ARL2_BOVIN
ID ARL2_BOVIN Reviewed; 184 AA.
AC Q2TA37;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=ADP-ribosylation factor-like protein 2;
GN Name=ARL2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION IN A COMPLEX WITH ARL2BP AND SLC25A6, SUBCELLULAR LOCATION,
RP 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 IDENTIFICATION IN A COMPLEX WITH PPP2CB; PPP2R1A; PPP2R2A; PPP2R5E AND
RP TBCD, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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 [4]
RP FUNCTION, INTERACTION WITH TBCD, MUTAGENESIS OF THR-30 AND GLN-70, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17704193; DOI=10.1096/fj.06-7786com;
RA Shultz T., Shmuel M., Hyman T., Altschuler Y.;
RT "Beta-tubulin cofactor D and ARL2 take part in apical junctional complex
RT disassembly and abrogate epithelial structure.";
RL FASEB J. 22:168-182(2008).
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. {ECO:0000269|PubMed:17704193}.
CC -!- SUBUNIT: Interacts with ELMOD2. Interacts with ARL2BP; the GTP-bound
CC form interacts with ARL2BP. The GDP-bound form interacts preferentially
CC with TBCD. Interacts with UNC119. Found in a complex with ARL2, ARL2BP
CC and SLC25A4. The GTP-bound form interacts with PDE6D (By similarity).
CC Found in a complex with ARL2, ARL2BP and SLC25A6. Found in a complex
CC with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD.
CC {ECO:0000250, ECO:0000269|PubMed:11809823, ECO:0000269|PubMed:12912990,
CC ECO:0000269|PubMed:17704193}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Mitochondrion
CC intermembrane space {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250}. Cytoplasm. Mitochondrion.
CC Note=The complex formed with ARL2BP, ARL2 and SLC25A4 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 (By similarity). The complex formed with
CC ARL2BP, ARL2 and SLC25A6 is expressed in mitochondria. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in liver and retina (at protein level).
CC {ECO:0000269|PubMed:11809823, ECO:0000269|PubMed:12912990}.
CC -!- PTM: Not N-myristoylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; BC111133; AAI11134.1; -; mRNA.
DR RefSeq; NP_001033168.1; NM_001038079.2.
DR AlphaFoldDB; Q2TA37; -.
DR SMR; Q2TA37; -.
DR STRING; 9913.ENSBTAP00000002890; -.
DR PaxDb; Q2TA37; -.
DR PRIDE; Q2TA37; -.
DR Ensembl; ENSBTAT00000002890; ENSBTAP00000002890; ENSBTAG00000002238.
DR GeneID; 511349; -.
DR KEGG; bta:511349; -.
DR CTD; 402; -.
DR VEuPathDB; HostDB:ENSBTAG00000002238; -.
DR VGNC; VGNC:97240; ARL2.
DR eggNOG; KOG0073; Eukaryota.
DR GeneTree; ENSGT00940000157941; -.
DR HOGENOM; CLU_040729_12_3_1; -.
DR InParanoid; Q2TA37; -.
DR OMA; EHRGYKL; -.
DR OrthoDB; 1271528at2759; -.
DR TreeFam; TF105462; -.
DR Reactome; R-BTA-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000002238; Expressed in laryngeal cartilage and 104 other tissues.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; TAS:AgBase.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019003; F:GDP binding; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0034333; P:adherens junction assembly; IDA:UniProtKB.
DR GO; GO:0070830; P:bicellular tight junction assembly; IDA: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; IDA: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; IEA:Ensembl.
DR GO; GO:0006110; P:regulation of glycolytic process; IEA:Ensembl.
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_0000245353"
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 /evidence="ECO:0000250|UniProtKB:P36404"
FT MUTAGEN 30
FT /note="T->L: No effect on tubulin degradation or cell
FT detachment. Inhibits TBCD-dependent tubulin degradation.
FT Does not reduces interaction with TBCD."
FT /evidence="ECO:0000269|PubMed:17704193"
FT MUTAGEN 70
FT /note="Q->L: No effect on tubulin degradation or cell
FT detachment. Does not reduce TBCD-dependent tubulin
FT degradation. Reduces slightly interaction with TBCD."
FT /evidence="ECO:0000269|PubMed:17704193"
SQ SEQUENCE 184 AA; 20907 MW; 27C9D726C92505E3 CRC64;
MGLLTILKKM KQKERELRLL MLGLDNAGKT TILKKFNGED IDTISPTLGF NIKTLEHRGF
KLNIWDVGGQ KSLRSYWRNY FESTDGLIWV VDSADRQRMQ DCQRELQNLL VEERLAGATL
LIFANKQDLP GALSSNAIRE ALELDSIRSH HWCIQGCSAV TGENLLPGID WLLDDISSRI
FMAD
