ID G3SLV6_LOXAF Unreviewed; 653 AA.
AC G3SLV6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Rab proteins geranylgeranyltransferase component A {ECO:0000256|PIRNR:PIRNR016550};
GN Name=CHM {ECO:0000313|Ensembl:ENSLAFP00000000437.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000000437.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000000437.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000000437.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000000437.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000000437.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Substrate-binding subunit (component A) of the Rab
CC geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab
CC proteins and presents the substrate peptide to the catalytic component
CC B. The component A is thought to be regenerated by transferring its
CC prenylated Rab back to the donor membrane.
CC {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 RefSeq; XP_010590997.1; XM_010592695.1.
DR AlphaFoldDB; G3SLV6; -.
DR STRING; 9785.ENSLAFP00000000437; -.
DR Ensembl; ENSLAFT00000000522.3; ENSLAFP00000000437.3; ENSLAFG00000000523.3.
DR GeneID; 100673876; -.
DR KEGG; lav:100673876; -.
DR CTD; 1121; -.
DR eggNOG; KOG4405; Eukaryota.
DR GeneTree; ENSGT00950000182994; -.
DR HOGENOM; CLU_021695_4_1_1; -.
DR InParanoid; G3SLV6; -.
DR OMA; LDQNDYY; -.
DR OrthoDB; 197300at2759; -.
DR TreeFam; TF320813; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006612; P:protein targeting to membrane; IEA:Ensembl.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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:SF12; RAB PROTEINS GERANYLGERANYLTRANSFERASE COMPONENT A 1; 1.
DR Pfam; PF00996; GDI; 2.
DR PIRSF; PIRSF016550; Rab_ger_ger_transf_A_euk; 1.
DR PRINTS; PR00893; RABESCORT.
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:UP000007646}.
FT REGION 148..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 653 AA; 73081 MW; A3F4BE15EFD81D80 CRC64;
MANNLPSEFD VIVIGTGLPE SVIAAACSRS GQRVLHVDSR SYYGGNWASF SFSGLLSWLK
EHQESSDAVN ESPTWQEQIL ENEEAIALSK KDRTIQHVEV FCYASQDLHE DVEEAGALQK
NRAPLTAVNP TEAADSVFLP KEDESLSTVS CEIPAEQPPS SNPESAPEVN DVEAVEEKEN
DGNDKTCVQA TSEKETGENV PTAENTAEQP KKNRITYSQI VKEGRRFNID LVSKLLYSRG
LLIELLIKSN VSRYAEFKNV TRILAFRDGR VEQVPCSRAD VFNSKQLTMV EKRMLMKFLT
FCMDYEEHPD EYKAYEEMTF SEYLKTQKLT PNLQYFVLHS IAMTSEATST TIDGLKATKN
FLRCLGRYGN TPFLFPLYGQ GELPQCFCRM CAVFGGIYCL HHSVQCLVVD KDSGKCKAII
DQFGQRIISK HFIVEDSYFS EKTCSNVQYR QISRAVLITD RSVLKADSDQ QISILTVPAS
KPGTFAVRVI ELCSSTMTCM KGTYLVHLTC TSSKTAREDL EPVVQELFTP YTETEIENDE
GKKPRLLWAL YFNMRDSSDI SRNSYNDLSS NIYICSGPDC GLGNDNAVKQ AEALFQQICP
NEDFCPPPPN PEDIVLDGDS LQPEPSESSS ILQTNSETPK ESPYLGNQEE PSE
//
