ARF3_ARATH
ID ARF3_ARATH Reviewed; 182 AA.
AC P40940; A8MRA0; Q541X9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=ADP-ribosylation factor 3;
DE Short=AtARF3;
DE AltName: Full=Protein ARF-LIKE 1;
DE Short=AtARL1;
GN Name=ARF3; Synonyms=ARL1; OrderedLocusNames=At2g24765;
GN ORFNames=F27A10.8, F27C12.31;
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 [MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=7991702; DOI=10.1104/pp.106.2.809;
RA Lebas M., Axelos M.;
RT "A cDNA encoding a new GTP-binding protein of the ADP-ribosylation factor
RT family from Arabidopsis.";
RL Plant Physiol. 106:809-810(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-79 AND 161-182 (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
RN [7]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF THR-31 AND GLN-71, AND INTERACTION
RP WITH GRIP.
RX PubMed=16236155; DOI=10.1111/j.1365-313x.2005.02542.x;
RA Latijnhouwers M., Hawes C., Carvalho C., Oparka K., Gillingham A.K.,
RA Boevink P.;
RT "An Arabidopsis GRIP domain protein locates to the trans-Golgi and binds
RT the small GTPase ARL1.";
RL Plant J. 44:459-470(2005).
RN [8]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-2; THR-31; PHE-51; GLN-71 AND
RP TYR-81, MYRISTOYLATION AT GLY-2, AND INTERACTION WITH GRIP.
RX PubMed=16830178; DOI=10.1007/s11103-006-0022-y;
RA Stefano G., Renna L., Hanton S.L., Chatre L., Haas T.A., Brandizzi F.;
RT "ARL1 plays a role in the binding of the GRIP domain of a peripheral matrix
RT protein to the Golgi apparatus in plant cells.";
RL Plant Mol. Biol. 61:431-449(2006).
CC -!- FUNCTION: GTP-binding protein involved in protein trafficking; may
CC modulate vesicle budding and uncoating within the Golgi apparatus.
CC -!- SUBUNIT: Interacts with GRIP; but preferentially when bound to GTP.
CC {ECO:0000269|PubMed:16236155, ECO:0000269|PubMed:16830178}.
CC -!- INTERACTION:
CC P40940; Q8S2T0: GRIP; NbExp=5; IntAct=EBI-1537890, EBI-1537908;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:16236155,
CC ECO:0000269|PubMed:16830178}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P40940-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P40940-2; Sequence=VSP_035207, VSP_035208;
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM15297.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM15475.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X77385; CAA54564.1; -; mRNA.
DR EMBL; AC006585; AAM15297.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007266; AAM15475.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07625.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07626.1; -; Genomic_DNA.
DR EMBL; AY063840; AAL36196.1; -; mRNA.
DR EMBL; AY150410; AAN12955.1; -; mRNA.
DR EMBL; AK117735; BAC42384.1; -; mRNA.
DR EMBL; Z25825; CAA81067.1; -; mRNA.
DR EMBL; Z25549; CAA80991.1; -; mRNA.
DR PIR; S41938; S41938.
DR RefSeq; NP_001077955.1; NM_001084486.1. [P40940-2]
DR RefSeq; NP_850057.1; NM_179726.3. [P40940-1]
DR AlphaFoldDB; P40940; -.
DR SMR; P40940; -.
DR BioGRID; 2366; 3.
DR IntAct; P40940; 4.
DR STRING; 3702.AT2G24765.1; -.
DR iPTMnet; P40940; -.
DR PaxDb; P40940; -.
DR PRIDE; P40940; -.
DR ProteomicsDB; 245185; -. [P40940-1]
DR EnsemblPlants; AT2G24765.1; AT2G24765.1; AT2G24765. [P40940-1]
DR EnsemblPlants; AT2G24765.2; AT2G24765.2; AT2G24765. [P40940-2]
DR GeneID; 817014; -.
DR Gramene; AT2G24765.1; AT2G24765.1; AT2G24765. [P40940-1]
DR Gramene; AT2G24765.2; AT2G24765.2; AT2G24765. [P40940-2]
DR KEGG; ath:AT2G24765; -.
DR Araport; AT2G24765; -.
DR TAIR; locus:2827399; AT2G24765.
DR eggNOG; KOG0070; Eukaryota.
DR HOGENOM; CLU_040729_9_3_1; -.
DR OMA; QEGMDWL; -.
DR PhylomeDB; P40940; -.
DR PRO; PR:P40940; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P40940; baseline and differential.
DR Genevisible; P40940; AT.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0005795; C:Golgi stack; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR024156; Small_GTPase_ARF.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR PANTHER; PTHR11711; PTHR11711; 1.
DR Pfam; PF00025; Arf; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51417; ARF; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ER-Golgi transport; Golgi apparatus; GTP-binding;
KW Lipoprotein; Myristate; Nucleotide-binding; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:16830178"
FT CHAIN 2..182
FT /note="ADP-ribosylation factor 3"
FT /id="PRO_0000207427"
FT BINDING 24..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 67..71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000305|PubMed:16830178"
FT VAR_SEQ 129..135
FT /note="DLPGALD -> KPWSCIR (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_035207"
FT VAR_SEQ 136..182
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_035208"
FT MUTAGEN 2
FT /note="G->A: Loss of Golgi targeting."
FT /evidence="ECO:0000269|PubMed:16830178"
FT MUTAGEN 31
FT /note="T->N: GDP-restricted form; no effect on targeting."
FT /evidence="ECO:0000269|PubMed:16236155,
FT ECO:0000269|PubMed:16830178"
FT MUTAGEN 51
FT /note="F->G: Reduced interaction with GRIP, but no effect
FT on targeting."
FT /evidence="ECO:0000269|PubMed:16830178"
FT MUTAGEN 71
FT /note="Q->L: GTP-restriced form; no effect on targeting."
FT /evidence="ECO:0000269|PubMed:16236155,
FT ECO:0000269|PubMed:16830178"
FT MUTAGEN 81
FT /note="Y->G: Reduced interaction with GRIP, but no effect
FT on targeting."
FT /evidence="ECO:0000269|PubMed:16830178"
SQ SEQUENCE 182 AA; 20242 MW; F5271FBBC69BAD7D CRC64;
MGILFTRMFS SVFGNKEARI LVLGLDNAGK TTILYRLQMG EVVSTIPTIG FNVETVQYNN
IKFQVWDLGG QTSIRPYWRC YFPNTQAVIY VVDSSDTDRI GVAKEEFHAI LEEDELKGAV
VLIFANKQDL PGALDDAAVT EALELHKIKS RQWAIFKTCA VKGEGLFEGL DWLSNTLKSG
SG
