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AGD9_ARATH
ID   AGD9_ARATH              Reviewed;         402 AA.
AC   Q9FIQ0;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Probable ADP-ribosylation factor GTPase-activating protein AGD9;
DE            Short=ARF GAP AGD9;
DE   AltName: Full=Protein ARF-GAP DOMAIN 9;
DE            Short=AtAGD9;
GN   Name=AGD9; OrderedLocusNames=At5g46750; ORFNames=MZA15.17;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA   Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT   features of the regions of 1,081,958 bp covered by seventeen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:379-391(1998).
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   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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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).
CC   -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor
CC       (ARF). {ECO:0000250}.
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DR   EMBL; AB016882; BAB08919.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95421.1; -; Genomic_DNA.
DR   EMBL; AY099693; AAM20544.1; -; mRNA.
DR   EMBL; AY128872; AAM91272.1; -; mRNA.
DR   RefSeq; NP_199487.1; NM_124045.5.
DR   AlphaFoldDB; Q9FIQ0; -.
DR   SMR; Q9FIQ0; -.
DR   BioGRID; 19966; 2.
DR   IntAct; Q9FIQ0; 1.
DR   STRING; 3702.AT5G46750.1; -.
DR   iPTMnet; Q9FIQ0; -.
DR   PaxDb; Q9FIQ0; -.
DR   PRIDE; Q9FIQ0; -.
DR   ProteomicsDB; 244743; -.
DR   EnsemblPlants; AT5G46750.1; AT5G46750.1; AT5G46750.
DR   GeneID; 834718; -.
DR   Gramene; AT5G46750.1; AT5G46750.1; AT5G46750.
DR   KEGG; ath:AT5G46750; -.
DR   Araport; AT5G46750; -.
DR   TAIR; locus:2178545; AT5G46750.
DR   eggNOG; KOG0706; Eukaryota.
DR   HOGENOM; CLU_023062_0_0_1; -.
DR   InParanoid; Q9FIQ0; -.
DR   OMA; QNVGESI; -.
DR   OrthoDB; 1155557at2759; -.
DR   PhylomeDB; Q9FIQ0; -.
DR   PRO; PR:Q9FIQ0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FIQ0; baseline and differential.
DR   Genevisible; Q9FIQ0; AT.
DR   GO; GO:0000139; C:Golgi membrane; IEA:GOC.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
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   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   1: Evidence at protein level;
KW   Acetylation; GTPase activation; Metal-binding; Phosphoprotein;
KW   Reference proteome; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..402
FT                   /note="Probable ADP-ribosylation factor GTPase-activating
FT                   protein AGD9"
FT                   /id="PRO_0000352500"
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          133..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          278..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   MOD_RES         307
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
SQ   SEQUENCE   402 AA;  43550 MW;  553B39E89E4BDB92 CRC64;
     MATENLTDKN VVFRKLKSKS ENKVCFDCSA KNPTWASVPY GIFLCIDCSA VHRSLGVHIS
     FVRSTNLDSW SPEQLRTMMF GGNNRAQVFF KQHGWNDGGK IEAKYTSRAA DMYRQTLAKE
     VAKAMAEETV LPSLSSVATS QPVESSENGF TSESPKESSL KQEAAVVSSP KASQKVVAST
     FKKPLVSRKS GKTGGLGARK LTTKSKDNLY EQKPEEPVPV IPAASPTNDT SAAGSSFASR
     FEYFDDEQSG GQSGTRVLSH VAPPKSSNFF NEFGMDSAFP KKSSSSSSKA QVEETDEARK
     KFSNAKSISS AQFFGNQNRD ADLDSKATLQ KFSGSAAISS SDLFGHGPDD SNIDITASDL
     INRISFQAQQ DMSSIANLAE ETKNKLGTFA SSIFSDLQDR ML
 
 
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