PGTA1_ARATH
ID PGTA1_ARATH Reviewed; 678 AA.
AC Q8VYB7; B9DHR9; Q9M0L4; Q9SB46; Q9STU6;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Geranylgeranyl transferase type-2 subunit alpha 1 {ECO:0000305};
DE EC=2.5.1.60 {ECO:0000269|PubMed:26589801};
DE AltName: Full=Geranylgeranyl transferase type II subunit alpha 1 {ECO:0000305};
DE AltName: Full=Rab geranylgeranyl transferase alpha subunit 1 {ECO:0000303|PubMed:26589801};
DE Short=AtRGTA1 {ECO:0000303|PubMed:26589801};
DE Short=Rab-GGT alpha 1 {ECO:0000305};
GN Name=RGTA1 {ECO:0000303|PubMed:26589801};
GN OrderedLocusNames=At4g24490 {ECO:0000312|Araport:AT4G24490};
GN ORFNames=F22K18.310 {ECO:0000312|EMBL:CAA23014.1},
GN T22A6.320 {ECO:0000312|EMBL:CAB45084.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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] OF 216-678.
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
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 Cys-aliphatic-aliphatic-X (CaaX) with
CC leucine in the terminal position. Substrates with the C-terminal
CC sequence -CSIL such as ARAC11/ROP1 or GG2/AGG2 are prenylated
CC independently of REP and when the alpha subunit is associated with a
CC beta subunit (RGTB1 or RGTB2) (PubMed:26589801).
CC {ECO:0000269|PubMed:26589801}.
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 -!- 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 -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA23014.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB45084.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79359.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL035356; CAA23014.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL078637; CAB45084.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161561; CAB79359.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84913.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84914.1; -; Genomic_DNA.
DR EMBL; AY072209; AAL60030.1; -; mRNA.
DR EMBL; AY117358; AAM51433.1; -; mRNA.
DR EMBL; AK317624; BAH20286.1; -; mRNA.
DR PIR; C85282; C85282.
DR PIR; T05585; T05585.
DR PIR; T09912; T09912.
DR RefSeq; NP_001078443.1; NM_001084974.1.
DR RefSeq; NP_194180.2; NM_118582.4.
DR AlphaFoldDB; Q8VYB7; -.
DR SMR; Q8VYB7; -.
DR STRING; 3702.AT4G24490.1; -.
DR PaxDb; Q8VYB7; -.
DR PRIDE; Q8VYB7; -.
DR ProteomicsDB; 235050; -.
DR EnsemblPlants; AT4G24490.1; AT4G24490.1; AT4G24490.
DR EnsemblPlants; AT4G24490.2; AT4G24490.2; AT4G24490.
DR GeneID; 828551; -.
DR Gramene; AT4G24490.1; AT4G24490.1; AT4G24490.
DR Gramene; AT4G24490.2; AT4G24490.2; AT4G24490.
DR KEGG; ath:AT4G24490; -.
DR Araport; AT4G24490; -.
DR TAIR; locus:2121860; AT4G24490.
DR eggNOG; KOG0529; Eukaryota.
DR HOGENOM; CLU_024090_0_0_1; -.
DR InParanoid; Q8VYB7; -.
DR OMA; YNEIGSH; -.
DR OrthoDB; 1527547at2759; -.
DR PhylomeDB; Q8VYB7; -.
DR BRENDA; 2.5.1.60; 399.
DR PRO; PR:Q8VYB7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8VYB7; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IDA:UniProtKB.
DR GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IDA:UniProtKB.
DR GO; GO:0018344; P:protein geranylgeranylation; IDA:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002088; Prenyl_trans_a.
DR Pfam; PF01239; PPTA; 5.
DR PROSITE; PS51450; LRR; 5.
DR PROSITE; PS51147; PFTA; 5.
PE 1: Evidence at protein level;
KW Leucine-rich repeat; Prenyltransferase; Reference proteome; Repeat;
KW Transferase.
FT CHAIN 1..678
FT /note="Geranylgeranyl transferase type-2 subunit alpha 1"
FT /id="PRO_0000436609"
FT REPEAT 40..74
FT /note="PFTA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00488"
FT REPEAT 86..120
FT /note="PFTA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00488"
FT REPEAT 121..155
FT /note="PFTA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00488"
FT REPEAT 156..190
FT /note="PFTA 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00488"
FT REPEAT 201..235
FT /note="PFTA 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00488"
FT REPEAT 510..532
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 533..554
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 555..578
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 580..604
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 638..663
FT /note="LRR 5"
FT /evidence="ECO:0000255"
SQ SEQUENCE 678 AA; 76909 MW; EF7524233E88FC55 CRC64;
MHGRPRNASK PEEEAASAAK AVQLRSLQSQ FMTNHHDKIY TNEAIELSTK LLEINPEAYT
AWNYRKLAVE DRLARIEPDP NLVSAILDEE LRVVESALRQ NFKSYGAWHH RKWVLSKGHS
SVGNELRLLE KFQKLDSRNF HAWNYRRFVV ELTNRSEQDE LQYTDDMINN NFSNYSAWHN
RSVLLSSLLA QNADGFMPNI KIPEEYDFVH SAIFTEPDDQ SGWFYHLWLL DQTLNVETPL
LTSSWPSHGS SIILSGAGCL SGSSSMFTTF CSESGSFPLI LYFDQAVGGV SSSTVTIDSE
LKGNEGLVWE PIPNKNSQVS CVWVARLKYV SSDPCEYKVK IRVGNSPGIV SSRGYNFNAP
YEFVFTAHVH DTVEDSQEGI VSWTDGFDIW DAKSKDLNSL VTLDRLNAEM DFKWRQEAID
SEVECFGILP DSKIGKLTLA RLLMAREAMV SDDAVKGVHY EEILQLYNDL MALDSSHYQY
YKDEHSKAFL HKVTSSSESL SRHLLRYRDM NNLVCLRLNN LSLSRIASVE KLLFVQMLDL
SHNELHSTEG LEAMQLLSCL NLSHNRIRSF SALDSLRHVK QLKVLDVSHN HIGKHSVDTT
RYLCSSPLSN SELGQDDVGK QNPGLVTKYW DAYCVLTDLN LKQLDIAGNE IAGEEFSSFV
LQVVPKLVWL DGQKKLGN
