ATLAS_DROME
ID ATLAS_DROME Reviewed; 541 AA.
AC Q9VC57;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Atlastin;
DE EC=3.6.5.-;
GN Name=atl; ORFNames=CG6668;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo, and Head;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-514, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [5]
RP DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF ARG-192 AND
RP ARG-214.
RX PubMed=17030474; DOI=10.1016/j.neurobiolaging.2006.09.004;
RA Lee Y., Paik D., Bang S., Kang J., Chun B., Lee S., Bae E., Chung J.,
RA Kim J.;
RT "Loss of spastic paraplegia gene atlastin induces age-dependent death of
RT dopaminergic neurons in Drosophila.";
RL Neurobiol. Aging 29:84-94(2008).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH SPAS, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=19341724; DOI=10.1016/j.ydbio.2009.03.019;
RA Lee M., Paik S.K., Lee M.-J., Kim Y.-J., Kim S., Nahm M., Oh S.-J.,
RA Kim H.-M., Yim J., Lee C.J., Bae Y.C., Lee S.;
RT "Drosophila Atlastin regulates the stability of muscle microtubules and is
RT required for synapse development.";
RL Dev. Biol. 330:250-262(2009).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-51, HOMOOLIGOMERIZATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=19633650; DOI=10.1038/nature08280;
RA Orso G., Pendin D., Liu S., Tosetto J., Moss T.J., Faust J.E., Micaroni M.,
RA Egorova A., Martinuzzi A., McNew J.A., Daga A.;
RT "Homotypic fusion of ER membranes requires the dynamin-like GTPase
RT Atlastin.";
RL Nature 460:978-983(2009).
CC -!- FUNCTION: GTPase tethering membranes through formation of trans-
CC homooligomers and mediating homotypic fusion of endoplasmic reticulum
CC membranes. Functions in endoplasmic reticulum tubular network
CC biogenesis. May also regulate microtubule polymerization and Golgi
CC biogenesis. Required for dopaminergic neurons survival and the growth
CC of muscles and synapses at neuromuscular junctions.
CC {ECO:0000269|PubMed:19341724, ECO:0000269|PubMed:19633650}.
CC -!- SUBUNIT: Homooligomer; trans-homooligomer between proteins on adjacent
CC membranes. Interacts with spas; interaction may regulate microtubule
CC dynamics. {ECO:0000269|PubMed:19341724}.
CC -!- INTERACTION:
CC Q9VC57; Q9VC57: atl; NbExp=10; IntAct=EBI-173493, EBI-173493;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19341724, ECO:0000269|PubMed:19633650}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:19341724,
CC ECO:0000269|PubMed:19633650}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:19341724}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19341724}. Note=Colocalizes with microtubules
CC (PubMed:19341724).
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:19633650}.
CC -!- DEVELOPMENTAL STAGE: Expression levels are high during embryonic
CC development. Expressed within neuropil regions of the brain and ventral
CC nerve cord in larval CNS and larval body-wall muscles (at protein
CC level). {ECO:0000269|PubMed:17030474, ECO:0000269|PubMed:19341724,
CC ECO:0000269|PubMed:19633650}.
CC -!- DISRUPTION PHENOTYPE: The gene is essential with only a few escapers.
CC Flies display a short life span and are sensitive to mechanical shocks.
CC Following bumping they undergo muscle spasm, followed by paralysis,
CC delayed spasm and finally recovery. The sensitivity to shocks increases
CC with age. {ECO:0000269|PubMed:17030474, ECO:0000269|PubMed:19341724}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. GB1/RHD3 GTPase family. GB1 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01052}.
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DR EMBL; AE014297; AAF56318.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14008.1; -; Genomic_DNA.
DR EMBL; AY069079; AAL39224.1; -; mRNA.
DR EMBL; BT004893; AAO47871.1; -; mRNA.
DR RefSeq; NP_001287506.1; NM_001300577.1.
DR RefSeq; NP_651274.1; NM_143017.3.
DR RefSeq; NP_733020.1; NM_170157.2.
DR PDB; 3X1D; X-ray; 2.87 A; A=1-541.
DR PDBsum; 3X1D; -.
DR AlphaFoldDB; Q9VC57; -.
DR SMR; Q9VC57; -.
DR BioGRID; 67860; 76.
DR DIP; DIP-59281N; -.
DR IntAct; Q9VC57; 1.
DR STRING; 7227.FBpp0084036; -.
DR TCDB; 1.N.5.1.2; the endoplasmic reticulum fusion gtpase, atlastin (atlastin) family.
DR iPTMnet; Q9VC57; -.
DR PaxDb; Q9VC57; -.
DR PRIDE; Q9VC57; -.
DR DNASU; 42934; -.
DR EnsemblMetazoa; FBtr0084656; FBpp0084036; FBgn0039213.
DR EnsemblMetazoa; FBtr0084657; FBpp0084037; FBgn0039213.
DR EnsemblMetazoa; FBtr0345218; FBpp0311413; FBgn0039213.
DR GeneID; 42934; -.
DR KEGG; dme:Dmel_CG6668; -.
DR UCSC; CG6668-RA; d. melanogaster.
DR CTD; 42934; -.
DR FlyBase; FBgn0039213; atl.
DR VEuPathDB; VectorBase:FBgn0039213; -.
DR eggNOG; KOG2037; Eukaryota.
DR GeneTree; ENSGT00940000165594; -.
DR HOGENOM; CLU_021447_2_1_1; -.
DR InParanoid; Q9VC57; -.
DR OMA; GFIHNIW; -.
DR OrthoDB; 1027269at2759; -.
DR PhylomeDB; Q9VC57; -.
DR SignaLink; Q9VC57; -.
DR BioGRID-ORCS; 42934; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42934; -.
DR PRO; PR:Q9VC57; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039213; Expressed in thoracico-abdominal ganglion (Drosophila) and 47 other tissues.
DR ExpressionAtlas; Q9VC57; baseline and differential.
DR Genevisible; Q9VC57; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; IDA:FlyBase.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IMP:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0032561; F:guanyl ribonucleotide binding; IMP:FlyBase.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IDA:FlyBase.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0061025; P:membrane fusion; IDA:UniProtKB.
DR GO; GO:0007019; P:microtubule depolymerization; IMP:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; IMP:UniProtKB.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:FlyBase.
DR GO; GO:0048691; P:positive regulation of axon extension involved in regeneration; IMP:FlyBase.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0031114; P:regulation of microtubule depolymerization; IMP:FlyBase.
DR GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0051124; P:synaptic assembly at neuromuscular junction; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030386; G_GB1_RHD3_dom.
DR InterPro; IPR036543; Guanylate-bd_C_sf.
DR InterPro; IPR015894; Guanylate-bd_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02263; GBP; 1.
DR SUPFAM; SSF48340; SSF48340; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51715; G_GB1_RHD3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Golgi apparatus; GTP-binding;
KW Hydrolase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..541
FT /note="Atlastin"
FT /id="PRO_0000384815"
FT TOPO_DOM 1..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..448
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 470..541
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..284
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT BINDING 45..52
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 93..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 192..193
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 251..254
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 514
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 51
FT /note="K->A: Loss of GTPase activity. Loss of endoplasmic
FT reticulum membrane fusion. Does not oligomerize."
FT /evidence="ECO:0000269|PubMed:19633650"
FT MUTAGEN 192
FT /note="R->Q: Sensitivity to mechanical shocks."
FT /evidence="ECO:0000269|PubMed:17030474"
FT MUTAGEN 214
FT /note="R->C: Sensitivity to mechanical shocks."
FT /evidence="ECO:0000269|PubMed:17030474"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:3X1D"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:3X1D"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:3X1D"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:3X1D"
FT HELIX 51..59
FT /evidence="ECO:0007829|PDB:3X1D"
FT TURN 63..67
FT /evidence="ECO:0007829|PDB:3X1D"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:3X1D"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:3X1D"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:3X1D"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:3X1D"
FT STRAND 147..156
FT /evidence="ECO:0007829|PDB:3X1D"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:3X1D"
FT TURN 164..170
FT /evidence="ECO:0007829|PDB:3X1D"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:3X1D"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:3X1D"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:3X1D"
FT HELIX 204..213
FT /evidence="ECO:0007829|PDB:3X1D"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:3X1D"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:3X1D"
FT TURN 228..232
FT /evidence="ECO:0007829|PDB:3X1D"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:3X1D"
FT STRAND 237..245
FT /evidence="ECO:0007829|PDB:3X1D"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:3X1D"
FT HELIX 266..279
FT /evidence="ECO:0007829|PDB:3X1D"
FT HELIX 300..307
FT /evidence="ECO:0007829|PDB:3X1D"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:3X1D"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:3X1D"
FT HELIX 323..343
FT /evidence="ECO:0007829|PDB:3X1D"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:3X1D"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:3X1D"
FT HELIX 362..375
FT /evidence="ECO:0007829|PDB:3X1D"
FT TURN 387..390
FT /evidence="ECO:0007829|PDB:3X1D"
FT HELIX 391..400
FT /evidence="ECO:0007829|PDB:3X1D"
FT TURN 402..405
FT /evidence="ECO:0007829|PDB:3X1D"
SQ SEQUENCE 541 AA; 60912 MW; 6BD0449025B0AE42 CRC64;
MGGSAVQVIN ASEEHTFVLN EDALSEVLMR DEVKDRFVCV VSVAGAFRKG KSFLLDFFLR
YMYSKYVHHD ATDWLGGESD PLEGFSWRGG SERDTTGILM WSDIFLHDYP NGDKIAIILL
DTQGAFDSQS TVRDCATVFA LSTMLSSVQI YNLSQNIQED DLQHLQLFTE YGRLALADTG
KKPFQRLQFL VRDWSFPYEA EYGALGGDKI LKRRLEVSDK QHPELQSLRR HISSCFTEVA
CFLMPHPGLN VATNPKFDGR LQDITPEFKS SLRSLVPMLL APDNLVYKEI SGQRVRARDL
IQYFQSYMNI YKGNELPEPK SMLVATAEAN HLTAVAAAKE LYGQLMEEVC GGTRPYLSTA
HLQTEHLRVK DKALFQFAAK RKMGGEEFTE KFRKQLEDDL EEVFTNYQAH NESKNIFKAA
RTPAVYFACA VIMYILSGIF GLVGLYTFAN FCNLVMGVAL LTLALWAYIR YSGELSDFGG
KLDDFATLLW EKFMRPIYHG CMEKGIHHVA THATEMAVGG GAASYRSQTS VNASNGKVKR
S
