ID   PGTA_RAT                Reviewed;         567 AA.
AC   Q08602;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   24-JAN-2024, entry version 172.
DE   RecName: Full=Geranylgeranyl transferase type-2 subunit alpha;
DE            EC=2.5.1.60;
DE   AltName: Full=Geranylgeranyl transferase type II subunit alpha;
DE   AltName: Full=Rab geranyl-geranyltransferase subunit alpha;
DE            Short=Rab GG transferase alpha;
DE            Short=Rab GGTase alpha;
DE   AltName: Full=Rab geranylgeranyltransferase subunit alpha;
GN   Name=Rabggta; Synonyms=Ggta;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP   SUBUNIT.
RC   TISSUE=Brain;
RX   PubMed=8505342; DOI=10.1016/s0021-9258(19)50329-5;
RA   Armstrong S.A., Seabra M.C., Suedhof T.C., Goldstein J.L., Brown M.S.;
RT   "cDNA cloning and expression of the alpha and beta subunits of rat Rab
RT   geranylgeranyl transferase.";
RL   J. Biol. Chem. 268:12221-12229(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   SUBUNIT.
RX   PubMed=11675392; DOI=10.1074/jbc.m108241200;
RA   Thoma N.H., Iakovenko A., Goody R.S., Alexandrov K.;
RT   "Phosphoisoprenoids modulate association of Rab geranylgeranyltransferase
RT   with REP-1.";
RL   J. Biol. Chem. 276:48637-48643(2001).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH RABGGTB, AND SUBUNIT.
RX   PubMed=10745007; DOI=10.1016/s0969-2126(00)00102-7;
RA   Zhang H., Seabra M.C., Deisenhofer J.;
RT   "Crystal structure of Rab geranylgeranyltransferase at 2.0 A resolution.";
RL   Structure 8:241-251(2000).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH GERANYGERANYL
RP   PHOSPHATE ANALOG; RABGGTB AND CHM/REP1, AND SUBUNIT.
RX   PubMed=12620235; DOI=10.1016/s1097-2765(03)00044-3;
RA   Pylypenko O., Rak A., Reents R., Niculae A., Sidorovitch V., Cioaca M.D.,
RA   Bessolitsyna E., Thomae N.H., Waldmann H., Schlichting I., Goody R.S.,
RA   Alexandrov K.;
RT   "Structure of Rab escort protein-1 in complex with Rab
RT   geranylgeranyltransferase.";
RL   Mol. Cell 11:483-494(2003).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-441 IN COMPLEX WITH INHIBITOR,
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=18399557; DOI=10.1002/anie.200705795;
RA   Guo Z., Wu Y.W., Tan K.T., Bon R.S., Guiu-Rozas E., Delon C., Nguyen T.U.,
RA   Wetzel S., Arndt S., Goody R.S., Blankenfeldt W., Alexandrov K.,
RA   Waldmann H.;
RT   "Development of selective RabGGTase inhibitors and crystal structure of a
RT   RabGGTase-inhibitor complex.";
RL   Angew. Chem. Int. Ed. Engl. 47:3747-3750(2008).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-441, FUNCTION, CATALYTIC
RP   ACTIVITY, AND SUBUNIT.
RX   PubMed=18756270; DOI=10.1038/emboj.2008.164;
RA   Guo Z., Wu Y.W., Das D., Delon C., Cramer J., Yu S., Thuns S., Lupilova N.,
RA   Waldmann H., Brunsveld L., Goody R.S., Alexandrov K., Blankenfeldt W.;
RT   "Structures of RabGGTase-substrate/product complexes provide insights into
RT   the evolution of protein prenylation.";
RL   EMBO J. 27:2444-2456(2008).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-441, FUNCTION, CATALYTIC
RP   ACTIVITY, AND SUBUNIT.
RX   PubMed=19894725; DOI=10.1021/jm901117d;
RA   Tan K.T., Guiu-Rozas E., Bon R.S., Guo Z., Delon C., Wetzel S., Arndt S.,
RA   Alexandrov K., Waldmann H., Goody R.S., Wu Y.W., Blankenfeldt W.;
RT   "Design, synthesis, and characterization of peptide-based rab
RT   geranylgeranyl transferase inhibitors.";
RL   J. Med. Chem. 52:8025-8037(2009).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-441, FUNCTION, CATALYTIC
RP   ACTIVITY, AND SUBUNIT.
RX   PubMed=21520375; DOI=10.1002/anie.201101210;
RA   Bon R.S., Guo Z., Stigter E.A., Wetzel S., Menninger S., Wolf A.,
RA   Choidas A., Alexandrov K., Blankenfeldt W., Goody R.S., Waldmann H.;
RT   "Structure-guided development of selective RabGGTase inhibitors.";
RL   Angew. Chem. Int. Ed. Engl. 50:4957-4961(2011).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-441, FUNCTION, CATALYTIC
RP   ACTIVITY, AND SUBUNIT.
RX   PubMed=22963166; DOI=10.1021/jm300624s;
RA   Stigter E.A., Guo Z., Bon R.S., Wu Y.W., Choidas A., Wolf A., Menninger S.,
RA   Waldmann H., Blankenfeldt W., Goody R.S.;
RT   "Development of selective, potent RabGGTase inhibitors.";
RL   J. Med. Chem. 55:8330-8340(2012).
CC   -!- FUNCTION: Catalyzes the transfer of a geranylgeranyl moiety from
CC       geranylgeranyl diphosphate to both cysteines of Rab proteins with the
CC       C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A
CC       and RAB7A. {ECO:0000269|PubMed:18399557, ECO:0000269|PubMed:18756270,
CC       ECO:0000269|PubMed:19894725, ECO:0000269|PubMed:21520375,
CC       ECO:0000269|PubMed:22963166, ECO:0000269|PubMed:8505342}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] =
CC         diphosphate + S-geranylgeranyl-L-cysteinyl-[protein];
CC         Xref=Rhea:RHEA:21240, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11537,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533,
CC         ChEBI:CHEBI:86021; EC=2.5.1.60;
CC         Evidence={ECO:0000269|PubMed:18756270, ECO:0000269|PubMed:19894725,
CC         ECO:0000269|PubMed:21520375, ECO:0000269|PubMed:22963166};
CC   -!- ACTIVITY REGULATION: The enzymatic reaction requires the aid of a Rab
CC       escort protein (also called component A), such as CHM.
CC   -!- SUBUNIT: Heterotrimer composed of RABGGTA, RABGGTB and CHM; within this
CC       trimer, RABGGTA and RABGGTB form the catalytic component B, while CHM
CC       (component A) mediates peptide substrate binding (PubMed:11675392,
CC       PubMed:10745007, PubMed:12620235, PubMed:18399557, PubMed:18756270,
CC       PubMed:19894725, PubMed:21520375, PubMed:22963166, PubMed:8505342). The
CC       Rab GGTase dimer (RGGT) interacts with CHM (component A) prior to Rab
CC       protein binding; the association is stabilized by geranylgeranyl
CC       pyrophosphate (GGpp) (PubMed:12620235). The CHM:RGGT:Rab complex is
CC       destabilized by GGpp (PubMed:12620235). Interacts with non-
CC       phosphorylated form of RAB8A; phosphorylation of RAB8A at 'Thr-72'
CC       disrupts this interaction (By similarity).
CC       {ECO:0000250|UniProtKB:Q92696, ECO:0000269|PubMed:10745007,
CC       ECO:0000269|PubMed:11675392, ECO:0000269|PubMed:12620235,
CC       ECO:0000269|PubMed:18399557, ECO:0000269|PubMed:18756270,
CC       ECO:0000269|PubMed:19894725, ECO:0000269|PubMed:21520375,
CC       ECO:0000269|PubMed:22963166, ECO:0000269|PubMed:8505342}.
CC   -!- TISSUE SPECIFICITY: Most abundant in the heart, brain, spleen and
CC       liver. Less in the lung, muscle, kidney and testis; in these tissues
CC       less abundant than the beta subunit.
CC   -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
CC       family. {ECO:0000305}.
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DR   EMBL; L10415; AAA41998.1; -; mRNA.
DR   EMBL; S62096; AAB27018.1; -; mRNA.
DR   EMBL; BC086547; AAH86547.1; -; mRNA.
DR   PIR; A45977; A45977.
DR   RefSeq; NP_113842.1; NM_031654.2.
DR   RefSeq; XP_006252071.1; XM_006252009.3.
DR   RefSeq; XP_006252072.1; XM_006252010.3.
DR   PDB; 1DCE; X-ray; 2.00 A; A/C=1-567.
DR   PDB; 1LTX; X-ray; 2.70 A; A=1-567.
DR   PDB; 3C72; X-ray; 2.30 A; A=1-236, A=353-441.
DR   PDB; 3DSS; X-ray; 1.80 A; A=1-237, A=353-441.
DR   PDB; 3DST; X-ray; 1.90 A; A=1-237, A=353-441.
DR   PDB; 3DSU; X-ray; 1.90 A; A=1-237, A=353-441.
DR   PDB; 3DSV; X-ray; 2.10 A; A=1-237, A=353-441.
DR   PDB; 3DSW; X-ray; 2.15 A; A=1-237, A=353-441.
DR   PDB; 3DSX; X-ray; 2.10 A; A=1-237, A=353-441.
DR   PDB; 3HXB; X-ray; 2.25 A; A=1-237, A=353-441.
DR   PDB; 3HXC; X-ray; 1.95 A; A=1-237, A=353-441.
DR   PDB; 3HXD; X-ray; 1.95 A; A=1-237, A=353-441.
DR   PDB; 3HXE; X-ray; 1.95 A; A=1-237, A=353-441.
DR   PDB; 3HXF; X-ray; 1.90 A; A=1-237, A=353-441.
DR   PDB; 3PZ1; X-ray; 1.95 A; A=1-237, A=353-441.
DR   PDB; 3PZ2; X-ray; 2.35 A; A=1-237, A=353-441.
DR   PDB; 3PZ3; X-ray; 2.00 A; A=1-237, A=353-441.
DR   PDB; 4EHM; X-ray; 2.20 A; A=1-237, A=353-441.
DR   PDB; 4GTS; X-ray; 2.45 A; A=1-237, A=353-441.
DR   PDB; 4GTT; X-ray; 2.05 A; A=1-237, A=353-441.
DR   PDB; 4GTV; X-ray; 1.95 A; A=1-237, A=353-441.
DR   PDBsum; 1DCE; -.
DR   PDBsum; 1LTX; -.
DR   PDBsum; 3C72; -.
DR   PDBsum; 3DSS; -.
DR   PDBsum; 3DST; -.
DR   PDBsum; 3DSU; -.
DR   PDBsum; 3DSV; -.
DR   PDBsum; 3DSW; -.
DR   PDBsum; 3DSX; -.
DR   PDBsum; 3HXB; -.
DR   PDBsum; 3HXC; -.
DR   PDBsum; 3HXD; -.
DR   PDBsum; 3HXE; -.
DR   PDBsum; 3HXF; -.
DR   PDBsum; 3PZ1; -.
DR   PDBsum; 3PZ2; -.
DR   PDBsum; 3PZ3; -.
DR   PDBsum; 4EHM; -.
DR   PDBsum; 4GTS; -.
DR   PDBsum; 4GTT; -.
DR   PDBsum; 4GTV; -.
DR   AlphaFoldDB; Q08602; -.
DR   SMR; Q08602; -.
DR   BioGRID; 248714; 3.
DR   ComplexPortal; CPX-2249; Protein geranylgeranyltransferase type II complex.
DR   DIP; DIP-6137N; -.
DR   IntAct; Q08602; 1.
DR   STRING; 10116.ENSRNOP00000049261; -.
DR   BindingDB; Q08602; -.
DR   ChEMBL; CHEMBL4523995; -.
DR   PhosphoSitePlus; Q08602; -.
DR   jPOST; Q08602; -.
DR   PaxDb; 10116-ENSRNOP00000049261; -.
DR   GeneID; 58983; -.
DR   KEGG; rno:58983; -.
DR   UCSC; RGD:621697; rat.
DR   AGR; RGD:621697; -.
DR   CTD; 5875; -.
DR   RGD; 621697; Rabggta.
DR   VEuPathDB; HostDB:ENSRNOG00000030483; -.
DR   eggNOG; KOG0529; Eukaryota.
DR   HOGENOM; CLU_031996_3_2_1; -.
DR   InParanoid; Q08602; -.
DR   OrthoDB; 5489560at2759; -.
DR   PhylomeDB; Q08602; -.
DR   TreeFam; TF315057; -.
DR   Reactome; R-RNO-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
DR   Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR   EvolutionaryTrace; Q08602; -.
DR   PRO; PR:Q08602; -.
DR   Proteomes; UP000002494; Chromosome 15.
DR   Bgee; ENSRNOG00000030483; Expressed in skeletal muscle tissue and 20 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IDA:UniProtKB.
DR   GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0018344; P:protein geranylgeranylation; IDA:UniProtKB.
DR   Gene3D; 1.25.40.120; Protein prenylyltransferase; 1.
DR   Gene3D; 2.60.40.1130; Rab geranylgeranyltransferase alpha-subunit, insert domain; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR002088; Prenyl_trans_a.
DR   InterPro; IPR036254; RabGGT_asu_insert-dom_sf.
DR   InterPro; IPR009087; RabGGT_asu_insert-domain.
DR   PANTHER; PTHR11129:SF2; GERANYLGERANYL TRANSFERASE TYPE-2 SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR11129; PROTEIN FARNESYLTRANSFERASE ALPHA SUBUNIT/RAB GERANYLGERANYL TRANSFERASE ALPHA SUBUNIT; 1.
DR   Pfam; PF01239; PPTA; 5.
DR   Pfam; PF07711; RabGGT_insert; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF48439; Protein prenylyltransferase; 1.
DR   SUPFAM; SSF49594; Rab geranylgeranyltransferase alpha-subunit, insert domain; 1.
DR   PROSITE; PS51147; PFTA; 6.
DR   Genevisible; Q08602; RN.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Leucine-rich repeat;
KW   Phosphoprotein; Prenyltransferase; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..567
FT                   /note="Geranylgeranyl transferase type-2 subunit alpha"
FT                   /id="PRO_0000119759"
FT   REPEAT          44..78
FT                   /note="PFTA 1"
FT   REPEAT          88..122
FT                   /note="PFTA 2"
FT   REPEAT          124..158
FT                   /note="PFTA 3"
FT   REPEAT          159..193
FT                   /note="PFTA 4"
FT   REPEAT          207..241
FT                   /note="PFTA 5"
FT   REPEAT          363..397
FT                   /note="PFTA 6"
FT   REPEAT          442..463
FT                   /note="LRR 1"
FT   REPEAT          464..486
FT                   /note="LRR 2"
FT   REPEAT          487..508
FT                   /note="LRR 3"
FT   REPEAT          509..530
FT                   /note="LRR 4"
FT   REPEAT          534..555
FT                   /note="LRR 5"
FT   MOD_RES         98
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JHK4"
FT   CONFLICT        169
FT                   /note="S -> D (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        227
FT                   /note="S -> Q (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           13..40
FT                   /evidence="ECO:0007829|PDB:3DSS"
FT   HELIX           46..56
FT                   /evidence="ECO:0007829|PDB:3DSS"
FT   HELIX           63..79
FT                   /evidence="ECO:0007829|PDB:3DSS"
FT   HELIX           82..102
FT                   /evidence="ECO:0007829|PDB:3DSS"
FT   HELIX           107..119
FT                   /evidence="ECO:0007829|PDB:3DSS"
FT   STRAND          120..122
FT                   /evidence="ECO:0007829|PDB:3C72"
FT   HELIX           125..138
FT                   /evidence="ECO:0007829|PDB:3DSS"
FT   HELIX           143..155
FT                   /evidence="ECO:0007829|PDB:3DSS"
FT   HELIX           160..173
FT                   /evidence="ECO:0007829|PDB:3DSS"
FT   HELIX           178..191
FT                   /evidence="ECO:0007829|PDB:3DSS"
FT   STRAND          197..199
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   HELIX           205..221
FT                   /evidence="ECO:0007829|PDB:3DSS"
FT   HELIX           226..237
FT                   /evidence="ECO:0007829|PDB:3DSS"
FT   STRAND          245..251
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   TURN            252..255
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   STRAND          256..265
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   STRAND          267..269
FT                   /evidence="ECO:0007829|PDB:1LTX"
FT   STRAND          274..283
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   STRAND          296..303
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   HELIX           306..308
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   STRAND          313..322
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   TURN            323..326
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   STRAND          327..334
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   STRAND          338..343
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   TURN            347..350
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   HELIX           353..355
FT                   /evidence="ECO:0007829|PDB:3DSS"
FT   HELIX           358..377
FT                   /evidence="ECO:0007829|PDB:3DSS"
FT   HELIX           382..395
FT                   /evidence="ECO:0007829|PDB:3DSS"
FT   TURN            397..400
FT                   /evidence="ECO:0007829|PDB:3DSS"
FT   HELIX           401..414
FT                   /evidence="ECO:0007829|PDB:3DSS"
FT   HELIX           416..418
FT                   /evidence="ECO:0007829|PDB:3DSS"
FT   HELIX           419..438
FT                   /evidence="ECO:0007829|PDB:3DSS"
FT   STRAND          444..447
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   HELIX           459..462
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   STRAND          467..469
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   HELIX           480..484
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   STRAND          490..492
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   HELIX           502..504
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   STRAND          512..514
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   STRAND          522..524
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   HELIX           527..531
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   STRAND          537..539
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   HELIX           544..547
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   STRAND          548..550
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   HELIX           554..558
FT                   /evidence="ECO:0007829|PDB:1DCE"
FT   STRAND          563..566
FT                   /evidence="ECO:0007829|PDB:1DCE"
SQ   SEQUENCE   567 AA;  64904 MW;  1F9D235F973EABD5 CRC64;
     MHGRLKVKTS EEQAEAKRLE REQKLKLYQS ATQAVFQKRQ AGELDESVLE LTSQILGANP
     DFATLWNCRR EVLQHLETEK SPEESAALVK AELGFLESCL RVNPKSYGTW HHRCWLLSRL
     PEPNWARELE LCARFLEADE RNFHCWDYRR FVAAQAAVAP AEELAFTDSL ITRNFSNYSS
     WHYRSCLLPQ LHPQPDSGPQ GRLPENVLLK ELELVQNAFF TDPNDQSAWF YHRWLLGRAE
     PHDVLCCVHV SREEACLSVC FSRPLTVGSR MGTLLLMVDE APLSVEWRTP DGRNRPSHVW
     LCDLPAASLN DQLPQHTFRV IWTGSDSQKE CVLLKDRPEC WCRDSATDEQ LFRCELSVEK
     STVLQSELES CKELQELEPE NKWCLLTIIL LMRALDPLLY EKETLQYFST LKAVDPMRAA
     YLDDLRSKFL LENSVLKMEY ADVRVLHLAH KDLTVLCHLE QLLLVTHLDL SHNRLRALPP
     ALAALRCLEV LQASDNALEN VDGVANLPRL QELLLCNNRL QQSAAIQPLV SCPRLVLLNL
     QGNSLCQEEG IQERLAEMLP SVSSILT
//