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   24-JAN-2024, entry version 163.
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,
RC   Pancreas, 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.ENSMUSP00000154725; -.
DR   iPTMnet; Q9JHK4; -.
DR   PhosphoSitePlus; Q9JHK4; -.
DR   SwissPalm; Q9JHK4; -.
DR   EPD; Q9JHK4; -.
DR   jPOST; Q9JHK4; -.
DR   MaxQB; Q9JHK4; -.
DR   PaxDb; 10090-ENSMUSP00000133032; -.
DR   PeptideAtlas; Q9JHK4; -.
DR   ProteomicsDB; 289481; -. [Q9JHK4-1]
DR   ProteomicsDB; 289482; -. [Q9JHK4-2]
DR   Pumba; Q9JHK4; -.
DR   Antibodypedia; 22812; 104 antibodies from 23 providers.
DR   DNASU; 56187; -.
DR   Ensembl; ENSMUST00000163889.3; ENSMUSP00000128668.2; ENSMUSG00000040472.16. [Q9JHK4-1]
DR   Ensembl; ENSMUST00000169237.8; ENSMUSP00000133032.2; ENSMUSG00000040472.16. [Q9JHK4-1]
DR   Ensembl; ENSMUST00000227061.2; ENSMUSP00000154725.2; ENSMUSG00000040472.16. [Q9JHK4-1]
DR   GeneID; 56187; -.
DR   KEGG; mmu:56187; -.
DR   UCSC; uc007uai.1; mouse. [Q9JHK4-1]
DR   AGR; MGI:1860443; -.
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; PKSYNAW; -.
DR   OrthoDB; 5489560at2759; -.
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 81 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 251 other cell types or tissues.
DR   ExpressionAtlas; Q9JHK4; baseline and differential.
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   Gene3D; 1.25.40.120; Protein prenylyltransferase; 1.
DR   Gene3D; 2.60.40.1130; Rab geranylgeranyltransferase alpha-subunit, insert domain; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 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   PANTHER; PTHR11129:SF2; GERANYLGERANYL TRANSFERASE TYPE-2 SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR11129; PROTEIN FARNESYLTRANSFERASE ALPHA SUBUNIT/RAB GERANYLGERANYL TRANSFERASE ALPHA SUBUNIT; 1.
DR   Pfam; PF01239; PPTA; 4.
DR   Pfam; PF07711; RabGGT_insert; 1.
DR   SUPFAM; SSF52075; Outer arm dynein light chain 1; 1.
DR   SUPFAM; SSF48439; Protein prenylyltransferase; 1.
DR   SUPFAM; SSF49594; Rab geranylgeranyltransferase alpha-subunit, insert domain; 1.
DR   PROSITE; PS51147; PFTA; 6.
DR   Genevisible; Q9JHK4; MM.
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
//