ARL2_CAEEL
ID ARL2_CAEEL Reviewed; 184 AA.
AC Q19705;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=ADP-ribosylation factor-like protein 2;
DE AltName: Full=Abnormal eversion of vulva protein 20;
GN Name=evl-20; Synonyms=arl-2; ORFNames=F22B5.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=12015966; DOI=10.1016/s1534-5807(02)00146-6;
RA Antoshechkin I., Han M.;
RT "The C. elegans evl-20 gene is a homolog of the small GTPase ARL2 and
RT regulates cytoskeleton dynamics during cytokinesis and morphogenesis.";
RL Dev. Cell 2:579-591(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION.
RX PubMed=15576487; DOI=10.1096/fj.04-2273com;
RA Li Y., Kelly W.G., Logsdon J.M. Jr., Schurko A.M., Harfe B.D.,
RA Hill-Harfe K.L., Kahn R.A.;
RT "Functional genomic analysis of the ADP-ribosylation factor family of
RT GTPases: phylogeny among diverse eukaryotes and function in C. elegans.";
RL FASEB J. 18:1834-1850(2004).
CC -!- FUNCTION: GTP-binding protein that functions in embryogenesis,
CC cytokinesis, germline development and microtubulule cytoskeleton
CC dynamics. {ECO:0000269|PubMed:12015966, ECO:0000269|PubMed:15576487}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12015966}. Cell
CC membrane {ECO:0000269|PubMed:12015966}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:12015966}. Note=Some diffuse cytoplasmic expression
CC is detected but expression is concentrated mainly next to centrosomes
CC and is excluded from the mitotic spindle area. Localizes to the
CC cortical plasma membrane of embryonic blastomeres.
CC -!- TISSUE SPECIFICITY: In the embryo, strongly expressed in migrating
CC hypodermal cells. Shortly before the beginning of elongation, expressed
CC in many developing neurons where it persists throughout adulthood. In
CC the larva, highly expressed in migrating hypodermal cells and the
CC uterus. Also expressed in vulva, spermatheca, sheath cells, distal tips
CC cells and proctoderm of the male tail. {ECO:0000269|PubMed:12015966}.
CC -!- DEVELOPMENTAL STAGE: Expression is first detected during embryogenesis
CC at the beginning of morphogenesis and continues in a subset of larval
CC tissues and in adult neurons. {ECO:0000269|PubMed:12015966}.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit abnormal vulva, gonad and male tail
CC development and disruption in embryonic proliferation. Subcellular
CC defects include a lack of microtubule cytoskeleton and excessive
CC chromosomes in oocyte nuclei. Many embryos show a lethal phenotype
CC arrested at the bean stage just prior to the beginning of
CC morphogenesis. {ECO:0000269|PubMed:12015966}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; Z50044; CAA90353.2; -; Genomic_DNA.
DR PIR; T21237; T21237.
DR RefSeq; NP_495779.1; NM_063378.1.
DR AlphaFoldDB; Q19705; -.
DR SMR; Q19705; -.
DR STRING; 6239.F22B5.1; -.
DR EPD; Q19705; -.
DR PaxDb; Q19705; -.
DR PeptideAtlas; Q19705; -.
DR EnsemblMetazoa; F22B5.1.1; F22B5.1.1; WBGene00001358.
DR GeneID; 191632; -.
DR KEGG; cel:CELE_F22B5.1; -.
DR UCSC; F22B5.1; c. elegans.
DR CTD; 191632; -.
DR WormBase; F22B5.1; CE27425; WBGene00001358; evl-20.
DR eggNOG; KOG0073; Eukaryota.
DR GeneTree; ENSGT00940000157941; -.
DR HOGENOM; CLU_040729_12_3_1; -.
DR InParanoid; Q19705; -.
DR OMA; EHRGYKL; -.
DR OrthoDB; 1271528at2759; -.
DR PhylomeDB; Q19705; -.
DR Reactome; R-CEL-9648002; RAS processing.
DR PRO; PR:Q19705; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001358; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005818; C:aster; IDA:WormBase.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; TAS:UniProtKB.
DR GO; GO:0043622; P:cortical microtubule organization; IMP:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:0030540; P:female genitalia development; IMP:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:WormBase.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cell membrane; Cytoplasm; Cytoskeleton;
KW Developmental protein; GTP-binding; Lipoprotein; Membrane; Myristate;
KW Nucleotide-binding; Reference proteome.
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_0000207440"
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 LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 184 AA; 20999 MW; 2CCEC9FE257F6916 CRC64;
MGFLKILRKQ RAREREMRIL ILGLDNAGKT TLMKKFLDEP TDTIEPTLGF DIKTVHFKDF
QLNLWDVGGQ KSLRSYWKNY FESTDALIWV VDSSDRERLL QCSEELKKLL GEERLAGASL
LVLANKSDLP GAIDVNSIAQ VLDLHSIKSH HWKIFSCCAL SGDRLVQAMT WLCDDVGSRL
FILD
