Reviewed, UniProtKB/Swiss-Prot Q9JHK4 (PGTA_MOUSE)

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

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	567 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 dimer By similarity.
Enzyme regulation	The enzymatic reaction requires the aid of a Rab escort protein (also called component A) By similarity.
Subunit structure	Heterodimer of an alpha and a beta subunit, collectively called component B By similarity.
Involvement in disease	Defects in Rabggta are the cause of the gunmetal (gm) phenotype. Mice homozygous for gm have prolonged bleeding, thrombocytopenia and reduced platelet alpha- and delta-granule contents. Ref.1
Sequence similarities	Belongs to the protein prenyltransferase subunit alpha family. Contains 6 PFTA repeats.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	Metal-binding Zinc
Molecular function	Prenyltransferase Transferase
Gene Ontology (GO)
Biological process	protein amino acid prenylation Inferred from electronic annotation. Source: InterPro protein geranylgeranylation Ref.1 Inferred from mutant phenotype. Source: MGI
Molecular function	Rab geranylgeranyltransferase activity Ref.1 Inferred from mutant phenotype. Source: MGI protein binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9JHK4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9JHK4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     337-339: HQE → DAV
     340-567: Missing.

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_0000119758
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 By similarity
Natural variations
	Alternative sequence	337 – 339	3	HQE → DAV in isoform 2.		VSP_009113
	Alternative sequence	340 – 567	228	Missing in isoform 2.		VSP_009114

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 387DA2DAC12C4C0D	FASTA	567	64,989
	10 20 30 40 50 60 MHGRLKVKTS EEQAEAKRLE REQKLKLYQS ATQAVFQKRE AGELDESVLE LTSQILGANP 70 80 90 100 110 120 DFATLWNCRR EVLQQLETQK SPEELAALVK AELGFLESCL RVNPKSYGTW HHRCWLLSRL 130 140 150 160 170 180 PEPNWARELE LCARFLEADE RNFHCWDYRR FVAAQAAVAP AEELAFTDSL ITRNFSNYSS 190 200 210 220 230 240 WHYRSCLLPQ LHPQPDSGPQ GRLPENVLLR ELELVQNAFF TDPNDQSAWF YHRWLLGRAE 250 260 270 280 290 300 PHDVLCCLHV SREEACLSVC FSRPLIVGSK MGTLLLTVDE APLSVEWRTP DGRNRPSHVW 310 320 330 340 350 360 LCDLPAASLN DHLPQHTFRV IWTGSDTQKE CVLLKGHQEC WCRDSATDEQ LFRCELSVEK 370 380 390 400 410 420 STVLQSELES CKELQELEPE NKWCLLTIIL LMRALDPLLY EKETLEYFST LKAVDPMRAA 430 440 450 460 470 480 YLDDLRSKFL VENSVLKMEY ADVRVLHLAH KDLTVLCHLE QLLLVTHLDL SHNRLRALPP 490 500 510 520 530 540 ALAALRCLEV LQASDNVLEN LDGVANLPRL RELLLCNNRL QQSAALQTLA SCPRLVFLNL 550 560 QGNSLCQEEG IRERLAEMLP SVSSILT
	Isoform 2. Checksum: B68BCAADA15ED4D2	FASTA	339	38,943
	10 20 30 40 50 60 MHGRLKVKTS EEQAEAKRLE REQKLKLYQS ATQAVFQKRE AGELDESVLE LTSQILGANP 70 80 90 100 110 120 DFATLWNCRR EVLQQLETQK SPEELAALVK AELGFLESCL RVNPKSYGTW HHRCWLLSRL 130 140 150 160 170 180 PEPNWARELE LCARFLEADE RNFHCWDYRR FVAAQAAVAP AEELAFTDSL ITRNFSNYSS 190 200 210 220 230 240 WHYRSCLLPQ LHPQPDSGPQ GRLPENVLLR ELELVQNAFF TDPNDQSAWF YHRWLLGRAE 250 260 270 280 290 300 PHDVLCCLHV SREEACLSVC FSRPLIVGSK MGTLLLTVDE APLSVEWRTP DGRNRPSHVW 310 320 330 LCDLPAASLN DHLPQHTFRV IWTGSDTQKE CVLLKGDAV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Rab geranylgeranyl transferase alpha mutation in the gunmetal mouse reduces Rab prenylation and platelet synthesis." Detter J.C., Zhang Q., Mules E.H., Novack E.K., Mishra V.S., Li W., McMurtrie E.B., Tchernev V.T., Wallace M.R., Seabra M.C., Swank R.T., Kingsmore S.K. Proc. Natl. Acad. Sci. U.S.A. 97:4144-4149(2000) [PubMed: 10737774] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), DISEASE. Strain: C57BL/6J and C57BL/6J-GM/GM.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Kidney.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF127654 Genomic DNA. Translation: AAF65918.1. AF127655 Genomic DNA. Translation: AAF65919.1. AF127656 mRNA. Translation: AAF65920.1. AF127658 mRNA. Translation: AAF65921.1. AF127659 mRNA. Translation: AAF65922.1. AF127660 mRNA. Translation: AAF65923.1. AF127662 mRNA. Translation: AAF65924.1. AK002625 mRNA. Translation: BAB22240.1.
IPI	IPI00271905. IPI00620701.
RefSeq	NP_062392.1.
UniGene	Mm.87216
3D structure databases
HSSP	HSSP built from PDB template 1LTX based on UniProtKB Q08602.
SMR	Q9JHK4. Positions 2-567.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9JHK4.
Proteomic databases
PRIDE	Q9JHK4.
Genome annotation databases
Ensembl	ENSMUST00000062861; ENSMUSP00000061498; ENSMUSG00000040472; Mus musculus. [Genome view]
GeneID	56187.
KEGG	mmu:56187.
UCSC	uc007uai.1. mouse.
Organism-specific databases
CTD	56187.
MGI	MGI:1860443. Rabggta.
Phylogenomic databases
HOGENOM	Q9JHK4.
HOVERGEN	Q9JHK4.
OMA	WHYRSCL.
Enzyme and pathway databases
BRENDA	2.5.1.60. 244.
Gene expression databases
ArrayExpress	Q9JHK4.
Bgee	Q9JHK4.
CleanEx	MM_RABGGTA.
Genevestigator	Q9JHK4.
GermOnline	ENSMUSG00000040472. Mus musculus.
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	311974.
SOURCE	Search...

Entry information

Entry name

PGTA_MOUSE

Accession

Primary (citable) accession number: Q9JHK4
Secondary accession number(s): Q9JLX2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	October 1, 2000
Last modified:	November 3, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)