ID L5JSL7_PTEAL Unreviewed; 650 AA.
AC L5JSL7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Rab proteins geranylgeranyltransferase component A {ECO:0000256|PIRNR:PIRNR016550};
GN ORFNames=PAL_GLEAN10002485 {ECO:0000313|EMBL:ELK02295.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK02295.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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 EMBL; KB031136; ELK02295.1; -; Genomic_DNA.
DR RefSeq; XP_006924180.1; XM_006924118.2.
DR AlphaFoldDB; L5JSL7; -.
DR STRING; 9402.L5JSL7; -.
DR GeneID; 102881079; -.
DR KEGG; pale:102881079; -.
DR CTD; 1122; -.
DR eggNOG; KOG4405; Eukaryota.
DR InParanoid; L5JSL7; -.
DR OrthoDB; 197300at2759; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
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:SF9; RAB PROTEINS GERANYLGERANYLTRANSFERASE COMPONENT A 2; 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:UP000010552};
KW Transferase {ECO:0000313|EMBL:ELK02295.1}.
SQ SEQUENCE 650 AA; 73076 MW; D2192DFF69041439 CRC64;
MADTLPTEFD VVIIGTGLPE SILAAACSRS GQRVLHIDSR SYYGGNWASF TFSGLLSWLK
EYQQTSDIED KSTTAWQDLI DDTEEAITLR RKDETIQHTE VFCYASQDMD DSTKKVDALQ
KNPSCVVHGT LTTPLDSACL SEETHMTSCK VPAEDTPKNE GEVLLEATNI EETQAKEKCK
DKTCTHTISD RDEDENRSVV EDSAERPKRN RVTYSQIVKE GRRFNIDLVS KLLYSQGLLI
DLLIKSNVSR YAEFKNVTRI LAFREGKVEQ VPCSRADVFN SKELTMVEKR MLMKFLTFCL
DYEQHPDEYQ DFTQCSFSEY LKTKKLTPNL QHFVLYSIAM TESSCTTVDG LKAAKNFLRC
LGRFGNTPFL FPLYGQGEIP QGFCRMCAVF GGIYCLRHKV QCLVIDRESG RCKAIIDHFG
QRISAKHFIV EDSYLSEETC SDVQYKQISR AVLITDQSLL QADSDQQISI LIVPPTEPGA
HAVRVTELCS STMTCMKDTY LVHLTCTSSK TAREDLESVV KKLFTPYAET EKDKEELAKP
RLLWALYFTM RDSSGISRSS YCGLPSNVYV CSGPDCGLGN EHAVQQAETL FQEIFPGEEF
CPPPPNPEDI IFDGDDKQPE ASGTNNIVMA KLESSEGSKN LESPGKHLQN
//
