMed:22673903"
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"
SQ SEQUENCE 184 AA; 20836 MW; 96993CCBECF6EE53 CRC64;
MGLLTILKKM KQKERDVRLL MLGLDNAGKT TILKKFNGED VDTISPTLGF NIKTLEHRGF
KLNIWDVGGQ KSLRSYWRNY FESTDGLIWV VDSADRQRMQ DCQRELQSLL VEERLAGATL
LIFANKQDLP GALSCNAIQE ALELDSIRSH HWRIQGCSAV TGEDLLPGID WLLDDISSRV
FTAD
