ID B3P8A4_DROER Unreviewed; 673 AA.
AC B3P8A4;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Mitochondrial Rho GTPase {ECO:0000256|PIRNR:PIRNR037488};
DE EC=3.6.5.- {ECO:0000256|PIRNR:PIRNR037488};
GN Name=Dere\GG12381 {ECO:0000313|EMBL:EDV53928.1};
GN ORFNames=Dere_GG12381 {ECO:0000313|EMBL:EDV53928.1};
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1] {ECO:0000313|EMBL:EDV53928.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV53928.1};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
RN [2] {ECO:0000313|EMBL:EDV53928.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV53928.1};
RX PubMed=18057021; DOI=10.1093/bioinformatics/btm542;
RA Zimin A.V., Smith D.R., Sutton G., Yorke J.A.;
RT "Assembly reconciliation.";
RL Bioinformatics 24:42-45(2008).
RN [3] {ECO:0000313|EMBL:EDV53928.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV53928.1};
RG FlyBase;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking.
CC {ECO:0000256|PIRNR:PIRNR037488}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-
CC pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}.
CC Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004200,
CC ECO:0000256|PIRNR:PIRNR037488}; Single-pass type IV membrane protein
CC {ECO:0000256|ARBA:ARBA00004200, ECO:0000256|PIRNR:PIRNR037488}.
CC -!- SIMILARITY: Belongs to the mitochondrial Rho GTPase family.
CC {ECO:0000256|ARBA:ARBA00007981, ECO:0000256|PIRNR:PIRNR037488}.
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DR EMBL; CH954182; EDV53928.1; -; Genomic_DNA.
DR RefSeq; XP_001982058.1; XM_001982022.2.
DR AlphaFoldDB; B3P8A4; -.
DR EnsemblMetazoa; FBtr0132435; FBpp0130927; FBgn0104669.
DR GeneID; 6555003; -.
DR KEGG; der:6555003; -.
DR eggNOG; KOG1707; Eukaryota.
DR HOGENOM; CLU_014255_3_1_1; -.
DR OMA; IILRKFH; -.
DR OrthoDB; 5481412at2759; -.
DR PhylomeDB; B3P8A4; -.
DR Proteomes; UP000008711; Unassembled WGS sequence.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0007005; P:mitochondrion organization; IEA:InterPro.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd01893; Miro1; 1.
DR CDD; cd01892; Miro2; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR013566; EF_hand_assoc_1.
DR InterPro; IPR013567; EF_hand_assoc_2.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR021181; Miro.
DR InterPro; IPR020860; MIRO_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003578; Small_GTPase_Rho.
DR PANTHER; PTHR24072:SF359; RAS-RELATED PROTEIN RAC1-RELATED; 1.
DR PANTHER; PTHR24072; RHO FAMILY GTPASE; 1.
DR Pfam; PF08355; EF_assoc_1; 1.
DR Pfam; PF08356; EF_assoc_2; 1.
DR Pfam; PF00071; Ras; 2.
DR PIRSF; PIRSF037488; Mt_Rho_GTPase; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS51423; MIRO; 2.
DR PROSITE; PS51419; RAB; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRNR:PIRNR037488};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PIRNR:PIRNR037488};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR037488};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR037488};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|PIRNR:PIRNR037488};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787,
KW ECO:0000256|PIRNR:PIRNR037488};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR037488}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 9..194
FT /note="Miro"
FT /evidence="ECO:0000259|PROSITE:PS51423"
FT DOMAIN 330..365
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 444..607
FT /note="Miro"
FT /evidence="ECO:0000259|PROSITE:PS51423"
SQ SEQUENCE 673 AA; 76538 MW; BB5E087ADD92F48F CRC64;
MGQYTASQRK NVRILLVGDA GVGKTSLILS LVSEEYPEEV PPRAEEITIP ANVTPEQVPT
SIVDFSTVEQ SEDALAAEIN KAHVVCIVYA VDDDDTLDRI TSHWLPLVRA KCNPSLDGDG
DAEAEAEGDI QREPIRKPIV LVGNKIDLIE YSTMDSVLAI MEDYPEIESC VECSAKTLHN
ISEMFYYAQK AVLHPTSPLY MMEEQELTSA CKKSLVRIFK ICDIDGDNLL NDYELNLFQR
RCFNTPLQPQ ILDEVKAVIQ KNVPDGIYND AVTLKGFLFL HCLFIQRGRN ETTWAVLRRF
GYNDHLEMCQ EYLRPPLKIP PGSSTELSHR GQQFLIAVFE RYDRDGDGAL SPEEHKMLFS
TCPAAPWSYS TDIRKSCPIN ETTGWVTLHG WLCRWTLMTL IDVVKTMEYL AYLGFNVHEN
DSQLAAIHVT RERRIDLAKR QSSRSVYKCH VIGPKGSGKT GMCRGFLVED MHKLIGKEFK
TNVVHCINSV QVYGQEKHLI LRDIDVRHAL DPLQPQEVNC DVACLVYDSS NPRSFEYVAR
IYIKYYAESK IPVMIVGTKS DMDERRQDYL MQPSEFCDKY KLLPPHLFSL KTNKKELYTK
LATMAAFPRF QAAWILFYKH RLVQLWESAH LRQFGLMTED PKLWWKAGLG VAAATMLGFI
VLKTLSAAGA HSR
//
