PGTA_BOVIN
ID PGTA_BOVIN Reviewed; 567 AA.
AC Q5EA80;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) 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; BT020689; AAX08706.1; -; mRNA.
DR EMBL; BT020760; AAX08777.1; -; mRNA.
DR EMBL; BT020911; AAX08928.1; -; mRNA.
DR EMBL; BC111228; AAI11229.1; -; mRNA.
DR EMBL; BT020650; AAX08667.1; -; mRNA.
DR RefSeq; NP_001015614.1; NM_001015614.1.
DR AlphaFoldDB; Q5EA80; -.
DR SMR; Q5EA80; -.
DR STRING; 9913.ENSBTAP00000025020; -.
DR PaxDb; Q5EA80; -.
DR PRIDE; Q5EA80; -.
DR Ensembl; ENSBTAT00000025020; ENSBTAP00000025020; ENSBTAG00000018796.
DR GeneID; 516619; -.
DR KEGG; bta:516619; -.
DR CTD; 5875; -.
DR VEuPathDB; HostDB:ENSBTAG00000018796; -.
DR VGNC; VGNC:33670; RABGGTA.
DR eggNOG; KOG0529; Eukaryota.
DR GeneTree; ENSGT00550000075121; -.
DR HOGENOM; CLU_031996_3_2_1; -.
DR InParanoid; Q5EA80; -.
DR OMA; YNAWHHR; -.
DR OrthoDB; 1527547at2759; -.
DR TreeFam; TF315057; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000018796; Expressed in infraspinatus muscle and 105 other tissues.
DR ExpressionAtlas; Q5EA80; 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; 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; 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 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_0000244431"
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; 64945 MW; 062DF9E97F366B3B CRC64;
MHGRLKVKTS EEQAEAKRLE REQKLKLYQA ATQTVFQKRQ AGELDESVLE LTSQILGANP
DFATLWNCRR EVLQQLEVQK SPEELATLVK AELGFLESCL RVNPKSYGTW HHRCWLLSRL
PEPNWARELE LCARFLEVDE RNFHCWDYRR FVAAQAAVPP AEELAFTDSL ITRNFSNYSS
WHYRSCLLPQ LHPQPDSGPQ GRLPEDVLLK ELELVQNAFF TDPNDQSAWF YHRWLLGRAD
PQDALRCLHV SRDEACLTVS FSRPLLVGSG METLLLMVDE SPLAVEWRTP EGRNRPSHIW
LCDLPATSLN DQLPQHTFRV IWTAGDAQKE CVLLKGRQEG WCRDSATDEQ LFRCELSVEK
STVLQSELES CKELQELEPE NKWCLLTIIL LMRALDPLQY EKETLQYFQT LKAVDPMRAA
YLDDLRSKFL LENSVLKMEY AEVRVLHLGH KDLTVLCHLE QLLLVTHLDL SHNRLRALPP
ALAALRCLEV LQANDNAIES LDGVTNLPRL QELILCNNRL QQPAVLQPLT SCPRLTLLNL
QGNPLCQAEG SSEHLAELLP SVSSILT
