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GDS1_DROME
ID   GDS1_DROME              Reviewed;         635 AA.
AC   A1Z6S7; A1Z6S6; O44116; Q86LF4; Q8T996;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=GTPase-GDP dissociation stimulator vimar {ECO:0000305};
GN   Name=vimar {ECO:0000312|FlyBase:FBgn0022960};
GN   Synonyms=l(2)k16722 {ECO:0000312|FlyBase:FBgn0022960};
GN   ORFNames=CG3572 {ECO:0000312|FlyBase:FBgn0022960};
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 {ECO:0000312|Proteomes:UP000000803};
RN   [1] {ECO:0000312|EMBL:AAB87984.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX   PubMed=9533953; DOI=10.1016/s0925-4773(98)00016-1;
RA   Lo P.C., Frasch M.;
RT   "bagpipe-Dependent expression of vimar, a novel Armadillo-repeats gene, in
RT   Drosophila visceral mesoderm.";
RL   Mech. Dev. 72:65-75(1998).
RN   [2] {ECO:0000312|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|EMBL:AAL40010.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAL40010.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAL40010.1};
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] {ECO:0000312|EMBL:AAO47869.1, ECO:0000312|EMBL:ACI15753.1, ECO:0000312|EMBL:ADX35945.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAO47869.1, ECO:0000312|EMBL:ACI15753.1,
RC   ECO:0000312|EMBL:ADX35945.1}; TISSUE=Embryo {ECO:0000312|EMBL:AAO47869.1};
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.,
RA   Booth B.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH MIRO, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=27716788; DOI=10.1371/journal.pgen.1006359;
RA   Ding L., Lei Y., Han Y., Li Y., Ji X., Liu L.;
RT   "Vimar Is a Novel Regulator of Mitochondrial Fission through Miro.";
RL   PLoS Genet. 12:e1006359-e1006359(2016).
CC   -!- FUNCTION: Probably acts as a GEF (guanine nucleotide exchange factor)
CC       for the Rho family of small GTP-binding proteins (G proteins) that
CC       stimulates the dissociation of GDP to enable subsequent binding of GTP
CC       (By similarity). May also chaperone the processing and/or trafficking
CC       of small GTPases independently of GEF activity (By similarity). By
CC       interacting with Miro, promotes mitochondrial fission in response to
CC       high calcium concentrations (PubMed:27716788).
CC       {ECO:0000250|UniProtKB:P52306, ECO:0000269|PubMed:27716788}.
CC   -!- SUBUNIT: Interacts with Miro. {ECO:0000269|PubMed:27716788}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000269|PubMed:27716788}. Mitochondrion
CC       {ECO:0000269|PubMed:27716788}. Cytoplasm, cytosol
CC       {ECO:0000269|PubMed:27716788}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the mesoderm during embryogenesis.
CC       {ECO:0000269|PubMed:9533953}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown perturbs mitochondrial
CC       distribution and dynamics. {ECO:0000269|PubMed:27716788}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL40010.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF034421; AAB87984.1; -; mRNA.
DR   EMBL; AE013599; AAS64794.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAF57418.1; -; Genomic_DNA.
DR   EMBL; BT004891; AAO47869.1; -; mRNA.
DR   EMBL; AY069865; AAL40010.1; ALT_INIT; mRNA.
DR   EMBL; BT044558; ACI15753.1; -; mRNA.
DR   EMBL; BT125966; ADX35945.1; -; mRNA.
DR   RefSeq; NP_477305.1; NM_057957.5.
DR   RefSeq; NP_995767.1; NM_206045.2.
DR   AlphaFoldDB; A1Z6S7; -.
DR   SMR; A1Z6S7; -.
DR   IntAct; A1Z6S7; 15.
DR   STRING; 7227.FBpp0085514; -.
DR   PaxDb; A1Z6S7; -.
DR   PeptideAtlas; A1Z6S7; -.
DR   DNASU; 35609; -.
DR   EnsemblMetazoa; FBtr0086182; FBpp0085514; FBgn0022960.
DR   EnsemblMetazoa; FBtr0086183; FBpp0089175; FBgn0022960.
DR   GeneID; 35609; -.
DR   KEGG; dme:Dmel_CG3572; -.
DR   UCSC; CG3572-RC; d. melanogaster.
DR   CTD; 35609; -.
DR   FlyBase; FBgn0022960; vimar.
DR   VEuPathDB; VectorBase:FBgn0022960; -.
DR   eggNOG; KOG4500; Eukaryota.
DR   GeneTree; ENSGT00390000014293; -.
DR   HOGENOM; CLU_021124_0_0_1; -.
DR   InParanoid; A1Z6S7; -.
DR   OMA; IAWLINN; -.
DR   OrthoDB; 561489at2759; -.
DR   PhylomeDB; A1Z6S7; -.
DR   BioGRID-ORCS; 35609; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; vimar; fly.
DR   GenomeRNAi; 35609; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0022960; Expressed in wing disc and 36 other tissues.
DR   ExpressionAtlas; A1Z6S7; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IGI:UniProtKB.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:FlyBase.
DR   GO; GO:1901215; P:negative regulation of neuron death; IMP:FlyBase.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR   GO; GO:0010821; P:regulation of mitochondrion organization; IGI:UniProtKB.
DR   GO; GO:0042052; P:rhabdomere development; IMP:FlyBase.
DR   Gene3D; 1.25.10.10; -; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR040144; RAP1GDS1.
DR   PANTHER; PTHR10957; PTHR10957; 1.
DR   SMART; SM00185; ARM; 4.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Endoplasmic reticulum; Guanine-nucleotide releasing factor;
KW   Mitochondrion; Reference proteome; Repeat.
FT   CHAIN           1..635
FT                   /note="GTPase-GDP dissociation stimulator vimar"
FT                   /id="PRO_0000455599"
FT   REPEAT          72..118
FT                   /note="ARM 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          346..391
FT                   /note="ARM 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          392..432
FT                   /note="ARM 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          510..550
FT                   /note="ARM 4"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        1..4
FT                   /note="MATA -> MAT (in Ref. 5; AAF57418/ADX35945 and 1;
FT                   AAB87984)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218
FT                   /note="S -> A (in Ref. 1; AAB87984 and 4; AAL40010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        621
FT                   /note="E -> G (in Ref. 5; AAO47869)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   635 AA;  70325 MW;  4027B8623F4AC3BE CRC64;
     MATAEIDDLI EKLKTTSVSP ANTTNLLCEI SATKDPKLFD KHELAECFLG LTKCDDTNVR
     KEAAKCIAEI TKSEVQRKKF TKRNIIAAFL ECLRQVPTSD GSMELPIQIC RALGNICYLN
     DEARDLILEL EGDAVLLRLL DITTIEDVAN AAQFIKVRGG LLSNYLLGGE GLAKRAMELG
     VMKKLQGIID IGASNVEQHE DLLLNTLPLL SILTENVSDL NFDSSLNIQL SRILAASTNP
     DLAEMCLELL HYQAESDEVK LILAKDGLCE TIYNLLEKYK TLASTSEARA LMKLACELIV
     LILTGDDSMH YLYTTPLLKN MVDWLDSTDI DLLTTGVLAL GNFARTDSHC IYFVEQQTMN
     KLLEVLAKNN GVKDDVRLQH ALLSALRNLV IPKPNKNAVI QAGLVQTILP MLEIHQPPVV
     FKLLGTLRMT VDGQEKLALE LLKNKTLIEQ LVHWSKSSDY AGVTGESLRL MAWLIKHAYL
     SKIAYALPRK GDAPAEQIAD KIPLTQDYDR SSLSEFLANE GTVEAMVSML TAQHLVMQNE
     ALIALCILSV VYLSQPSEAA QAQLLQDELV KCEVGKKLAE LISKSSDTMT KEIVENLQNC
     VNLLKSSEQL VAHLEQHNIN ELLKSIPILT EYCTL
 
 
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