AGD10_ARATH
ID AGD10_ARATH Reviewed; 395 AA.
AC O82171; Q3EBM9;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein AGD10;
DE Short=ARF GAP AGD10;
DE AltName: Full=Protein ARF-GAP DOMAIN 10;
DE Short=AtAGD10;
DE AltName: Full=Protein MATERNAL EFFECT EMBRYO ARREST 28;
DE AltName: Full=Protein ROOT AND POLLEN ARFGAP;
GN Name=AGD10; Synonyms=MEE28, RPA; OrderedLocusNames=At2g35210;
GN ORFNames=T4C15.12;
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=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 [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] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12644670; DOI=10.1104/pp.013052;
RA Vernoud V., Horton A.C., Yang Z., Nielsen E.;
RT "Analysis of the small GTPase gene superfamily of Arabidopsis.";
RL Plant Physiol. 131:1191-1208(2003).
RN [6]
RP FUNCTION.
RX PubMed=15634699; DOI=10.1242/dev.01595;
RA Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S., Johnson C.S.,
RA Capron A., Xie L.-F., Ye D., Sundaresan V.;
RT "Genetic and molecular identification of genes required for female
RT gametophyte development and function in Arabidopsis.";
RL Development 132:603-614(2005).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16731582; DOI=10.1104/pp.106.077818;
RA Song X.-F., Yang C.-Y., Liu J., Yang W.-C.;
RT "RPA, a class II ARFGAP protein, activates ARF1 and U5 and plays a role in
RT root hair development in Arabidopsis.";
RL Plant Physiol. 141:966-976(2006).
CC -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor
CC (ARF). Activates ARF1 and ARF2. Required for female gametophyte
CC development. Involved in root hair and pollen tube growth.
CC {ECO:0000269|PubMed:15634699, ECO:0000269|PubMed:16731582}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:16731582}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O82171-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O82171-2; Sequence=VSP_035551, VSP_035552;
CC -!- TISSUE SPECIFICITY: Expressed specifically in roots, pollen grains and
CC pollen tubes. {ECO:0000269|PubMed:16731582}.
CC -!- DOMAIN: The C-terminal domain (317-395) is responsible for the Golgi
CC localization.
CC -!- DISRUPTION PHENOTYPE: Plants are arrested during endosperm development
CC and have altered root hair development and pollen tube elongation.
CC {ECO:0000269|PubMed:16731582}.
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DR EMBL; AC004667; AAC61816.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09080.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09081.1; -; Genomic_DNA.
DR EMBL; AY085599; AAM62820.1; -; mRNA.
DR EMBL; AK229368; BAF01231.1; -; mRNA.
DR PIR; H84765; H84765.
DR RefSeq; NP_565801.1; NM_129074.3. [O82171-1]
DR RefSeq; NP_973603.1; NM_201874.2. [O82171-2]
DR AlphaFoldDB; O82171; -.
DR SMR; O82171; -.
DR STRING; 3702.AT2G35210.1; -.
DR iPTMnet; O82171; -.
DR PaxDb; O82171; -.
DR PRIDE; O82171; -.
DR ProteomicsDB; 244741; -. [O82171-1]
DR EnsemblPlants; AT2G35210.1; AT2G35210.1; AT2G35210. [O82171-1]
DR EnsemblPlants; AT2G35210.2; AT2G35210.2; AT2G35210. [O82171-2]
DR GeneID; 818088; -.
DR Gramene; AT2G35210.1; AT2G35210.1; AT2G35210. [O82171-1]
DR Gramene; AT2G35210.2; AT2G35210.2; AT2G35210. [O82171-2]
DR KEGG; ath:AT2G35210; -.
DR Araport; AT2G35210; -.
DR TAIR; locus:2063429; AT2G35210.
DR eggNOG; KOG0706; Eukaryota.
DR HOGENOM; CLU_023062_0_0_1; -.
DR InParanoid; O82171; -.
DR OMA; ETLYDQK; -.
DR PhylomeDB; O82171; -.
DR PRO; PR:O82171; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82171; baseline and differential.
DR Genevisible; O82171; AT.
DR GO; GO:0000139; C:Golgi membrane; IEA:GOC.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; IBA:GO_Central.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR Gene3D; 1.10.220.150; -; 1.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR Pfam; PF01412; ArfGap; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Coiled coil; Golgi apparatus;
KW GTPase activation; Metal-binding; Phosphoprotein; Reference proteome; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9FIQ0"
FT CHAIN 2..395
FT /note="ADP-ribosylation factor GTPase-activating protein
FT AGD10"
FT /id="PRO_0000352501"
FT DOMAIN 10..128
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT ZN_FING 25..48
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 125..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 361..389
FT /evidence="ECO:0000255"
FT COMPBIAS 141..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9FIQ0"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FIQ0"
FT VAR_SEQ 334..371
FT /note="GSSAISSADLFGDGDGDFPLDLTAGDLLNRLSLQAQQD -> QSLVLICLET
FT VMEISLLISLRVIFSTAYLSRHNKTYHH (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_035551"
FT VAR_SEQ 372..395
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_035552"
SQ SEQUENCE 395 AA; 43097 MW; E387B8F8062D57B3 CRC64;
MASENLNDKI SVFKKLKAKS DNKICFDCNA KNPTWASVTY GIFLCIDCSA VHRSLGVHIS
FVRSTNLDSW SSEQLKMMIY GGNNRAQVFF KQYGWSDGGK TEAKYTSRAA DLYKQILAKE
VAKSKAEEEL DLPPSPPDST QVPNGLSSIK TSEALKESNT LKQQEKPDVV PVSPRISRSV
KKPLGAKKTG KTGGLGARKL TTKSSGTLYD QKPEESVIIQ ATSPVSAKSA RSSFSSRFDY
ADNVQNREDY MSPQVVSHVA PPKSSGFFEE ELEMNGGRFQ KKPITSSSKL QIQETDEARK
KFTNAKSISS AQYFGNDNNS ADLEAKSSLK KFSGSSAISS ADLFGDGDGD FPLDLTAGDL
LNRLSLQAQQ DISSLKNMAE ETKKKLGSVA SSLWV
