ID A0A078GHA6_BRANA Unreviewed; 566 AA.
AC A0A078GHA6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Rab escort protein 1 {ECO:0000256|PIRNR:PIRNR016550};
GN Name=BnaA05g30830D {ECO:0000313|EMBL:CDY24684.1};
GN ORFNames=GSBRNA2T00027065001 {ECO:0000313|EMBL:CDY24684.1};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY24684.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY24684.1, ECO:0000313|Proteomes:UP000028999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX PubMed=25146293; DOI=10.1126/science.1253435;
RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT Brassica napus oilseed genome.";
RL Science 345:950-953(2014).
CC -!- FUNCTION: Substrate-binding subunit of the Rab
CC geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab
CC proteins. {ECO:0000256|PIRNR:PIRNR016550}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR016550}.
CC -!- SIMILARITY: Belongs to the Rab GDI family.
CC {ECO:0000256|ARBA:ARBA00005593, ECO:0000256|PIRNR:PIRNR016550}.
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DR EMBL; LK032162; CDY24684.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078GHA6; -.
DR STRING; 3708.A0A078GHA6; -.
DR PaxDb; 3708-A0A078GHA6; -.
DR EnsemblPlants; CDY24684; CDY24684; GSBRNA2T00027065001.
DR Gramene; CDY24684; CDY24684; GSBRNA2T00027065001.
DR OMA; LMKFLTA; -.
DR Proteomes; UP000028999; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IBA:GO_Central.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:UniProtKB-UniRule.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR Gene3D; 3.30.519.10; Guanine Nucleotide Dissociation Inhibitor, domain 2; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR018203; GDP_dissociation_inhibitor.
DR InterPro; IPR001738; Rab_escort.
DR PANTHER; PTHR11787; RAB GDP-DISSOCIATION INHIBITOR; 1.
DR PANTHER; PTHR11787:SF4; RAB PROTEINS GERANYLGERANYLTRANSFERASE COMPONENT A; 1.
DR Pfam; PF00996; GDI; 2.
DR PIRSF; PIRSF016550; Rab_ger_ger_transf_A_euk; 2.
DR PRINTS; PR00891; RABGDIREP.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR016550};
KW GTPase activation {ECO:0000256|PIRNR:PIRNR016550};
KW Reference proteome {ECO:0000313|Proteomes:UP000028999}.
FT REGION 541..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..566
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 566 AA; 60827 MW; 2F3E0304A81B1647 CRC64;
MSDLPPYPPL DPTTYDLIIV GTGVSESILS AAASSSGTSV LHLDPNPFYG SHSASLSLPD
LTSFLHSNSL SPPPPPPSDT PDFLSVDLAT RSLYSSVEIA TFDSSILDER HSRKFNVDLC
GPRVLFCADE SINLMLKSGS NNYVEFKSVD ASFVGDSSGE LRSVPDSRAA IFKDKSLGLM
EKKQLMKFFK LVQAHLAAAA ASSTESDEGA VKIAEEDMES PFVDFLAKMP LPPKIKSIIL
YGIAMVDYDQ DNVEACGDLL KTREGIARLA LYITSIGRFS NALGALIYPI YGQGELPQAF
CRRAAVKGCI YVLRMPITAL LLDKASELIE TGGYKGVRLA TGQEIFSQKL ILDPCITVGS
ESMSSLTDQQ KETLRVLVPK SISSEGKIAR GICIIRGSVK ADISNALVVY PPKSLFPEQL
AAIRVLQLGS GLAVCPADMH VLYFSTVCEN DDQGKAALLS AMSTLIKPQV PENLQSDSAV
ENDTAEAAKP VVLWRALYVQ AMVKGEFGGS ISSAASPDGN LSYNELVESA VKLYEQLMGS
EELFKEETSP DNTTEEENDG GVEIEA
//
