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ARL8_DROME
ID   ARL8_DROME              Reviewed;         186 AA.
AC   Q9VHV5;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=ADP-ribosylation factor-like protein 8 {ECO:0000303|PubMed:29940804, ECO:0000312|FlyBase:FBgn0037551};
DE   AltName: Full=Novel small G protein indispensable for equal chromosome segregation;
DE            Short=dGie;
GN   Name=Arl8 {ECO:0000303|PubMed:29940804, ECO:0000312|FlyBase:FBgn0037551};
GN   Synonyms=Gie {ECO:0000303|PubMed:15331635,
GN   ECO:0000312|FlyBase:FBgn0037551};
GN   ORFNames=CG7891 {ECO:0000312|FlyBase:FBgn0037551};
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 [MRNA], FUNCTION, AND INTERACTION WITH TUBULIN.
RX   PubMed=15331635; DOI=10.1242/jcs.01347;
RA   Okai T., Araki Y., Tada M., Tateno T., Kontani K., Katada T.;
RT   "Novel small GTPase subfamily capable of associating with tubulin is
RT   required for chromosome segregation.";
RL   J. Cell Sci. 117:4705-4715(2004).
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=Embryo;
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   SUBCELLULAR LOCATION.
RX   PubMed=16537643; DOI=10.1242/jcs.02958;
RA   Hofmann I., Munro S.;
RT   "An N-terminally acetylated Arf-like GTPase is localised to lysosomes and
RT   affects their motility.";
RL   J. Cell Sci. 119:1494-1503(2006).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=29940804; DOI=10.1080/15548627.2018.1458170;
RA   Lund V.K., Madsen K.L., Kjaerulff O.;
RT   "Drosophila Rab2 controls endosome-lysosome fusion and LAMP delivery to
RT   late endosomes.";
RL   Autophagy 14:1520-1542(2018).
RN   [7]
RP   FUNCTION, INTERACTION WITH RILPL, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP   STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF THR-34 AND GLN-75.
RX   PubMed=30115618; DOI=10.1242/bio.035964;
RA   Rosa-Ferreira C., Sweeney S.T., Munro S.;
RT   "The small G protein Arl8 contributes to lysosomal function and long-range
RT   axonal transport in Drosophila.";
RL   Biol. Open 7:0-0(2018).
RN   [8]
RP   FUNCTION, INTERACTION WITH UNC-104, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=30174114; DOI=10.1016/j.neuron.2018.08.004;
RA   Vukoja A., Rey U., Petzoldt A.G., Ott C., Vollweiter D., Quentin C.,
RA   Puchkov D., Reynolds E., Lehmann M., Hohensee S., Rosa S., Lipowsky R.,
RA   Sigrist S.J., Haucke V.;
RT   "Presynaptic Biogenesis Requires Axonal Transport of Lysosome-Related
RT   Vesicles.";
RL   Neuron 99:1216-1232(2018).
CC   -!- FUNCTION: Required for normal functioning of the late endocytic pathway
CC       including lysosome motility and late endosome-lysosome fusion
CC       (PubMed:16537643, PubMed:29940804, PubMed:30115618). Not required for
CC       the delivery of lysosomal membrane protein-containing vesicles to late
CC       endosomes (PubMed:29940804). In larval motorneurons, mediates the
CC       anterograde axonal long-range transport of presynaptic lysosome-related
CC       vesicles required for presynaptic biogenesis and synaptic function
CC       (PubMed:30174114, PubMed:30115618). Essential role in chromosome
CC       segregation (PubMed:15331635). {ECO:0000269|PubMed:15331635,
CC       ECO:0000269|PubMed:16537643, ECO:0000269|PubMed:29940804,
CC       ECO:0000269|PubMed:30115618, ECO:0000269|PubMed:30174114}.
CC   -!- SUBUNIT: Interacts with tubulin (PubMed:15331635). Interacts (in GTP-
CC       bound form) with Rilpl (PubMed:30115618). Interacts with unc-104
CC       (PubMed:30174114). {ECO:0000269|PubMed:15331635,
CC       ECO:0000269|PubMed:30115618, ECO:0000269|PubMed:30174114}.
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:16537643,
CC       ECO:0000269|PubMed:30115618, ECO:0000269|PubMed:30174114}. Synapse
CC       {ECO:0000269|PubMed:30115618, ECO:0000269|PubMed:30174114}. Cell
CC       projection, axon {ECO:0000269|PubMed:30115618,
CC       ECO:0000269|PubMed:30174114}. Perikaryon {ECO:0000269|PubMed:30115618,
CC       ECO:0000269|PubMed:30174114}. Note=Localizes the perinuclear region
CC       when associated with CG11448. {ECO:0000269|PubMed:30115618,
CC       ECO:0000269|PubMed:30174114}.
CC   -!- TISSUE SPECIFICITY: Expressed throughout development, from embryo to
CC       adult stage, in different tissues such as larval motor neurons,
CC       salivary glands, testis and ovaries (at protein level).
CC       {ECO:0000269|PubMed:30115618}.
CC   -!- DISRUPTION PHENOTYPE: Lethal from late larval stages (PubMed:29940804,
CC       PubMed:30115618). In garland cells, results in defective late endosome-
CC       lysosome fusion and inability to form a rapidly exchanging terminal
CC       lysosomal network (PubMed:29940804). In motor neurons, results in
CC       defective anterograde axonal long-range transport of lysosome-related
CC       vesicles which leads to defective protein localization to presynaptic
CC       active zone and synaptic vesicles (PubMed:30174114, PubMed:30115618).
CC       This results into a reduction of number of boutons per synapses which
CC       limits neurotrasmitter release and leads to posterior paralysis
CC       (PubMed:30174114, PubMed:30115618). RNAi-mediated knockdown in larval
CC       presynaptic motoneurons results in defective presynaptic biogenesis
CC       (PubMed:30174114). {ECO:0000269|PubMed:29940804,
CC       ECO:0000269|PubMed:30115618, ECO:0000269|PubMed:30174114}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC       {ECO:0000305}.
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DR   EMBL; AB185208; BAD30092.1; -; mRNA.
DR   EMBL; AE014297; AAF54194.1; -; Genomic_DNA.
DR   EMBL; AY094809; AAM11162.1; -; mRNA.
DR   RefSeq; NP_001287225.1; NM_001300296.1.
DR   RefSeq; NP_001287226.1; NM_001300297.1.
DR   RefSeq; NP_649769.1; NM_141512.3.
DR   AlphaFoldDB; Q9VHV5; -.
DR   SMR; Q9VHV5; -.
DR   BioGRID; 66144; 33.
DR   IntAct; Q9VHV5; 5.
DR   STRING; 7227.FBpp0081290; -.
DR   PaxDb; Q9VHV5; -.
DR   PRIDE; Q9VHV5; -.
DR   DNASU; 40961; -.
DR   EnsemblMetazoa; FBtr0081794; FBpp0081290; FBgn0037551.
DR   EnsemblMetazoa; FBtr0339723; FBpp0308779; FBgn0037551.
DR   EnsemblMetazoa; FBtr0339724; FBpp0308780; FBgn0037551.
DR   GeneID; 40961; -.
DR   KEGG; dme:Dmel_CG7891; -.
DR   UCSC; CG7891-RA; d. melanogaster.
DR   CTD; 327551; -.
DR   FlyBase; FBgn0037551; Arl8.
DR   VEuPathDB; VectorBase:FBgn0037551; -.
DR   eggNOG; KOG0075; Eukaryota.
DR   GeneTree; ENSGT00940000165940; -.
DR   HOGENOM; CLU_040729_10_0_1; -.
DR   InParanoid; Q9VHV5; -.
DR   OMA; GREVSCY; -.
DR   OrthoDB; 1123043at2759; -.
DR   PhylomeDB; Q9VHV5; -.
DR   Reactome; R-DME-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 40961; 1 hit in 3 CRISPR screens.
DR   ChiTaRS; Gie; fly.
DR   GenomeRNAi; 40961; -.
DR   PRO; PR:Q9VHV5; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0037551; Expressed in saliva-secreting gland and 39 other tissues.
DR   ExpressionAtlas; Q9VHV5; baseline and differential.
DR   Genevisible; Q9VHV5; DM.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0030424; C:axon; IDA:UniProtKB.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0032419; C:extrinsic component of lysosome membrane; IDA:UniProtKB.
DR   GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR   GO; GO:0005764; C:lysosome; IDA:FlyBase.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:1990027; C:S bouton; IDA:UniProtKB.
DR   GO; GO:0051233; C:spindle midzone; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR   GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
DR   GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
DR   GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0008089; P:anterograde axonal transport; IMP:UniProtKB.
DR   GO; GO:0061909; P:autophagosome-lysosome fusion; IMP:FlyBase.
DR   GO; GO:0098930; P:axonal transport; IMP:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:1902774; P:late endosome to lysosome transport; IMP:UniProtKB.
DR   GO; GO:0032418; P:lysosome localization; IMP:FlyBase.
DR   GO; GO:0007269; P:neurotransmitter secretion; IMP:UniProtKB.
DR   GO; GO:0099054; P:presynapse assembly; IMP:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0001666; P:response to hypoxia; IMP:FlyBase.
DR   GO; GO:0000819; P:sister chromatid segregation; IMP:UniProtKB.
DR   CDD; cd04159; Arl10_like; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR044154; Arl8a/8b.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR006689; Small_GTPase_ARF/SAR.
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; Cell division; Cell projection; Chromosome partition;
KW   GTP-binding; Lysosome; Membrane; Mitosis; Nucleotide-binding;
KW   Protein transport; Reference proteome; Synapse; Transport.
FT   CHAIN           1..186
FT                   /note="ADP-ribosylation factor-like protein 8"
FT                   /id="PRO_0000232927"
FT   INTRAMEM        1..19
FT                   /note="Note=Mediates targeting to membranes"
FT                   /evidence="ECO:0000250"
FT   BINDING         29..35
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         71..75
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         130..133
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         34
FT                   /note="T->N: Probably constitutively inactive (GDP-locked
FT                   form). Abolishes interaction with CG11448."
FT                   /evidence="ECO:0000269|PubMed:30115618"
FT   MUTAGEN         75
FT                   /note="Q->L: Probably constitutively active (GTP-locked
FT                   form). Does not affect interaction with CG11448."
FT                   /evidence="ECO:0000269|PubMed:30115618"
SQ   SEQUENCE   186 AA;  21254 MW;  B437D8EC4D001EE0 CRC64;
     MLALINRILE WFKSIFWKEE MELTLVGLQF SGKTTFVNVI ASGQFAEDMI PTVGFNMRKI
     TRGNVTIKVW DIGGQPRFRS MWERYCRGVN AIVYMVDAAD LDKLEASRNE LHSLLDKPQL
     AGIPVLVLGN KRDLPGALDE TGLIERMNLS SIQDREICCY SISCKEKDNI DITLQWLIQH
     SKSQSR
 
 
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