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MIRO1_CHICK
ID   MIRO1_CHICK             Reviewed;         619 AA.
AC   Q5ZM73;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Mitochondrial Rho GTPase 1;
DE            Short=MIRO-1;
DE            EC=3.6.5.-;
DE   AltName: Full=Ras homolog gene family member T1;
GN   Name=RHOT1; ORFNames=RCJMB04_2p2;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking.
CC       Probably involved in control of anterograde transport of mitochondria
CC       and their subcellular distribution (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC       Single-pass type IV membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the mitochondrial Rho GTPase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00757, ECO:0000305}.
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DR   EMBL; AJ719511; CAG31170.1; -; mRNA.
DR   RefSeq; NP_001006208.1; NM_001006208.1.
DR   AlphaFoldDB; Q5ZM73; -.
DR   SMR; Q5ZM73; -.
DR   STRING; 9031.ENSGALP00000005362; -.
DR   PaxDb; Q5ZM73; -.
DR   PRIDE; Q5ZM73; -.
DR   GeneID; 417410; -.
DR   KEGG; gga:417410; -.
DR   CTD; 55288; -.
DR   VEuPathDB; HostDB:geneid_417410; -.
DR   eggNOG; KOG1707; Eukaryota.
DR   InParanoid; Q5ZM73; -.
DR   OrthoDB; 538388at2759; -.
DR   PhylomeDB; Q5ZM73; -.
DR   PRO; PR:Q5ZM73; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0019725; P:cellular homeostasis; ISS:UniProtKB.
DR   GO; GO:0097345; P:mitochondrial outer membrane permeabilization; ISS:UniProtKB.
DR   GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR   GO; GO:0047497; P:mitochondrion transport along microtubule; ISS:UniProtKB.
DR   GO; GO:0010821; P:regulation of mitochondrion organization; IBA:GO_Central.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 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; IPR029506; Miro-1.
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; PTHR24072; 1.
DR   PANTHER; PTHR24072:SF124; PTHR24072:SF124; 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   SMART; SM00054; EFh; 2.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS51423; MIRO; 2.
PE   2: Evidence at transcript level;
KW   Calcium; GTP-binding; Hydrolase; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion outer membrane; Nucleotide-binding; Reference proteome;
KW   Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..619
FT                   /note="Mitochondrial Rho GTPase 1"
FT                   /id="PRO_0000239315"
FT   TOPO_DOM        1..593
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        594..616
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        617..619
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          2..168
FT                   /note="Miro 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00757"
FT   DOMAIN          184..219
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          304..339
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          417..580
FT                   /note="Miro 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00757"
FT   BINDING         11..18
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         57..61
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         118..121
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         197
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         199
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         201
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         203
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         208
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         317
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         319
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         321
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         328
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         426..433
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         464..468
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         528..531
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   619 AA;  70894 MW;  455212030C3632F4 CRC64;
     MKKDVRILLV GEPRVGKTSL IMSLVSEEFP EEVPPRAEEI TIPADVTPER VPTHIVDYSE
     AEQNDEQLYH EISQANVICI VYAVNNKNSI DKVTSRWIPL INERTDKDSR LPLILVGNKS
     DLVEYSSMET ILPIMNQYTE IETCVECSAK NLKNRSELFY YAQKAVLHPT GPLYCPEEKE
     MKPACIKALT RIFRISDQDN DGTLNDAELN FFQRICFNTP LAPQALEDVK NVVRKNVSDG
     VADNGLTLKG FLFLHTLFIQ RGRHETTWTV LRRFGYDDDL ELTPEYLFPL LKIPPDCTTE
     LNHHAYLFLQ SIFDKHDLDR DCALSPDELK DLFKVFPYMP WGPDVNNTVC TNGKGGWITY
     QGFLSQWTLT TYLDVQRCLE YLGYLGYSIL AEQESQASAI TVTRDKKIDL QKKQTQRNVF
     RCNVVGMKGC GKSGVLQALL GRNLMRQRQI RAEHKSYYAI NTVYVYGQEK YLLLHDVSDS
     EFLTDAETIC DVVCLVYDVS NPKSFEYCVR IFKQHFMDSR IPCLVVAAKS DLHEVRQEYS
     ISPAEFCKKH KMPPPQAFTC NTVDMPSKDI FVKLTTMAMY PHVTQADLKS STFWLRASFG
     ATVFAFLGFA MYKALIKQR
 
 
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