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Geranylgeranyl transferase type-2 subunit alpha (EC 2.5.1.60) (Geranylgeranyl transferase type II subunit alpha) (Rab geranyl-geranyltransferase subunit alpha) (Rab GG transferase alpha) (Rab GGTase alpha) (Rab geranylgeranyltransferase subunit alpha)

 PGTA_RAT                Reviewed;         567 AA.
Q08602;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
07-NOV-2018, entry version 147.
RecName: Full=Geranylgeranyl transferase type-2 subunit alpha;
EC=2.5.1.60;
AltName: Full=Geranylgeranyl transferase type II subunit alpha;
AltName: Full=Rab geranyl-geranyltransferase subunit alpha;
Short=Rab GG transferase alpha;
Short=Rab GGTase alpha;
AltName: Full=Rab geranylgeranyltransferase subunit alpha;
Name=Rabggta; Synonyms=Ggta;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
SUBUNIT.
TISSUE=Brain;
PubMed=8505342;
Armstrong S.A., Seabra M.C., Suedhof T.C., Goldstein J.L., Brown M.S.;
"cDNA cloning and expression of the alpha and beta subunits of rat Rab
geranylgeranyl transferase.";
J. Biol. Chem. 268:12221-12229(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
SUBUNIT.
PubMed=11675392; DOI=10.1074/jbc.M108241200;
Thoma N.H., Iakovenko A., Goody R.S., Alexandrov K.;
"Phosphoisoprenoids modulate association of Rab
geranylgeranyltransferase with REP-1.";
J. Biol. Chem. 276:48637-48643(2001).
[4]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH RABGGTB, AND
SUBUNIT.
PubMed=10745007; DOI=10.1016/S0969-2126(00)00102-7;
Zhang H., Seabra M.C., Deisenhofer J.;
"Crystal structure of Rab geranylgeranyltransferase at 2.0 A
resolution.";
Structure 8:241-251(2000).
[5]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH GERANYGERANYL
PHOSPHATE ANALOG; RABGGTB AND CHM/REP1, AND SUBUNIT.
PubMed=12620235; DOI=10.1016/S1097-2765(03)00044-3;
Pylypenko O., Rak A., Reents R., Niculae A., Sidorovitch V.,
Cioaca M.D., Bessolitsyna E., Thomae N.H., Waldmann H.,
Schlichting I., Goody R.S., Alexandrov K.;
"Structure of Rab escort protein-1 in complex with Rab
geranylgeranyltransferase.";
Mol. Cell 11:483-494(2003).
[6]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-441 IN COMPLEX WITH
INHIBITOR, FUNCTION, AND SUBUNIT.
PubMed=18399557; DOI=10.1002/anie.200705795;
Guo Z., Wu Y.W., Tan K.T., Bon R.S., Guiu-Rozas E., Delon C.,
Nguyen T.U., Wetzel S., Arndt S., Goody R.S., Blankenfeldt W.,
Alexandrov K., Waldmann H.;
"Development of selective RabGGTase inhibitors and crystal structure
of a RabGGTase-inhibitor complex.";
Angew. Chem. Int. Ed. Engl. 47:3747-3750(2008).
[7]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-441, FUNCTION, CATALYTIC
ACTIVITY, AND SUBUNIT.
PubMed=18756270; DOI=10.1038/emboj.2008.164;
Guo Z., Wu Y.W., Das D., Delon C., Cramer J., Yu S., Thuns S.,
Lupilova N., Waldmann H., Brunsveld L., Goody R.S., Alexandrov K.,
Blankenfeldt W.;
"Structures of RabGGTase-substrate/product complexes provide insights
into the evolution of protein prenylation.";
EMBO J. 27:2444-2456(2008).
[8]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-441, FUNCTION, CATALYTIC
ACTIVITY, AND SUBUNIT.
PubMed=19894725; DOI=10.1021/jm901117d;
Tan K.T., Guiu-Rozas E., Bon R.S., Guo Z., Delon C., Wetzel S.,
Arndt S., Alexandrov K., Waldmann H., Goody R.S., Wu Y.W.,
Blankenfeldt W.;
"Design, synthesis, and characterization of peptide-based rab
geranylgeranyl transferase inhibitors.";
J. Med. Chem. 52:8025-8037(2009).
[9]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-441, FUNCTION, CATALYTIC
ACTIVITY, AND SUBUNIT.
PubMed=21520375; DOI=10.1002/anie.201101210;
Bon R.S., Guo Z., Stigter E.A., Wetzel S., Menninger S., Wolf A.,
Choidas A., Alexandrov K., Blankenfeldt W., Goody R.S., Waldmann H.;
"Structure-guided development of selective RabGGTase inhibitors.";
Angew. Chem. Int. Ed. Engl. 50:4957-4961(2011).
[10]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-441, FUNCTION, CATALYTIC
ACTIVITY, AND SUBUNIT.
PubMed=22963166; DOI=10.1021/jm300624s;
Stigter E.A., Guo Z., Bon R.S., Wu Y.W., Choidas A., Wolf A.,
Menninger S., Waldmann H., Blankenfeldt W., Goody R.S.;
"Development of selective, potent RabGGTase inhibitors.";
J. Med. Chem. 55:8330-8340(2012).
-!- FUNCTION: Catalyzes the transfer of a geranylgeranyl moiety from
geranylgeranyl diphosphate to both cysteines of Rab proteins with
the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A,
RAB3A, RAB5A and RAB7A. {ECO:0000269|PubMed:18399557,
ECO:0000269|PubMed:18756270, ECO:0000269|PubMed:19894725,
ECO:0000269|PubMed:21520375, ECO:0000269|PubMed:22963166,
ECO:0000269|PubMed:8505342}.
-!- CATALYTIC ACTIVITY: Geranylgeranyl diphosphate + protein-cysteine
= S-geranylgeranyl-protein + diphosphate.
{ECO:0000269|PubMed:18756270, ECO:0000269|PubMed:19894725,
ECO:0000269|PubMed:21520375, ECO:0000269|PubMed:22963166}.
-!- ACTIVITY REGULATION: The enzymatic reaction requires the aid of a
Rab escort protein (also called component A), such as CHM.
-!- SUBUNIT: Heterotrimer composed of RABGGTA, RABGGTB and CHM; within
this trimer, RABGGTA and RABGGTB form the catalytic component B,
while CHM (component A) mediates peptide substrate binding. The
Rab GGTase dimer (RGGT) interacts with CHM (component A) prior to
Rab protein binding; the association is stabilized by
geranylgeranyl pyrophosphate (GGpp). The CHM:RGGT:Rab complex is
destabilized by GGpp. {ECO:0000269|PubMed:10745007,
ECO:0000269|PubMed:11675392, ECO:0000269|PubMed:12620235,
ECO:0000269|PubMed:18399557, ECO:0000269|PubMed:18756270,
ECO:0000269|PubMed:19894725, ECO:0000269|PubMed:21520375,
ECO:0000269|PubMed:22963166, ECO:0000269|PubMed:8505342}.
-!- TISSUE SPECIFICITY: Most abundant in the heart, brain, spleen and
liver. Less in the lung, muscle, kidney and testis; in these
tissues less abundant than the beta subunit.
-!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L10415; AAA41998.1; -; mRNA.
EMBL; S62096; AAB27018.1; -; mRNA.
EMBL; BC086547; AAH86547.1; -; mRNA.
PIR; A45977; A45977.
RefSeq; NP_113842.1; NM_031654.2.
RefSeq; XP_006252071.1; XM_006252009.3.
RefSeq; XP_006252072.1; XM_006252010.3.
UniGene; Rn.29434; -.
PDB; 1DCE; X-ray; 2.00 A; A/C=1-567.
PDB; 1LTX; X-ray; 2.70 A; A=1-567.
PDB; 3C72; X-ray; 2.30 A; A=1-236, A=353-441.
PDB; 3DSS; X-ray; 1.80 A; A=1-237, A=353-441.
PDB; 3DST; X-ray; 1.90 A; A=1-237, A=353-441.
PDB; 3DSU; X-ray; 1.90 A; A=1-237, A=353-441.
PDB; 3DSV; X-ray; 2.10 A; A=1-237, A=353-441.
PDB; 3DSW; X-ray; 2.15 A; A=1-237, A=353-441.
PDB; 3DSX; X-ray; 2.10 A; A=1-237, A=353-441.
PDB; 3HXB; X-ray; 2.25 A; A=1-237, A=353-441.
PDB; 3HXC; X-ray; 1.95 A; A=1-237, A=353-441.
PDB; 3HXD; X-ray; 1.95 A; A=1-237, A=353-441.
PDB; 3HXE; X-ray; 1.95 A; A=1-237, A=353-441.
PDB; 3HXF; X-ray; 1.90 A; A=1-237, A=353-441.
PDB; 3PZ1; X-ray; 1.95 A; A=1-237, A=353-441.
PDB; 3PZ2; X-ray; 2.35 A; A=1-237, A=353-441.
PDB; 3PZ3; X-ray; 2.00 A; A=1-237, A=353-441.
PDB; 4EHM; X-ray; 2.20 A; A=1-237, A=353-441.
PDB; 4GTS; X-ray; 2.45 A; A=1-237, A=353-441.
PDB; 4GTT; X-ray; 2.05 A; A=1-237, A=353-441.
PDB; 4GTV; X-ray; 1.95 A; A=1-237, A=353-441.
PDBsum; 1DCE; -.
PDBsum; 1LTX; -.
PDBsum; 3C72; -.
PDBsum; 3DSS; -.
PDBsum; 3DST; -.
PDBsum; 3DSU; -.
PDBsum; 3DSV; -.
PDBsum; 3DSW; -.
PDBsum; 3DSX; -.
PDBsum; 3HXB; -.
PDBsum; 3HXC; -.
PDBsum; 3HXD; -.
PDBsum; 3HXE; -.
PDBsum; 3HXF; -.
PDBsum; 3PZ1; -.
PDBsum; 3PZ2; -.
PDBsum; 3PZ3; -.
PDBsum; 4EHM; -.
PDBsum; 4GTS; -.
PDBsum; 4GTT; -.
PDBsum; 4GTV; -.
ProteinModelPortal; Q08602; -.
SMR; Q08602; -.
ComplexPortal; CPX-2249; Protein geranylgeranyltransferase type II complex.
DIP; DIP-6137N; -.
IntAct; Q08602; 1.
STRING; 10116.ENSRNOP00000049261; -.
PaxDb; Q08602; -.
PRIDE; Q08602; -.
Ensembl; ENSRNOT00000048455; ENSRNOP00000049261; ENSRNOG00000030483.
GeneID; 58983; -.
KEGG; rno:58983; -.
UCSC; RGD:621697; rat.
CTD; 5875; -.
RGD; 621697; Rabggta.
eggNOG; KOG0529; Eukaryota.
eggNOG; COG5536; LUCA.
GeneTree; ENSGT00550000075121; -.
HOGENOM; HOG000007845; -.
HOVERGEN; HBG002171; -.
InParanoid; Q08602; -.
KO; K14050; -.
OMA; NDSSAWF; -.
OrthoDB; EOG091G0L9H; -.
PhylomeDB; Q08602; -.
TreeFam; TF315057; -.
Reactome; R-RNO-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
Reactome; R-RNO-8873719; RAB geranylgeranylation.
EvolutionaryTrace; Q08602; -.
PRO; PR:Q08602; -.
Proteomes; UP000002494; Chromosome 15.
Bgee; ENSRNOG00000030483; Expressed in 10 organ(s), highest expression level in skeletal muscle tissue.
Genevisible; Q08602; RN.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:CAFA.
GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IDA:UniProtKB.
GO; GO:0017137; F:Rab GTPase binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0018344; P:protein geranylgeranylation; IDA:UniProtKB.
GO; GO:0065003; P:protein-containing complex assembly; IMP:CAFA.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR002088; Prenyl_trans_a.
InterPro; IPR036254; RabGGT_asu_insert-dom_sf.
InterPro; IPR009087; RabGGT_asu_insert-domain.
InterPro; IPR032955; RabGGTase_alpha.
PANTHER; PTHR11129:SF2; PTHR11129:SF2; 1.
Pfam; PF01239; PPTA; 4.
Pfam; PF07711; RabGGT_insert; 1.
ProDom; PD331837; RabGG_trans_A; 1.
SUPFAM; SSF49594; SSF49594; 1.
PROSITE; PS51147; PFTA; 6.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Leucine-rich repeat; Phosphoprotein; Prenyltransferase;
Reference proteome; Repeat; Transferase.
CHAIN 1 567 Geranylgeranyl transferase type-2 subunit
alpha.
/FTId=PRO_0000119759.
REPEAT 44 78 PFTA 1.
REPEAT 88 122 PFTA 2.
REPEAT 124 158 PFTA 3.
REPEAT 159 193 PFTA 4.
REPEAT 207 241 PFTA 5.
REPEAT 363 397 PFTA 6.
REPEAT 442 463 LRR 1.
REPEAT 464 486 LRR 2.
REPEAT 487 508 LRR 3.
REPEAT 509 530 LRR 4.
REPEAT 534 555 LRR 5.
MOD_RES 98 98 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JHK4}.
CONFLICT 169 169 S -> D (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 227 227 S -> Q (in Ref. 1; AA sequence).
{ECO:0000305}.
HELIX 13 40 {ECO:0000244|PDB:3DSS}.
HELIX 46 56 {ECO:0000244|PDB:3DSS}.
HELIX 63 79 {ECO:0000244|PDB:3DSS}.
HELIX 82 102 {ECO:0000244|PDB:3DSS}.
HELIX 107 119 {ECO:0000244|PDB:3DSS}.
STRAND 120 122 {ECO:0000244|PDB:3C72}.
HELIX 125 138 {ECO:0000244|PDB:3DSS}.
HELIX 143 155 {ECO:0000244|PDB:3DSS}.
HELIX 160 173 {ECO:0000244|PDB:3DSS}.
HELIX 178 191 {ECO:0000244|PDB:3DSS}.
STRAND 197 199 {ECO:0000244|PDB:1DCE}.
HELIX 205 221 {ECO:0000244|PDB:3DSS}.
HELIX 226 237 {ECO:0000244|PDB:3DSS}.
STRAND 245 251 {ECO:0000244|PDB:1DCE}.
TURN 252 255 {ECO:0000244|PDB:1DCE}.
STRAND 256 265 {ECO:0000244|PDB:1DCE}.
STRAND 267 269 {ECO:0000244|PDB:1LTX}.
STRAND 274 283 {ECO:0000244|PDB:1DCE}.
STRAND 296 303 {ECO:0000244|PDB:1DCE}.
HELIX 306 308 {ECO:0000244|PDB:1DCE}.
STRAND 313 322 {ECO:0000244|PDB:1DCE}.
TURN 323 326 {ECO:0000244|PDB:1DCE}.
STRAND 327 334 {ECO:0000244|PDB:1DCE}.
STRAND 338 343 {ECO:0000244|PDB:1DCE}.
TURN 347 350 {ECO:0000244|PDB:1DCE}.
HELIX 353 355 {ECO:0000244|PDB:3DSS}.
HELIX 358 377 {ECO:0000244|PDB:3DSS}.
HELIX 382 395 {ECO:0000244|PDB:3DSS}.
TURN 397 400 {ECO:0000244|PDB:3DSS}.
HELIX 401 414 {ECO:0000244|PDB:3DSS}.
HELIX 416 418 {ECO:0000244|PDB:3DSS}.
HELIX 419 438 {ECO:0000244|PDB:3DSS}.
STRAND 444 447 {ECO:0000244|PDB:1DCE}.
HELIX 459 462 {ECO:0000244|PDB:1DCE}.
STRAND 467 469 {ECO:0000244|PDB:1DCE}.
HELIX 480 484 {ECO:0000244|PDB:1DCE}.
STRAND 490 492 {ECO:0000244|PDB:1DCE}.
HELIX 502 504 {ECO:0000244|PDB:1DCE}.
STRAND 512 514 {ECO:0000244|PDB:1DCE}.
STRAND 522 524 {ECO:0000244|PDB:1DCE}.
HELIX 527 531 {ECO:0000244|PDB:1DCE}.
STRAND 537 539 {ECO:0000244|PDB:1DCE}.
HELIX 544 547 {ECO:0000244|PDB:1DCE}.
STRAND 548 550 {ECO:0000244|PDB:1DCE}.
HELIX 554 558 {ECO:0000244|PDB:1DCE}.
STRAND 563 566 {ECO:0000244|PDB:1DCE}.
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


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