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Geranylgeranyl transferase type-2 subunit beta 2 (EC 2.5.1.60) (Geranylgeranyl transferase type II subunit beta 2) (Rab geranylgeranyl transferase beta subunit 2) (AtRGTB2) (Rab-GGT beta 2)

 PGTB2_ARATH             Reviewed;         317 AA.
Q9LHL5; Q8LFX5;
06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
05-JUL-2017, entry version 118.
RecName: Full=Geranylgeranyl transferase type-2 subunit beta 2 {ECO:0000305};
EC=2.5.1.60 {ECO:0000269|PubMed:25316062};
AltName: Full=Geranylgeranyl transferase type II subunit beta 2 {ECO:0000305};
AltName: Full=Rab geranylgeranyl transferase beta subunit 2 {ECO:0000303|PubMed:25316062};
Short=AtRGTB2 {ECO:0000303|PubMed:25316062};
Short=Rab-GGT beta 2 {ECO:0000305};
Name=RGTB2 {ECO:0000303|PubMed:25316062};
OrderedLocusNames=At3g12070 {ECO:0000312|Araport:AT3G12070};
ORFNames=T21B14.11 {ECO:0000312|EMBL:AAG51055.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10907853; DOI=10.1093/dnares/7.3.217;
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 3. II.
Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC
and BAC clones.";
DNA Res. 7:217-221(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
"Arabidopsis ORF Clones.";
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=25316062; DOI=10.1093/jxb/eru412;
Gutkowska M., Wnuk M., Nowakowska J., Lichocka M., Stronkowski M.M.,
Swiezewska E.;
"Rab geranylgeranyl transferase beta subunit is essential for male
fertility and tip growth in Arabidopsis.";
J. Exp. Bot. 66:213-224(2015).
[7]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AND SUBUNIT.
PubMed=26589801; DOI=10.1074/jbc.M115.673491;
Shi W., Zeng Q., Kunkel B.N., Running M.P.;
"Arabidopsis Rab geranylgeranyltransferases demonstrate redundancy and
broad substrate specificity in vitro.";
J. Biol. Chem. 291:1398-1410(2016).
-!- FUNCTION: Catalyzes the transfer of a geranylgeranyl moiety from
geranylgeranyl diphosphate to both cysteines of Rab proteins with
the C-terminal sequence -CCXX, CXXX, -XCCX and -XCXC, such as
RABA1A, RABA2A, RABF2A and RABG2 (PubMed:26589801). In vitro, can
prenylate PGGTI targets with the C-terminal sequence Cys-
aliphatic-aliphatic-X (CaaX) with leucine in the terminal
position. Substrates with the C-terminal sequence -CSIL such as
ARAC11/ROP1 or GG2/AGG2 are prenylated independently of REP and
when the beta subunit is associated with the alpha subunit RGTA1
(PubMed:26589801). {ECO:0000269|PubMed:26589801}.
-!- FUNCTION: Required for male fertility and root tip growth.
{ECO:0000269|PubMed:25316062}.
-!- CATALYTIC ACTIVITY: Geranylgeranyl diphosphate + protein-cysteine
= S-geranylgeranyl-protein + diphosphate.
{ECO:0000269|PubMed:26589801}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P53610};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P53610};
-!- ENZYME REGULATION: The enzymatic reaction requires the aid of the
Rab escort protein REP. {ECO:0000269|PubMed:26589801}.
-!- SUBUNIT: Heterotrimer composed of the alpha subunit RGTA, the beta
subunit RGTB and REP; within this trimer, RGTA and RGTB form the
catalytic component, while REP mediates peptide substrate binding.
{ECO:0000269|PubMed:26589801}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
conditions. The double mutant plants rgtb1 and rgtb2 are male
sterile, due to shrunken pollen with abnormal exine structure, and
strong disorganization of the endoplasmic reticulum membranes.
{ECO:0000269|Ref.5}.
-!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
family. {ECO:0000305}.
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EMBL; AP002040; BAB03119.1; -; Genomic_DNA.
EMBL; AP002063; BAB03119.1; JOINED; Genomic_DNA.
EMBL; AC069473; AAG51055.1; -; Genomic_DNA.
EMBL; CP002686; AEE75144.1; -; Genomic_DNA.
EMBL; CP002686; AEE75145.1; -; Genomic_DNA.
EMBL; CP002686; ANM65899.1; -; Genomic_DNA.
EMBL; BT028896; ABI49443.1; -; mRNA.
EMBL; AY084593; AAM61158.1; -; mRNA.
RefSeq; NP_001327836.1; NM_001337972.1.
RefSeq; NP_187814.1; NM_112041.3.
RefSeq; NP_850567.1; NM_180236.4.
UniGene; At.39649; -.
ProteinModelPortal; Q9LHL5; -.
SMR; Q9LHL5; -.
STRING; 3702.AT3G12070.1; -.
PaxDb; Q9LHL5; -.
PRIDE; Q9LHL5; -.
EnsemblPlants; AT3G12070.1; AT3G12070.1; AT3G12070.
EnsemblPlants; AT3G12070.2; AT3G12070.2; AT3G12070.
EnsemblPlants; AT3G12070.3; AT3G12070.3; AT3G12070.
GeneID; 820381; -.
Gramene; AT3G12070.1; AT3G12070.1; AT3G12070.
Gramene; AT3G12070.2; AT3G12070.2; AT3G12070.
Gramene; AT3G12070.3; AT3G12070.3; AT3G12070.
KEGG; ath:AT3G12070; -.
Araport; AT3G12070; -.
TAIR; locus:2088614; AT3G12070.
eggNOG; KOG0366; Eukaryota.
eggNOG; COG5029; LUCA.
KO; K05956; -.
OMA; WWILSAL; -.
OrthoDB; EOG09360FD0; -.
PhylomeDB; Q9LHL5; -.
Reactome; R-ATH-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
Reactome; R-ATH-8873719; RAB geranylgeranylation.
PRO; PR:Q9LHL5; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9LHL5; baseline and differential.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IDA:UniProtKB.
GO; GO:0009555; P:pollen development; IMP:UniProtKB.
GO; GO:0018344; P:protein geranylgeranylation; IDA:UniProtKB.
GO; GO:0048364; P:root development; IMP:UniProtKB.
CDD; cd02894; GGTase-II; 1.
InterPro; IPR001330; PFTB_repeat.
InterPro; IPR026873; Ptb1.
InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
Pfam; PF00432; Prenyltrans; 5.
SUPFAM; SSF48239; SSF48239; 1.
1: Evidence at protein level;
Complete proteome; Metal-binding; Prenyltransferase;
Reference proteome; Repeat; Transferase.
CHAIN 1 317 Geranylgeranyl transferase type-2 subunit
beta 2.
/FTId=PRO_0000436612.
REPEAT 7 50 PFTB 1. {ECO:0000255}.
REPEAT 57 98 PFTB 2. {ECO:0000255}.
REPEAT 105 146 PFTB 3. {ECO:0000255}.
REPEAT 153 194 PFTB 4. {ECO:0000255}.
REPEAT 201 243 PFTB 5. {ECO:0000255}.
REPEAT 250 292 PFTB 6. {ECO:0000255}.
REGION 179 181 Geranylgeranyl diphosphate binding.
{ECO:0000250|UniProtKB:P53610}.
REGION 222 225 Geranylgeranyl diphosphate binding.
{ECO:0000250|UniProtKB:P53610}.
REGION 231 234 Geranylgeranyl diphosphate binding.
{ECO:0000250|UniProtKB:P53610}.
METAL 228 228 Zinc; catalytic.
{ECO:0000250|UniProtKB:P53610}.
METAL 230 230 Zinc; catalytic.
{ECO:0000250|UniProtKB:P53610}.
METAL 280 280 Zinc; via tele nitrogen; catalytic.
{ECO:0000250|UniProtKB:P53610}.
CONFLICT 8 8 G -> D (in Ref. 5; AAM61158).
{ECO:0000305}.
SEQUENCE 317 AA; 35193 MW; 02705755FF230843 CRC64;
MADKLVAGKH LRYILNLMAE KKKESFESVV MDHLRMNGAY WGLTTLALLD KLGSVSEDEV
VSWVMTCQHE SGGFAGNTGH DPHVLYTLSA VQILALFDKL NILDVEKVSN YIAGLQNEDG
SFSGDIWGEV DTRFSYIAIC CLSILKCLDK INVKKAVDYI VSCKNLDGGF GCSPGAESHA
GQIFCCVGAL AITGNLHRVD KDLLGWWLCE RQDYESGGLN GRPEKLPDVC YSWWVLSSLI
MIDRVHWIEK AKLVKFILDS QDMDNGGISD RPSYTVDIFH TYFGVAGLSL LEYPGVKTID
PAYALPVHVI NRILFTK


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