Reviewed, UniProtKB/Swiss-Prot P53612 (PGTB2_MOUSE)

Names and origin

Protein names

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

Gene names

Name:

Rabggtb

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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 By similarity.
Catalytic activity	Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.
Cofactor	Binds 1 zinc ion per subunit By similarity.
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. Interaction of beta subunit with prenylated PTP4A2 precludes its association with subunit alpha, and inhibits enzyme activity By similarity.
Tissue specificity	Ubiquitous. Detected in all the major organs in adult animals. Ref.2
Developmental stage	Specific expression was elevated in mid-gestation stages, particularly developing liver and spinal cord. Ref.2
Induction	Increased dramatically by cycloheximide (CHX) treatment within a short time (as early as 2 hours). Actinomycin D was used to determine the half-life, CHX treatment resulted in a dramatic increase of the half-life from 8 hours to greater than 12 hours. Ref.2
Sequence similarities	Belongs to the protein prenyltransferase subunit beta family. Contains 6 PFTB repeats.

Ontologies

Keywords
Domain	Repeat
Ligand	Metal-binding Zinc
Molecular function	Prenyltransferase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Molecular function	Rab geranylgeranyltransferase activity Inferred from electronic annotation. Source: EC 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 – 339	339	Geranylgeranyl transferase type-2 subunit beta		PRO_0000119773
Regions
	Repeat	28 – 69	42	PFTB 1
	Repeat	76 – 117	42	PFTB 2
	Repeat	124 – 165	42	PFTB 3
	Repeat	172 – 213	42	PFTB 4
	Repeat	220 – 261	42	PFTB 5
	Repeat	268 – 310	43	PFTB 6
Sites
	Metal binding	246	1	Zinc By similarity
	Metal binding	248	1	Zinc By similarity
	Metal binding	298	1	Zinc By similarity
Amino acid modifications
	Modified residue	11	1	Phosphothreonine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P53612-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: C364F1AF237802AB	FASTA	339	37,706
	10 20 30 40 50 60 MGSLLFSWKG TQQKDVTIKS DAPDTLLLEK HADYIASYGS KKDDYEYCMS EYLRMSGVYW 70 80 90 100 110 120 GLTVMDLMGQ LHRMNREEIL VFIKSCQHEC GGISASIGHD PHLLYTLSAV QILTLYDSVH 130 140 150 160 170 180 VINVDKVVAY VQSLQKEDGS FAGDIWGEID TRFSFCAVAT LALLGKLDAI NVEKAIEFVL 190 200 210 220 230 240 SCMNFDGGFG CRPGSESHAG QIYCCTGFLA ITSQLHQVNS DLLGWWLCEA QLPSGALNGR 250 260 270 280 290 300 REKLPDVCYS WWVLASLKII GRLHWIVSEK LRSFILACQD EETGGFADRP GDMVDPFHTL 310 320 330 FGIAGLSLLG EEQIKPVSPV FCMPEEVLQR VNVQPELVS

References

[1]	"Studies of cloning, chromosomal mapping, and embryonic expression of the mouse Rab geranylgeranyl transferase beta subunit." Wei L.-N., Lee C.-H., Chinpaisal C., Copeland N.G., Gilbert D.J., Jenkins N.A., Hsu Y.-C. Cell Growth Differ. 6:607-614(1995) [PubMed: 7544156] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: CD-1. Tissue: Embryo.
[2]	"Studies of the mouse Rab geranylgeranyl transferase beta subunit: gene structure, expression and regulation." Chinpaisal C., Lee C.-H., Wei L.-N. Gene 184:237-243(1997) [PubMed: 9031634] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION. Strain: CD-1. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U12922 mRNA. Translation: AAB01502.1.
IPI	IPI00133505.
PIR	I49116. JC6177.
UniGene	Mm.277831
3D structure databases
HSSP	HSSP built from PDB template 1LTX based on UniProtKB Q08603.
SMR	P53612. Positions 11-339.
ModBase	Search...
Protein-protein interaction databases
STRING	P53612.
PTM databases
PhosphoSite	P53612.
Proteomic databases
PRIDE	P53612.
Genome annotation databases
Ensembl	ENSMUST00000089950; ENSMUSP00000087396; ENSMUSG00000038975; Mus musculus. [Genome view]
KEGG	mmu:19352.
UCSC	uc008rug.1. mouse.
Organism-specific databases
CTD	19352.
MGI	MGI:99537. Rabggtb.
Phylogenomic databases
HOGENOM	P53612.
HOVERGEN	P53612.
Enzyme and pathway databases
BRENDA	2.5.1.60. 244.
Gene expression databases
ArrayExpress	P53612.
Bgee	P53612.
CleanEx	MM_RABGGTB.
Genevestigator	P53612.
GermOnline	ENSMUSG00000038975. Mus musculus.
Family and domain databases
InterPro	IPR001330. Prenyltrans. [Graphical view]
Pfam	PF00432. Prenyltrans. 5 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	296383.
SOURCE	Search...

Entry information

Entry name

PGTB2_MOUSE

Accession

Primary (citable) accession number: P53612

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	October 13, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)