PGTA_PIG
ID PGTA_PIG Reviewed; 567 AA.
AC A5A779;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Okumura N., Matsumoto T., Hamasima N., Uenishi H., Ogawa T., Komatsuda A.,
RA Fukudome N., Ide H., Suzuki A., Kojima C., Awata T.;
RT "Sequences and genetic variations of fourty-four porcine coat color related
RT genes.";
RL Submitted (SEP-2006) 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 (By similarity).
CC Interacts with non-phosphorylated form of RAB8A; phosphorylation of
CC RAB8A disrupts this interaction (By similarity).
CC {ECO:0000250|UniProtKB:Q92696}.
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
CC family. {ECO:0000305}.
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DR EMBL; AB271949; BAF62324.1; -; mRNA.
DR RefSeq; NP_001092063.1; NM_001098593.1.
DR RefSeq; XP_005666280.1; XM_005666223.2.
DR AlphaFoldDB; A5A779; -.
DR SMR; A5A779; -.
DR STRING; 9823.ENSSSCP00000002178; -.
DR PaxDb; A5A779; -.
DR PeptideAtlas; A5A779; -.
DR PRIDE; A5A779; -.
DR Ensembl; ENSSSCT00000002230; ENSSSCP00000002178; ENSSSCG00000001992.
DR Ensembl; ENSSSCT00005025033; ENSSSCP00005015104; ENSSSCG00005015999.
DR Ensembl; ENSSSCT00005025120; ENSSSCP00005015164; ENSSSCG00005015999.
DR Ensembl; ENSSSCT00070006142; ENSSSCP00070005016; ENSSSCG00070003166.
DR GeneID; 100049679; -.
DR KEGG; ssc:100049679; -.
DR CTD; 5875; -.
DR VGNC; VGNC:92046; RABGGTA.
DR eggNOG; KOG0529; Eukaryota.
DR GeneTree; ENSGT00550000075121; -.
DR HOGENOM; CLU_031996_3_2_1; -.
DR InParanoid; A5A779; -.
DR OMA; YNAWHHR; -.
DR OrthoDB; 1527547at2759; -.
DR TreeFam; TF315057; -.
DR Proteomes; UP000008227; Chromosome 7.
DR Proteomes; UP000314985; Chromosome 7.
DR Bgee; ENSSSCG00000001992; Expressed in longissimus lumborum muscle and 40 other tissues.
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_0000331286"
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; 64901 MW; 79BFCA2DD50C4F97 CRC64;
MHGRLKVKTS EEQAEAKRLE REQKLKLYQT ATQTVFQKRQ AGELDESVLE LTSQILGANP
DFATLWNCRR EVLQRLEVQK SPEELAALVK AELGFLESCL RVNPKSYGTW HHRCWLLGRL
PEPNWARELE LCARFLEVDE RNFHCWDYRR FVASQAAVPP AEELAFTDSL ITRNFSNYSS
WHYRSCLLPQ LHPQPDSGPQ GRLPEDVLLK ELELVQNAFF TDPNDQSAWF YHRWLLGRAD
PQDALRCLHV SRDEACLTVS FSRPLLVGPS TETLLLMVNE SPLSVEWRTP DGRNRPSHVW
LCDLPAASLN DHLPQHTFRV IWTAGNAQKE CVLLKGRQEG WCRDSATDEQ LFRCELSVEK
STVLQSELES CKELQELEPE NKWCLLTIIL LMRALDPLLY EKETLQYFQT LKAVDPMRAA
YLDDLRSKFL LENSVLKMEY ADVRVLHLGH KDLTVLCHLE QLLLVTHLDL SHNRLRALPP
ALAALRCLEV LQANDNAIES LDGVTNLPRL QELSLCNNRL QQPAVLQPLA SCPRLVLLNL
QDNPLCQAVG ISEHLAELLP SVSSILT
