Reviewed, UniProtKB/Swiss-Prot Q08602 (PGTA_RAT)

Names and origin

Protein names

Recommended name:
    Geranylgeranyl transferase type-2 subunit alpha
    EC=2.5.1.60
Alternative name(s):
    Geranylgeranyl transferase type II subunit alpha
    Rab geranylgeranyltransferase subunit alpha
    Rab geranyl-geranyltransferase subunit alpha
      Short name=Rab GG transferase alpha
      Short name=Rab GGTase alpha

Gene names

Name:	Rabggta
Synonyms:	Ggta

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	567 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to both cysteines in Rab proteins with an -XXCC, -XCXC and -CCXX C-terminal, such as RAB1A, RAB3A and RAB5A respectively.
Catalytic activity	Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.
Cofactor	Binds 1 zinc ion per dimer.
Enzyme regulation	The enzymatic reaction requires the aid of a Rab escort protein (also called component A).
Subunit structure	Heterodimer of an alpha and a beta subunit, collectively called component B. Ref.3 Ref.4
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.
Sequence similarities	Belongs to the protein prenyltransferase subunit alpha family. Contains 6 PFTA repeats.

Ontologies

Keywords
Domain	Repeat
Ligand	Metal-binding Zinc
Molecular function	Prenyltransferase Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	protein amino acid geranylgeranylation Ref.1 Inferred from direct assay. Source: RGD
Molecular function	Rab geranylgeranyltransferase activity Ref.1 Inferred from direct assay. Source: RGD protein binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 567

567

Geranylgeranyl transferase type-2 subunit alpha

PRO_0000119759

Regions

Repeat

44 – 78

35

PFTA 1

Repeat

88 – 122

35

PFTA 2

Repeat

124 – 158

35

PFTA 3

Repeat

159 – 193

35

PFTA 4

Repeat

207 – 241

35

PFTA 5

Repeat

363 – 397

35

PFTA 6

Sites

Metal binding

2

1

Zinc

Experimental info

Sequence conflict

169

1

S → D AA sequence Ref.1

Sequence conflict

227

1

S → Q AA sequence Ref.1

Secondary structure

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567

Helix Strand Turn

Details...

Helix

29 – 40

12

Helix

49 – 58

10

Helix

63 – 72

10

Helix

73 – 75

3

Beta strand

76 – 80

5

Turn

82 – 84

3

Helix

85 – 102

18

Helix

107 – 119

13

Helix

125 – 138

14

Helix

143 – 155

13

Helix

160 – 173

14

Helix

178 – 187

10

Turn

188 – 191

4

Helix

205 – 216

12

Helix

218 – 221

4

Helix

226 – 234

9

Beta strand

245 – 251

7

Turn

252 – 255

4

Beta strand

256 – 265

10

Beta strand

267 – 269

3

Beta strand

274 – 282

9

Beta strand

296 – 303

8

Helix

306 – 308

3

Beta strand

310 – 322

13

Turn

323 – 325

3

Beta strand

328 – 334

7

Beta strand

338 – 343

6

Turn

346 – 350

5

Helix

358 – 377

20

Helix

382 – 395

14

Turn

397 – 400

4

Helix

401 – 414

14

Helix

416 – 418

3

Helix

419 – 441

23

Beta strand

444 – 447

4

Helix

459 – 461

3

Beta strand

467 – 469

3

Helix

480 – 484

5

Beta strand

490 – 492

3

Helix

502 – 504

3

Beta strand

512 – 514

3

Helix

523 – 531

9

Beta strand

537 – 539

3

Helix

544 – 547

4

Helix

551 – 558

8

Sequences

	Sequence		Length	Mass (Da)
	Q08602-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 1F9D235F973EABD5	FASTA	567	64,904
	10 20 30 40 50 60 MHGRLKVKTS EEQAEAKRLE REQKLKLYQS ATQAVFQKRQ AGELDESVLE LTSQILGANP 70 80 90 100 110 120 DFATLWNCRR EVLQHLETEK SPEESAALVK AELGFLESCL RVNPKSYGTW HHRCWLLSRL 130 140 150 160 170 180 PEPNWARELE LCARFLEADE RNFHCWDYRR FVAAQAAVAP AEELAFTDSL ITRNFSNYSS 190 200 210 220 230 240 WHYRSCLLPQ LHPQPDSGPQ GRLPENVLLK ELELVQNAFF TDPNDQSAWF YHRWLLGRAE 250 260 270 280 290 300 PHDVLCCVHV SREEACLSVC FSRPLTVGSR MGTLLLMVDE APLSVEWRTP DGRNRPSHVW 310 320 330 340 350 360 LCDLPAASLN DQLPQHTFRV IWTGSDSQKE CVLLKDRPEC WCRDSATDEQ LFRCELSVEK 370 380 390 400 410 420 STVLQSELES CKELQELEPE NKWCLLTIIL LMRALDPLLY EKETLQYFST LKAVDPMRAA 430 440 450 460 470 480 YLDDLRSKFL LENSVLKMEY ADVRVLHLAH KDLTVLCHLE QLLLVTHLDL SHNRLRALPP 490 500 510 520 530 540 ALAALRCLEV LQASDNALEN VDGVANLPRL QELLLCNNRL QQSAAIQPLV SCPRLVLLNL 550 560 QGNSLCQEEG IQERLAEMLP SVSSILT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning and expression of the alpha and beta subunits of rat Rab geranylgeranyl transferase." Armstrong S.A., Seabra M.C., Suedhof T.C., Goldstein J.L., Brown M.S. J. Biol. Chem. 268:12221-12229(1993) [PubMed: 8505342] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Brain.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary.
[3]	"Crystal structure of Rab geranylgeranyltransferase at 2.0 A resolution." Zhang H., Seabra M.C., Deisenhofer J. Structure 8:241-251(2000) [PubMed: 10745007] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT.
[4]	"Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase." 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. Mol. Cell 11:483-494(2003) [PubMed: 12620235] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT AND REP1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L10415 mRNA. Translation: AAA41998.1.
S62096 mRNA. Translation: AAB27018.1.
BC086547 mRNA. Translation: AAH86547.1.

IPI

IPI00231284.

PIR

A45977.

RefSeq

NP_113842.1.

UniGene

Rn.29434

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DCE	X-ray	2.00	A/C	1-567	[»]
1LTX	X-ray	2.70	A	1-567	[»]
3C72	X-ray	2.30	A	1-441	[»]
3DSS	X-ray	1.80	A	1-441	[»]
3DST	X-ray	1.90	A	1-441	[»]
3DSU	X-ray	1.90	A	1-441	[»]
3DSV	X-ray	2.10	A	1-441	[»]
3DSW	X-ray	2.15	A	1-441	[»]
3DSX	X-ray	2.10	A	1-441	[»]
3HXB	X-ray	2.25	A	1-441	[»]
3HXC	X-ray	1.95	A	1-441	[»]
3HXD	X-ray	1.95	A	1-441	[»]
3HXE	X-ray	1.95	A	1-441	[»]
3HXF	X-ray	1.90	A	1-441	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6137N.

STRING

Q08602.

Genome annotation databases

Ensembl

ENSRNOT00000048455; ENSRNOP00000049261; ENSRNOG00000030483; Rattus norvegicus. [Genome view]

GeneID

58983.

KEGG

rno:58983.

UCSC

NM_031654. rat.

Organism-specific databases

CTD

58983.

RGD

621697. Rabggta.

Phylogenomic databases

HOVERGEN

Q08602.

Enzyme and pathway databases

BRENDA

2.5.1.60. 248.

Gene expression databases

ArrayExpress

Q08602.

Genevestigator

Q08602.

GermOnline

ENSRNOG00000030483. Rattus norvegicus.

Family and domain databases

InterPro

IPR001611. Leu-rich_rpt.
IPR002088. Prenyl_trans_a.
IPR008940. Prenyltransferase.
IPR009087. RabGG_trans_A.
[Graphical view]

Gene3D

G3DSA:1.25.40.120. Prenyl_trans. 1 hit.

Pfam

PF00560. LRR_1. 1 hit.
PF01239. PPTA. 6 hits.
PF07711. RabGGT_insert. 1 hit.
[Graphical view]

PROSITE

PS51147. PFTA. 6 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

611680.

Entry information

Entry name

PGTA_RAT

Accession

Primary (citable) accession number: Q08602

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	November 3, 2009
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)