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Q9JHK4 (PGTA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Geranylgeranyl transferase type-2 subunit alpha

EC=2.5.1.60
Alternative name(s):
Geranylgeranyl transferase type II subunit alpha
Rab geranyl-geranyltransferase subunit alpha
Short name=Rab GG transferase alpha
Short name=Rab GGTase alpha
Rab geranylgeranyltransferase subunit alpha
Gene names
Name:Rabggta
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length567 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

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. Ref.1

Catalytic activity

Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.

Enzyme regulation

The enzymatic reaction requires the aid of a Rab escort protein (also called component A), such as CHM By similarity.

Subunit structure

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 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 5 LRR (leucine-rich) repeats.

Contains 6 PFTA repeats.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 567567Geranylgeranyl transferase type-2 subunit alpha
PRO_0000119758

Regions

Repeat44 – 7835PFTA 1
Repeat88 – 12235PFTA 2
Repeat124 – 15835PFTA 3
Repeat159 – 19335PFTA 4
Repeat207 – 24135PFTA 5
Repeat363 – 39735PFTA 6
Repeat442 – 46322LRR 1
Repeat464 – 48623LRR 2
Repeat487 – 50822LRR 3
Repeat509 – 53022LRR 4
Repeat534 – 55522LRR 5

Natural variations

Alternative sequence337 – 3393HQE → DAV in isoform 2.
VSP_009113
Alternative sequence340 – 567228Missing in isoform 2.
VSP_009114

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 387DA2DAC12C4C0D

FASTA56764,989
        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 

« Hide

Isoform 2 [UniParc].

Checksum: B68BCAADA15ED4D2
Show »

FASTA33938,943

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), DISEASE, FUNCTION.
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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS36933.1. [Q9JHK4-1]
RefSeqNP_062392.1. NM_019519.2. [Q9JHK4-1]
XP_006519357.1. XM_006519294.1. [Q9JHK4-1]
XP_006519358.1. XM_006519295.1. [Q9JHK4-1]
UniGeneMm.87216.

3D structure databases

ProteinModelPortalQ9JHK4.
SMRQ9JHK4. Positions 2-567.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207827. 1 interaction.
IntActQ9JHK4. 1 interaction.
STRING10090.ENSMUSP00000061498.

PTM databases

PhosphoSiteQ9JHK4.

Proteomic databases

MaxQBQ9JHK4.
PaxDbQ9JHK4.
PRIDEQ9JHK4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000062861; ENSMUSP00000061498; ENSMUSG00000040472. [Q9JHK4-1]
ENSMUST00000163889; ENSMUSP00000128668; ENSMUSG00000040472. [Q9JHK4-1]
ENSMUST00000169237; ENSMUSP00000133032; ENSMUSG00000040472. [Q9JHK4-1]
GeneID56187.
KEGGmmu:56187.
UCSCuc007uai.1. mouse. [Q9JHK4-1]

Organism-specific databases

CTD5875.
MGIMGI:1860443. Rabggta.

Phylogenomic databases

eggNOGCOG5536.
GeneTreeENSGT00550000075121.
HOGENOMHOG000007845.
HOVERGENHBG002171.
InParanoidQ9JHK4.
KOK14050.
OMAWNCRREV.
OrthoDBEOG7PP56C.
PhylomeDBQ9JHK4.
TreeFamTF315057.

Gene expression databases

BgeeQ9JHK4.
CleanExMM_RABGGTA.
GenevestigatorQ9JHK4.

Family and domain databases

Gene3D2.60.40.1130. 1 hit.
InterProIPR001611. Leu-rich_rpt.
IPR002088. Prenyl_trans_a.
IPR009087. RabGGT_asu_insert-domain.
[Graphical view]
PfamPF00560. LRR_1. 1 hit.
PF01239. PPTA. 5 hits.
PF07711. RabGGT_insert. 1 hit.
[Graphical view]
ProDomPD331837. RabGG_trans_A. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF49594. SSF49594. 1 hit.
PROSITEPS51147. PFTA. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9JHK4.
NextBio311974.
PROQ9JHK4.
SOURCESearch...

Entry information

Entry namePGTA_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot