ID   PGTA_PONAB              Reviewed;         567 AA.
AC   Q5NVK5;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
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   -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
CC       family. {ECO:0000305}.
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DR   EMBL; CR926021; CAI29658.1; -; mRNA.
DR   RefSeq; NP_001127096.1; NM_001133624.1.
DR   AlphaFoldDB; Q5NVK5; -.
DR   SMR; Q5NVK5; -.
DR   STRING; 9601.ENSPPYP00000006478; -.
DR   GeneID; 100174130; -.
DR   KEGG; pon:100174130; -.
DR   CTD; 5875; -.
DR   eggNOG; KOG0529; Eukaryota.
DR   InParanoid; Q5NVK5; -.
DR   OrthoDB; 1527547at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0004663; F:Rab geranylgeranyltransferase activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR001611; Leu-rich_rpt.
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; PS51450; LRR; 5.
DR   PROSITE; PS51147; PFTA; 6.
PE   2: Evidence at transcript level;
KW   Leucine-rich repeat; Phosphoprotein; Prenyltransferase; Reference proteome;
KW   Repeat; Transferase.
FT   CHAIN           1..567
FT                   /note="Geranylgeranyl transferase type-2 subunit alpha"
FT                   /id="PRO_0000229771"
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:0000250|UniProtKB:Q9JHK4"
SQ   SEQUENCE   567 AA;  65107 MW;  6C511480882981F2 CRC64;
     MHGRLKVKTS EEQAEAKRLE REQKLKLYQS ATQAVFQKRQ AGELDESVLE LTSQILGANP
     DFATLWNCRR EVLQQLETQK SPEELAALVK AELGFLESCL RVNPKSYGTW HHRCWLLGRL
     PEPNWTRELE LCARFLEVDE RNFHCWDYRR FVATQAAVPP AEELAFTDSL ITRNFSNYSS
     WHYRSCLLPQ LHPQPDSGPQ GRLPEDVLLK ELELVQNAFF TDPNDQSAWF YHRWLLGRAD
     PQDALRCLHV SREEACLTVS FSRPLLVGSR TEILLLMVDD SPLIVEWRTP DGRNRPSHVW
     LCDLPAASLN DQLPQHTFRV IWTAGDVQKE CVLLKGRQEG WCRDSTTDEQ LFRCELSVEK
     STVLQSELES CKELQELEPE NKWCLLTIIL LMRALDPLLY EKETLRYFQT LKAVDPMRAA
     YLDDLRSKFL LENSVLKMEY AEVRVLHLAH KDLTVLCHLE QLLLVTHLDL SHNRLRTLPP
     ALAALRCLEV LQASDNAIES LDGVTNLPRL QELLLCNNRL QRPAVLQPLA SCPRLVLLNL
     QGNPLCQAVG ILEQLAELPP SVNSILT