PGTB2_ARATH
ID PGTB2_ARATH Reviewed; 317 AA.
AC Q9LHL5; Q8LFX5;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Geranylgeranyl transferase type-2 subunit beta 2 {ECO:0000305};
DE EC=2.5.1.60 {ECO:0000269|PubMed:25316062};
DE AltName: Full=Geranylgeranyl transferase type II subunit beta 2 {ECO:0000305};
DE AltName: Full=Rab geranylgeranyl transferase beta subunit 2 {ECO:0000303|PubMed:25316062};
DE Short=AtRGTB2 {ECO:0000303|PubMed:25316062};
DE Short=Rab-GGT beta 2 {ECO:0000305};
GN Name=RGTB2 {ECO:0000303|PubMed:25316062};
GN OrderedLocusNames=At3g12070 {ECO:0000312|Araport:AT3G12070};
GN ORFNames=T21B14.11 {ECO:0000312|EMBL:AAG51055.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25316062; DOI=10.1093/jxb/eru412;
RA Gutkowska M., Wnuk M., Nowakowska J., Lichocka M., Stronkowski M.M.,
RA Swiezewska E.;
RT "Rab geranylgeranyl transferase beta subunit is essential for male
RT fertility and tip growth in Arabidopsis.";
RL J. Exp. Bot. 66:213-224(2015).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=26589801; DOI=10.1074/jbc.m115.673491;
RA Shi W., Zeng Q., Kunkel B.N., Running M.P.;
RT "Arabidopsis Rab geranylgeranyltransferases demonstrate redundancy and
RT broad substrate specificity in vitro.";
RL J. Biol. Chem. 291:1398-1410(2016).
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 -CCXX, CXXX, -XCCX and -XCXC, such as RABA1A,
CC RABA2A, RABF2A and RABG2 (PubMed:26589801). In vitro, can prenylate
CC PGGTI targets with the C-terminal sequence Cys-aliphatic-aliphatic-X
CC (CaaX) with leucine in the terminal position. Substrates with the C-
CC terminal sequence -CSIL such as ARAC11/ROP1 or GG2/AGG2 are prenylated
CC independently of REP and when the beta subunit is associated with the
CC alpha subunit RGTA1 (PubMed:26589801). {ECO:0000269|PubMed:26589801}.
CC -!- FUNCTION: Required for male fertility and root tip growth.
CC {ECO:0000269|PubMed:25316062}.
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 Evidence={ECO:0000269|PubMed:26589801};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P53610};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P53610};
CC -!- ACTIVITY REGULATION: The enzymatic reaction requires the aid of the Rab
CC escort protein REP. {ECO:0000269|PubMed:26589801}.
CC -!- SUBUNIT: Heterotrimer composed of the alpha subunit RGTA, the beta
CC subunit RGTB and REP; within this trimer, RGTA and RGTB form the
CC catalytic component, while REP mediates peptide substrate binding.
CC {ECO:0000269|PubMed:26589801}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. The double mutant plants rgtb1 and rgtb2 are male sterile,
CC due to shrunken pollen with abnormal exine structure, and strong
CC disorganization of the endoplasmic reticulum membranes.
CC {ECO:0000269|Ref.5}.
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC family. {ECO:0000305}.
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DR EMBL; AP002040; BAB03119.1; -; Genomic_DNA.
DR EMBL; AP002063; BAB03119.1; JOINED; Genomic_DNA.
DR EMBL; AC069473; AAG51055.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75144.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75145.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65899.1; -; Genomic_DNA.
DR EMBL; BT028896; ABI49443.1; -; mRNA.
DR EMBL; AY084593; AAM61158.1; -; mRNA.
DR RefSeq; NP_001327836.1; NM_001337972.1.
DR RefSeq; NP_187814.1; NM_112041.3.
DR RefSeq; NP_850567.1; NM_180236.4.
DR AlphaFoldDB; Q9LHL5; -.
DR SMR; Q9LHL5; -.
DR STRING; 3702.AT3G12070.1; -.
DR PaxDb; Q9LHL5; -.
DR PRIDE; Q9LHL5; -.
DR ProteomicsDB; 235101; -.
DR EnsemblPlants; AT3G12070.1; AT3G12070.1; AT3G12070.
DR EnsemblPlants; AT3G12070.2; AT3G12070.2; AT3G12070.
DR EnsemblPlants; AT3G12070.3; AT3G12070.3; AT3G12070.
DR GeneID; 820381; -.
DR Gramene; AT3G12070.1; AT3G12070.1; AT3G12070.
DR Gramene; AT3G12070.2; AT3G12070.2; AT3G12070.
DR Gramene; AT3G12070.3; AT3G12070.3; AT3G12070.
DR KEGG; ath:AT3G12070; -.
DR Araport; AT3G12070; -.
DR TAIR; locus:2088614; AT3G12070.
DR eggNOG; KOG0366; Eukaryota.
DR HOGENOM; CLU_028946_3_0_1; -.
DR InParanoid; Q9LHL5; -.
DR OMA; ICSCEIL; -.
DR OrthoDB; 1042804at2759; -.
DR PhylomeDB; Q9LHL5; -.
DR BRENDA; 2.5.1.60; 399.
DR PRO; PR:Q9LHL5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LHL5; baseline and differential.
DR GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009555; P:pollen development; IMP:UniProtKB.
DR GO; GO:0018344; P:protein geranylgeranylation; IDA:UniProtKB.
DR GO; GO:0018342; P:protein prenylation; IBA:GO_Central.
DR GO; GO:0048364; P:root development; IMP:UniProtKB.
DR CDD; cd02894; GGTase-II; 1.
DR InterPro; IPR001330; PFTB_repeat.
DR InterPro; IPR045089; PGGT1B-like.
DR InterPro; IPR026873; Ptb1.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11774; PTHR11774; 1.
DR Pfam; PF00432; Prenyltrans; 5.
DR SUPFAM; SSF48239; SSF48239; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Prenyltransferase; Reference proteome; Repeat; Transferase;
KW Zinc.
FT CHAIN 1..317
FT /note="Geranylgeranyl transferase type-2 subunit beta 2"
FT /id="PRO_0000436612"
FT REPEAT 7..50
FT /note="PFTB 1"
FT /evidence="ECO:0000255"
FT REPEAT 57..98
FT /note="PFTB 2"
FT /evidence="ECO:0000255"
FT REPEAT 105..146
FT /note="PFTB 3"
FT /evidence="ECO:0000255"
FT REPEAT 153..194
FT /note="PFTB 4"
FT /evidence="ECO:0000255"
FT REPEAT 201..243
FT /note="PFTB 5"
FT /evidence="ECO:0000255"
FT REPEAT 250..292
FT /note="PFTB 6"
FT /evidence="ECO:0000255"
FT BINDING 179..181
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 222..225
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 231..234
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT CONFLICT 8
FT /note="G -> D (in Ref. 5; AAM61158)"
FT /evidence="ECO:0000305"
SQ 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
