PG2B1_ARATH
ID PG2B1_ARATH Reviewed; 321 AA.
AC Q84J75; Q9FMP2;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Geranylgeranyl transferase type-2 subunit beta 1 {ECO:0000305};
DE EC=2.5.1.60 {ECO:0000269|PubMed:20180921};
DE AltName: Full=Geranylgeranyl transferase type II subunit beta 1 {ECO:0000305};
DE AltName: Full=Rab geranylgeranyl transferase beta subunit 1 {ECO:0000303|PubMed:20180921};
DE Short=AtRGTB1 {ECO:0000303|PubMed:20180921};
DE Short=Rab-GGT beta 1 {ECO:0000305};
GN Name=RGTB1 {ECO:0000303|PubMed:20180921};
GN OrderedLocusNames=At5g12210 {ECO:0000312|Araport:AT5G12210};
GN ORFNames=MXC9.17 {ECO:0000312|EMBL:BAB10039.1};
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-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=20180921; DOI=10.1111/j.1365-313x.2010.04172.x;
RA Hala M., Soukupova H., Synek L., Zarsky V.;
RT "Arabidopsis RAB geranylgeranyl transferase beta-subunit mutant is
RT constitutively photomorphogenic, and has shoot growth and gravitropic
RT defects.";
RL Plant J. 62:615-627(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
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 [9]
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). Involved in the
CC geranylgeranylation of RABA2A (PubMed:20180921). In vitro, can
CC prenylate PGGTI targets with the C-terminal sequence Cys-aliphatic-
CC aliphatic-X (CaaX) with leucine in the terminal position. Substrates
CC with the C-terminal sequence -CSIL such as ARAC11/ROP1 or GG2/AGG2 are
CC prenylated independently of REP and when the beta subunit is associated
CC with the alpha subunit RGTA1 (PubMed:26589801).
CC {ECO:0000269|PubMed:20180921, 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P18898};
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q84J75-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Pleiotropic effects on plant growth and
CC development, including dwarf size, aberrant root development, multiple
CC inflorescence stems and small siliques mostly sterile. Impaired shoot
CC gravitropism and photomorphogenesis (PubMed:20180921). The double
CC mutant plants rgtb1 and rgtb2 are male sterile, due to shrunken pollen
CC with abnormal exine structure, and strong disorganization of the
CC endoplasmic reticulum membranes (PubMed:25316062).
CC {ECO:0000269|PubMed:20180921, ECO:0000269|PubMed:25316062}.
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM65965.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB10039.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB007727; BAB10039.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED91774.1; -; Genomic_DNA.
DR EMBL; BT004816; AAO44082.1; -; mRNA.
DR EMBL; BT004818; AAO44084.1; -; mRNA.
DR EMBL; AK227802; BAE99784.1; -; mRNA.
DR EMBL; AY088429; AAM65965.1; ALT_INIT; mRNA.
DR RefSeq; NP_568259.1; NM_121259.4. [Q84J75-1]
DR AlphaFoldDB; Q84J75; -.
DR SMR; Q84J75; -.
DR STRING; 3702.AT5G12210.1; -.
DR iPTMnet; Q84J75; -.
DR PaxDb; Q84J75; -.
DR PRIDE; Q84J75; -.
DR ProteomicsDB; 236787; -. [Q84J75-1]
DR EnsemblPlants; AT5G12210.1; AT5G12210.1; AT5G12210. [Q84J75-1]
DR GeneID; 831094; -.
DR Gramene; AT5G12210.1; AT5G12210.1; AT5G12210. [Q84J75-1]
DR KEGG; ath:AT5G12210; -.
DR Araport; AT5G12210; -.
DR TAIR; locus:2177058; AT5G12210.
DR eggNOG; KOG0366; Eukaryota.
DR InParanoid; Q84J75; -.
DR PhylomeDB; Q84J75; -.
DR BRENDA; 2.5.1.60; 399.
DR PRO; PR:Q84J75; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84J75; 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:0010315; P:auxin export across the plasma membrane; IMP:TAIR.
DR GO; GO:0010252; P:auxin homeostasis; IMP:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR GO; GO:0009960; P:endosperm development; IMP:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:UniProtKB.
DR GO; GO:0010183; P:pollen tube guidance; IMP:TAIR.
DR GO; GO:0140301; P:pollen-stigma interaction; IMP:TAIR.
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 GO; GO:0010214; P:seed coat development; IMP:TAIR.
DR GO; GO:0048316; P:seed development; IMP:TAIR.
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 Acetylation; Alternative splicing; Magnesium; Metal-binding;
KW Prenyltransferase; Reference proteome; Repeat; Transferase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..321
FT /note="Geranylgeranyl transferase type-2 subunit beta 1"
FT /id="PRO_0000436611"
FT REPEAT 14..55
FT /note="PFTB 1"
FT /evidence="ECO:0000255"
FT REPEAT 62..103
FT /note="PFTB 2"
FT /evidence="ECO:0000255"
FT REPEAT 110..151
FT /note="PFTB 3"
FT /evidence="ECO:0000255"
FT REPEAT 158..199
FT /note="PFTB 4"
FT /evidence="ECO:0000255"
FT REPEAT 206..247
FT /note="PFTB 5"
FT /evidence="ECO:0000255"
FT REPEAT 254..296
FT /note="PFTB 6"
FT /evidence="ECO:0000255"
FT BINDING 184..186
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 226..229
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 235..238
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 321 AA; 35496 MW; E51D6FB0938EB898 CRC64;
MSSTSSSQMV QLVADKHVRY ILMAEKKKES FESVVMDHLR MNGAYWGLTT LDLLDKLGCV
SEEEVISWLM TCQHESGGFA GNTGHDPHIL YTLSAVQILA LFDKINILDI GKVSSYVAKL
QNEDGSFSGD MWGEIDTRFS YIAICCLSIL KCLDKINVEK AVKYIVSCKN LDGGFGCTPG
AESHAGQIFC CVGALAITGS LHHVDKDSLG WWLCERQLKA GGLNGRPEKL ADVCYSWWVL
SSLIMIDRVH WIDKAKLVKF ILDCQDLDNG GISDRPEDAV DIFHTYFGVA GLSLLEYPGV
KVIDPAYALP VDVVNRIIFT K
