ID A0A087H7L3_ARAAL Unreviewed; 549 AA.
AC A0A087H7L3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Rab escort protein 1 {ECO:0000256|PIRNR:PIRNR016550};
GN OrderedLocusNames=AALP_Aa3g071400 {ECO:0000313|EMBL:KFK38115.1};
OS Arabis alpina (Alpine rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK38115.1, ECO:0000313|Proteomes:UP000029120};
RN [1] {ECO:0000313|Proteomes:UP000029120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120};
RX PubMed=27246759; DOI=10.1038/nplants.2014.23;
RA Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V.,
RA Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B.,
RA Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L.,
RA Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L.,
RA Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R.,
RA Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F.,
RA Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H.,
RA Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.;
RT "Genome expansion of Arabis alpina linked with retrotransposition and
RT reduced symmetric DNA methylation.";
RL Nat. Plants 1:14023-14023(2015).
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; CM002871; KFK38115.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087H7L3; -.
DR EnsemblPlants; KFK38115; KFK38115; AALP_AA3G071400.
DR Gramene; KFK38115; KFK38115; AALP_AA3G071400.
DR eggNOG; KOG4405; Eukaryota.
DR OMA; LDQNDYY; -.
DR OrthoDB; 197300at2759; -.
DR Proteomes; UP000029120; Chromosome 3.
DR GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IEA:UniProtKB-UniRule.
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:0004663; F:Rab geranylgeranyltransferase activity; IEA:EnsemblPlants.
DR GO; GO:0031267; F:small GTPase binding; IEA:EnsemblPlants.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0009846; P:pollen germination; IEA:EnsemblPlants.
DR GO; GO:0010152; P:pollen maturation; IEA:EnsemblPlants.
DR GO; GO:0009860; P:pollen tube growth; IEA:EnsemblPlants.
DR GO; GO:2000541; P:positive regulation of protein geranylgeranylation; IEA:EnsemblPlants.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:UniProtKB-UniRule.
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; IPR017230; Mrs6.
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 PRINTS; PR00894; YEASTMRS6P.
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:UP000029120}.
FT REGION 524..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 549 AA; 60199 MW; 14B3B17AF3DE8E0C CRC64;
MPDLPPYPPL DPTNYDLIIV GTGVSESIFA AAASSSGSSV LHLDPNPFYG SHFASLSLPD
LTSFLQSNSV SPPPPPPQSS HDFLSVDLVN RSLYSSVEIS SFEPEILEEQ HSRKFNVDLC
GPRAIFCSDE SINLMLKSGS NNYVEFKSVD SSFVGDSCGE LRNVPDSRGA IFKDKSLTLL
EKNQLMKFFK LVQQHLASTS ETTDEATVRI SEKDMETPFV EFLTKMRLPP KIKSIILYAI
AMLDYDQENI ETCRDLLKTK EGIDRLALYI TSIGRFSNAF GAMIYPIYGQ GELPQAFCRR
AAVKGCIYVL RMPVTALLLD KETGAYKGVR LASGQEIFSQ KLILDPSITV GLESLSSSLT
DQQKETLRVL VPKAISSKGK IARGICIIRG SVKAKTSSAL IVYPPKSLFP EQQTAIRVLQ
LGSGLAACPA EMHVLYLSTL CDNDEQGKTA LLSAMTTLIK PPVPENDTVD AKPVVLWRAL
YVQEMVKGEF GGTISSAASP DGNFSYNEIV ESAKKLYEQV MGSEELFKEE TSPEKTMEEE
NDGGLEIED
//
