PGTA_MOUSE
ID PGTA_MOUSE Reviewed; 567 AA.
AC Q9JHK4; Q9JLX2;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Geranylgeranyl transferase type-2 subunit alpha;
DE EC=2.5.1.60;
DE AltName: Full=Geranylgeranyl transferase type II subunit alpha;
DE AltName: Full=Rab geranyl-geranyltransferase subunit alpha;
DE Short=Rab GG transferase alpha;
DE Short=Rab GGTase alpha;
DE AltName: Full=Rab geranylgeranyltransferase subunit alpha;
GN Name=Rabggta;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), DISEASE, AND
RP FUNCTION.
RC STRAIN=C57BL/6J, and C57BL/6J-GM/GM;
RX PubMed=10737774; DOI=10.1073/pnas.080517697;
RA Detter J.C., Zhang Q., Mules E.H., Novack E.K., Mishra V.S., Li W.,
RA McMurtrie E.B., Tchernev V.T., Wallace M.R., Seabra M.C., Swank R.T.,
RA Kingsmore S.K.;
RT "Rab geranylgeranyl transferase alpha mutation in the gunmetal mouse
RT reduces Rab prenylation and platelet synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:4144-4149(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the transfer of a geranylgeranyl moiety from
CC geranylgeranyl diphosphate to both cysteines of Rab proteins with the
CC C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A
CC and RAB7A. {ECO:0000269|PubMed:10737774}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] =
CC diphosphate + S-geranylgeranyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:21240, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11537,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533,
CC ChEBI:CHEBI:86021; EC=2.5.1.60;
CC -!- ACTIVITY REGULATION: The enzymatic reaction requires the aid of a Rab
CC escort protein (also called component A), such as CHM. {ECO:0000250}.
CC -!- SUBUNIT: Heterotrimer composed of RABGGTA, RABGGTB and CHM; within this
CC trimer, RABGGTA and RABGGTB form the catalytic component B, while CHM
CC (component A) mediates peptide substrate binding. The Rab GGTase dimer
CC (RGGT) interacts with CHM (component A) prior to Rab protein binding;
CC the association is stabilized by geranylgeranyl pyrophosphate (GGpp).
CC The CHM:RGGT:Rab complex is destabilized by GGpp. Interacts with non-
CC phosphorylated form of RAB8A; phosphorylation of RAB8A at 'Thr-72'
CC disrupts this interaction. {ECO:0000250|UniProtKB:Q92696}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JHK4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JHK4-2; Sequence=VSP_009113, VSP_009114;
CC -!- DISEASE: Note=Defects in Rabggta are the cause of the gunmetal (gm)
CC phenotype. Mice homozygous for gm have prolonged bleeding,
CC thrombocytopenia and reduced platelet alpha- and delta-granule
CC contents. {ECO:0000269|PubMed:10737774}.
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
CC family. {ECO:0000305}.
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DR EMBL; AF127654; AAF65918.1; -; Genomic_DNA.
DR EMBL; AF127655; AAF65919.1; -; Genomic_DNA.
DR EMBL; AF127656; AAF65920.1; -; mRNA.
DR EMBL; AF127658; AAF65921.1; -; mRNA.
DR EMBL; AF127659; AAF65922.1; -; mRNA.
DR EMBL; AF127660; AAF65923.1; -; mRNA.
DR EMBL; AF127662; AAF65924.1; -; mRNA.
DR EMBL; AK002625; BAB22240.1; -; mRNA.
DR CCDS; CCDS36933.1; -. [Q9JHK4-1]
DR RefSeq; NP_062392.1; NM_019519.2. [Q9JHK4-1]
DR RefSeq; XP_006519357.1; XM_006519294.2.
DR RefSeq; XP_006519358.1; XM_006519295.1.
DR AlphaFoldDB; Q9JHK4; -.
DR SMR; Q9JHK4; -.
DR BioGRID; 207827; 9.
DR ComplexPortal; CPX-2920; Protein geranylgeranyltransferase type II complex.
DR IntAct; Q9JHK4; 1.
DR STRING; 10090.ENSMUSP00000133032; -.
DR iPTMnet; Q9JHK4; -.
DR PhosphoSitePlus; Q9JHK4; -.
DR SwissPalm; Q9JHK4; -.
DR EPD; Q9JHK4; -.
DR jPOST; Q9JHK4; -.
DR MaxQB; Q9JHK4; -.
DR PaxDb; Q9JHK4; -.
DR PeptideAtlas; Q9JHK4; -.
DR PRIDE; Q9JHK4; -.
DR ProteomicsDB; 289481; -. [Q9JHK4-1]
DR ProteomicsDB; 289482; -. [Q9JHK4-2]
DR Antibodypedia; 22812; 90 antibodies from 22 providers.
DR DNASU; 56187; -.
DR Ensembl; ENSMUST00000163889; ENSMUSP00000128668; ENSMUSG00000040472. [Q9JHK4-1]
DR Ensembl; ENSMUST00000169237; ENSMUSP00000133032; ENSMUSG00000040472. [Q9JHK4-1]
DR Ensembl; ENSMUST00000227061; ENSMUSP00000154725; ENSMUSG00000040472. [Q9JHK4-1]
DR GeneID; 56187; -.
DR KEGG; mmu:56187; -.
DR UCSC; uc007uai.1; mouse. [Q9JHK4-1]
DR CTD; 5875; -.
DR MGI; MGI:1860443; Rabggta.
DR VEuPathDB; HostDB:ENSMUSG00000040472; -.
DR eggNOG; KOG0529; Eukaryota.
DR GeneTree; ENSGT00550000075121; -.
DR HOGENOM; CLU_031996_3_2_1; -.
DR InParanoid; Q9JHK4; -.
DR OMA; YNAWHHR; -.
DR OrthoDB; 1527547at2759; -.
DR PhylomeDB; Q9JHK4; -.
DR TreeFam; TF315057; -.
DR Reactome; R-MMU-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR BioGRID-ORCS; 56187; 29 hits in 76 CRISPR screens.
DR ChiTaRS; Rabggta; mouse.
DR EvolutionaryTrace; Q9JHK4; -.
DR PRO; PR:Q9JHK4; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9JHK4; protein.
DR Bgee; ENSMUSG00000040472; Expressed in ectoplacental cone and 248 other tissues.
DR ExpressionAtlas; Q9JHK4; baseline and differential.
DR Genevisible; Q9JHK4; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; ISS:UniProtKB.
DR GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IMP:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0018344; P:protein geranylgeranylation; IMP:MGI.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002088; Prenyl_trans_a.
DR InterPro; IPR036254; RabGGT_asu_insert-dom_sf.
DR InterPro; IPR009087; RabGGT_asu_insert-domain.
DR InterPro; IPR032955; RabGGTase_alpha.
DR PANTHER; PTHR11129:SF2; PTHR11129:SF2; 1.
DR Pfam; PF01239; PPTA; 5.
DR Pfam; PF07711; RabGGT_insert; 1.
DR SUPFAM; SSF49594; SSF49594; 1.
DR PROSITE; PS51147; PFTA; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; Leucine-rich repeat; Phosphoprotein;
KW Prenyltransferase; Reference proteome; Repeat; Transferase.
FT CHAIN 1..567
FT /note="Geranylgeranyl transferase type-2 subunit alpha"
FT /id="PRO_0000119758"
FT REPEAT 44..78
FT /note="PFTA 1"
FT REPEAT 88..122
FT /note="PFTA 2"
FT REPEAT 124..158
FT /note="PFTA 3"
FT REPEAT 159..193
FT /note="PFTA 4"
FT REPEAT 207..241
FT /note="PFTA 5"
FT REPEAT 363..397
FT /note="PFTA 6"
FT REPEAT 442..463
FT /note="LRR 1"
FT REPEAT 464..486
FT /note="LRR 2"
FT REPEAT 487..508
FT /note="LRR 3"
FT REPEAT 509..530
FT /note="LRR 4"
FT REPEAT 534..555
FT /note="LRR 5"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 337..339
FT /note="HQE -> DAV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10737774"
FT /id="VSP_009113"
FT VAR_SEQ 340..567
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10737774"
FT /id="VSP_009114"
SQ SEQUENCE 567 AA; 64989 MW; 387DA2DAC12C4C0D CRC64;
MHGRLKVKTS EEQAEAKRLE REQKLKLYQS ATQAVFQKRE AGELDESVLE LTSQILGANP
DFATLWNCRR EVLQQLETQK SPEELAALVK AELGFLESCL RVNPKSYGTW HHRCWLLSRL
PEPNWARELE LCARFLEADE RNFHCWDYRR FVAAQAAVAP AEELAFTDSL ITRNFSNYSS
WHYRSCLLPQ LHPQPDSGPQ GRLPENVLLR ELELVQNAFF TDPNDQSAWF YHRWLLGRAE
PHDVLCCLHV SREEACLSVC FSRPLIVGSK MGTLLLTVDE APLSVEWRTP DGRNRPSHVW
LCDLPAASLN DHLPQHTFRV IWTGSDTQKE CVLLKGHQEC WCRDSATDEQ LFRCELSVEK
STVLQSELES CKELQELEPE NKWCLLTIIL LMRALDPLLY EKETLEYFST LKAVDPMRAA
YLDDLRSKFL VENSVLKMEY ADVRVLHLAH KDLTVLCHLE QLLLVTHLDL SHNRLRALPP
ALAALRCLEV LQASDNVLEN LDGVANLPRL RELLLCNNRL QQSAALQTLA SCPRLVFLNL
QGNSLCQEEG IRERLAEMLP SVSSILT
