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Database: UniProt
Entry: ARL2_DROME
LinkDB: ARL2_DROME
Original site: ARL2_DROME 
ID   ARL2_DROME              Reviewed;         184 AA.
AC   Q06849; B5RJE0; Q95TW2; Q9VHS1;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   24-JAN-2024, entry version 171.
DE   RecName: Full=ADP-ribosylation factor-like protein 2;
GN   Name=Arl2; Synonyms=Arf84F; ORFNames=CG7435;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=iso1;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Ovary;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley;
RA   Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: GTP-binding protein involved in protein trafficking; may
CC       modulate vesicle budding and uncoating within the Golgi apparatus.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC       {ECO:0000305}.
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DR   EMBL; L14923; AAA74629.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF54228.1; -; Genomic_DNA.
DR   EMBL; AY058480; AAL13709.1; -; mRNA.
DR   EMBL; BT044414; ACH92479.1; -; mRNA.
DR   RefSeq; NP_476886.1; NM_057538.3.
DR   AlphaFoldDB; Q06849; -.
DR   SMR; Q06849; -.
DR   BioGRID; 66174; 12.
DR   DIP; DIP-21465N; -.
DR   STRING; 7227.FBpp0081328; -.
DR   PaxDb; 7227-FBpp0081328; -.
DR   DNASU; 40993; -.
DR   EnsemblMetazoa; FBtr0081838; FBpp0081328; FBgn0004908.
DR   GeneID; 40993; -.
DR   KEGG; dme:Dmel_CG7435; -.
DR   AGR; FB:FBgn0004908; -.
DR   CTD; 402; -.
DR   FlyBase; FBgn0004908; Arl2.
DR   VEuPathDB; VectorBase:FBgn0004908; -.
DR   eggNOG; KOG0073; Eukaryota.
DR   GeneTree; ENSGT00940000157941; -.
DR   HOGENOM; CLU_040729_12_3_1; -.
DR   InParanoid; Q06849; -.
DR   OMA; MNIDRHW; -.
DR   OrthoDB; 5349301at2759; -.
DR   PhylomeDB; Q06849; -.
DR   Reactome; R-DME-9648002; RAS processing.
DR   BioGRID-ORCS; 40993; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 40993; -.
DR   PRO; PR:Q06849; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0004908; Expressed in testis and 25 other cell types or tissues.
DR   Genevisible; Q06849; DM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0005525; F:GTP binding; ISS:FlyBase.
DR   GO; GO:0003924; F:GTPase activity; ISS:FlyBase.
DR   GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:FlyBase.
DR   GO; GO:0045196; P:establishment or maintenance of neuroblast polarity; IMP:FlyBase.
DR   GO; GO:1902850; P:microtubule cytoskeleton organization involved in mitosis; IMP:FlyBase.
DR   GO; GO:0007269; P:neurotransmitter secretion; TAS:FlyBase.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0048488; P:synaptic vesicle endocytosis; TAS:FlyBase.
DR   CDD; cd04154; Arl2; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR45697:SF2; ADP-RIBOSYLATION FACTOR-LIKE PROTEIN 2; 1.
DR   PANTHER; PTHR45697; ADP-RIBOSYLATION FACTOR-LIKE PROTEIN 2-RELATED; 1.
DR   Pfam; PF00025; Arf; 1.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00177; ARF; 1.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00178; SAR; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51417; ARF; 1.
PE   2: Evidence at transcript level;
KW   GTP-binding; Lipoprotein; Myristate; Nucleotide-binding;
KW   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_0000207449"
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         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"
FT   CONFLICT        72
FT                   /note="S -> Y (in Ref. 4; AAL13709)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   184 AA;  20834 MW;  F1C8894BE74466B6 CRC64;
     MGFLTVLKKM RQKEREMRIL LLGLDNAGKT TILKRFNGEP IDTISPTLGF NIKTLEHNGY
     TLNMWDVGGQ KSLRSYWRNY FESTDGLVWV VDSADRMRLE SCGQELQVLL QEERLAGATL
     LVLCNKQDLP GALSSNEIKE ILHLEDITTH HWLVAGVSAV TGEKLLSSMD WLIADIAKRI
     FTLD
//
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