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AGD5_ARATH
ID   AGD5_ARATH              Reviewed;         483 AA.
AC   Q9FL69; C4NZX2; Q8L8M0; Q9FVH4;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=ADP-ribosylation factor GTPase-activating protein AGD5 {ECO:0000303|PubMed:12644670};
DE            Short=ARF GAP AGD5 {ECO:0000303|PubMed:12644670};
DE   AltName: Full=Protein ARF-GAP DOMAIN 5 {ECO:0000303|PubMed:12644670};
DE            Short=AtAGD5 {ECO:0000303|PubMed:12644670};
DE   AltName: Full=Protein MODIFIED TRANSPORT TO THE VACUOLE 4 {ECO:0000303|PubMed:23771894};
DE   AltName: Full=Protein NEVERSHED {ECO:0000303|PubMed:19429787};
DE   AltName: Full=Protein ZIGA3 {ECO:0000303|PubMed:11202441};
GN   Name=AGD5 {ECO:0000303|PubMed:12644670};
GN   Synonyms=MTV4 {ECO:0000303|PubMed:23771894},
GN   NEV {ECO:0000303|PubMed:19429787}, ZIG3 {ECO:0000303|PubMed:11202441},
GN   ZIGA3 {ECO:0000303|PubMed:11202441};
GN   OrderedLocusNames=At5g54310 {ECO:0000312|Araport:AT5G54310};
GN   ORFNames=MDK4.13 {ECO:0000312|EMBL:BAB10754.1};
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 [MRNA], FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF
RP   CYS-34; CYS-51 AND ARG-59, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=19429787; DOI=10.1242/dev.033605;
RA   Liljegren S.J., Leslie M.E., Darnielle L., Lewis M.W., Taylor S.M., Luo R.,
RA   Geldner N., Chory J., Randazzo P.A., Yanofsky M.F., Ecker J.R.;
RT   "Regulation of membrane trafficking and organ separation by the NEVERSHED
RT   ARF-GAP protein.";
RL   Development 136:1909-1918(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA   Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT   features of the regions of 1,381,565 bp covered by twenty one physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:131-145(1998).
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].
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].
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   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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 7-483.
RC   STRAIN=cv. Columbia;
RX   PubMed=11202441; DOI=10.1023/a:1026509002161;
RA   Jensen R.B., Lykke-Andersen K., Frandsen G.I., Nielsen H.B., Haseloff J.,
RA   Jespersen H.M., Mundy J., Skriver K.;
RT   "Promiscuous and specific phospholipid binding by domains in ZAC, a
RT   membrane-associated Arabidopsis protein with an ARF GAP zinc finger and a
RT   C2 domain.";
RL   Plant Mol. Biol. 44:799-814(2000).
RN   [8]
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   [9]
RP   NOT SURE.
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).
RN   [10]
RP   IDENTIFICATION BY 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   [11]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX   PubMed=20081191; DOI=10.1242/dev.041335;
RA   Leslie M.E., Lewis M.W., Youn J.-Y., Daniels M.J., Liljegren S.J.;
RT   "The EVERSHED receptor-like kinase modulates floral organ shedding in
RT   Arabidopsis.";
RL   Development 137:467-476(2010).
RN   [12]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20230490; DOI=10.1111/j.1365-313x.2010.04194.x;
RA   Lewis M.W., Leslie M.E., Fulcher E.H., Darnielle L., Healy P.N.,
RA   Youn J.-Y., Liljegren S.J.;
RT   "The SERK1 receptor-like kinase regulates organ separation in Arabidopsis
RT   flowers.";
RL   Plant J. 62:817-828(2010).
RN   [13]
RP   FUNCTION, MUTAGENESIS OF ARG-59, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP   ARF1.
RC   STRAIN=cv. Columbia;
RX   PubMed=21105926; DOI=10.1111/j.1365-313x.2010.04369.x;
RA   Stefano G., Renna L., Rossi M., Azzarello E., Pollastri S., Brandizzi F.,
RA   Baluska F., Mancuso S.;
RT   "AGD5 is a GTPase-activating protein at the trans-Golgi network.";
RL   Plant J. 64:790-799(2010).
RN   [14]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. C24, cv. Columbia, and cv. Landsberg erecta;
RX   PubMed=23963677; DOI=10.1093/jxb/ert232;
RA   Liu B., Butenko M.A., Shi C.-L., Bolivar J.L., Winge P., Stenvik G.-E.,
RA   Vie A.K., Leslie M.E., Brembu T., Kristiansen W., Bones A.M.,
RA   Patterson S.E., Liljegren S.J., Aalen R.B.;
RT   "NEVERSHED and INFLORESCENCE DEFICIENT IN ABSCISSION are differentially
RT   required for cell expansion and cell separation during floral organ
RT   abscission in Arabidopsis thaliana.";
RL   J. Exp. Bot. 64:5345-5357(2013).
RN   [15]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH
RP   CLATHRIN, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Columbia;
RX   PubMed=23771894; DOI=10.1105/tpc.113.111724;
RA   Sauer M., Delgadillo M.O., Zouhar J., Reynolds G.D., Pennington J.G.,
RA   Jiang L., Liljegren S.J., Stierhof Y.-D., De Jaeger G., Otegui M.S.,
RA   Bednarek S.Y., Rojo E.;
RT   "MTV1 and MTV4 encode plant-specific ENTH and ARF GAP proteins that mediate
RT   clathrin-dependent trafficking of vacuolar cargo from the trans-Golgi
RT   network.";
RL   Plant Cell 25:2217-2235(2013).
RN   [16]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND REVIEW.
RX   PubMed=25763490; DOI=10.4161/psb.29115;
RA   Gubert C.M., Liljegren S.J.;
RT   "HAESA and HAESA-LIKE2 activate organ abscission downstream of NEVERSHED
RT   and EVERSHED in Arabidopsis flowers.";
RL   Plant Signal. Behav. 9:E29115-E29115(2014).
CC   -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor
CC       (ARF) (PubMed:19429787). Mediates clathrin-dependent trafficking of
CC       vacuolar cargo from the trans-Golgi network (TGN) (PubMed:23771894).
CC       Promotes plant growth (PubMed:23771894, PubMed:25763490). Involved in
CC       the regulation of membrane trafficking and cell separation during
CC       floral organ shedding and abscission (PubMed:19429787, PubMed:20081191,
CC       PubMed:20230490, PubMed:23963677). Prevents abscission zone (AZ) cells
CC       enlargement (PubMed:23963677, PubMed:25763490). Exhibits ARF-GTPase
CC       activity toward ARF1 at TGN (PubMed:21105926).
CC       {ECO:0000269|PubMed:19429787, ECO:0000269|PubMed:20081191,
CC       ECO:0000269|PubMed:20230490, ECO:0000269|PubMed:21105926,
CC       ECO:0000269|PubMed:23771894, ECO:0000269|PubMed:23963677,
CC       ECO:0000269|PubMed:25763490}.
CC   -!- SUBUNIT: Interacts with ARF1 at trans-Golgi network (TGN)
CC       (PubMed:21105926). Binds to clathrin heavy chain (PubMed:23771894).
CC       {ECO:0000269|PubMed:21105926, ECO:0000269|PubMed:23771894}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC       {ECO:0000269|PubMed:19429787, ECO:0000269|PubMed:21105926,
CC       ECO:0000269|PubMed:23771894}. Endosome {ECO:0000269|PubMed:19429787}.
CC       Cytoplasmic vesicle, clathrin-coated vesicle
CC       {ECO:0000269|PubMed:23771894}. Note=Colocalizes with AGD5 at the trans-
CC       Golgi network (TGN) (PubMed:21105926). Colocalizes with clathrin at the
CC       TGN (PubMed:23771894). {ECO:0000269|PubMed:21105926,
CC       ECO:0000269|PubMed:23771894}.
CC   -!- TISSUE SPECIFICITY: Expressed in inflorescence stems, abscission zones,
CC       stigmas, roots, roots meristems, embryos, and floral and leaf
CC       vasculatures. {ECO:0000269|PubMed:19429787,
CC       ECO:0000269|PubMed:23771894}.
CC   -!- DEVELOPMENTAL STAGE: Strongly expressed in developing and mature
CC       embryos. {ECO:0000269|PubMed:23771894}.
CC   -!- DISRUPTION PHENOTYPE: Abnormal vacuolar trafficking of soluble cargo
CC       proteins, and premature termination of the shoot apical meristem and of
CC       floral meristems leading to short siliques and abscission defect
CC       (PubMed:23771894, PubMed:25763490). Plant missing both AGD5 and MTV1
CC       are severely dwarfed and have altered subcellular distribution of
CC       clathrin-coated vesicle (CCV) cargo exported from the trans-Golgi
CC       network (TGN) (PubMed:23771894). Floral organs remain attached to the
CC       plant body after the shedding of mature seeds, including abnormal petal
CC       breakstrength (pBS) (PubMed:23963677, PubMed:19429787, PubMed:20081191,
CC       PubMed:20230490). Ectopic enlargement of abscission zone (AZ) cells
CC       during shedding (PubMed:23963677). Impaired floral organ shedding
CC       associated with defects in the structure of the Golgi apparatus and
CC       extensive accumulation of vesicles adjacent to the cell walls in
CC       abscission zone regions (PubMed:19429787, PubMed:20081191,
CC       PubMed:20230490). Rescued by SOBIR1/EVR disruption, leading to
CC       premature shedding of floral organs and enlarge abscission zones
CC       (PubMed:20081191). Rescued by SERK1 disruption, leading to normal Golgi
CC       apparatus and endosome, as well as correct floral organ shedding
CC       (PubMed:20230490). {ECO:0000269|PubMed:19429787,
CC       ECO:0000269|PubMed:20081191, ECO:0000269|PubMed:20230490,
CC       ECO:0000269|PubMed:23771894, ECO:0000269|PubMed:23963677,
CC       ECO:0000269|PubMed:25763490}.
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DR   EMBL; FJ794601; ACQ91177.1; -; mRNA.
DR   EMBL; AB010695; BAB10754.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96483.1; -; Genomic_DNA.
DR   EMBL; AY099716; AAM20567.1; -; mRNA.
DR   EMBL; BT000287; AAN15606.1; -; mRNA.
DR   EMBL; AY088913; AAM67219.1; -; mRNA.
DR   EMBL; AK226402; BAE98548.1; -; mRNA.
DR   EMBL; AF184144; AAG17004.1; -; mRNA.
DR   RefSeq; NP_568807.1; NM_124811.5.
DR   AlphaFoldDB; Q9FL69; -.
DR   SMR; Q9FL69; -.
DR   BioGRID; 20763; 3.
DR   STRING; 3702.AT5G54310.1; -.
DR   iPTMnet; Q9FL69; -.
DR   MetOSite; Q9FL69; -.
DR   PaxDb; Q9FL69; -.
DR   PRIDE; Q9FL69; -.
DR   ProteomicsDB; 244742; -.
DR   EnsemblPlants; AT5G54310.1; AT5G54310.1; AT5G54310.
DR   GeneID; 835519; -.
DR   Gramene; AT5G54310.1; AT5G54310.1; AT5G54310.
DR   KEGG; ath:AT5G54310; -.
DR   Araport; AT5G54310; -.
DR   TAIR; locus:2162580; AT5G54310.
DR   eggNOG; KOG0703; Eukaryota.
DR   HOGENOM; CLU_030143_0_0_1; -.
DR   InParanoid; Q9FL69; -.
DR   OMA; RSSFEQH; -.
DR   OrthoDB; 1097163at2759; -.
DR   PhylomeDB; Q9FL69; -.
DR   PRO; PR:Q9FL69; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FL69; baseline and differential.
DR   Genevisible; Q9FL69; AT.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
DR   GO; GO:0005768; C:endosome; IDA:TAIR.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR   GO; GO:0030276; F:clathrin binding; IDA:UniProtKB.
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:0090630; P:activation of GTPase activity; IDA:TAIR.
DR   GO; GO:0035652; P:clathrin-coated vesicle cargo loading; IMP:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:TAIR.
DR   GO; GO:0010227; P:floral organ abscission; IMP:UniProtKB.
DR   GO; GO:0060866; P:leaf abscission; IMP:TAIR.
DR   GO; GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
DR   GO; GO:0060858; P:vesicle-mediated transport involved in floral organ abscission; IMP:UniProtKB.
DR   Gene3D; 1.10.220.150; -; 1.
DR   InterPro; IPR044520; ARF_GAP_AGD5/15.
DR   InterPro; IPR037278; ARFGAP/RecO.
DR   InterPro; IPR001164; ArfGAP_dom.
DR   InterPro; IPR038508; ArfGAP_dom_sf.
DR   PANTHER; PTHR46419; PTHR46419; 1.
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   Cytoplasmic vesicle; Endosome; Golgi apparatus; GTPase activation;
KW   Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..483
FT                   /note="ADP-ribosylation factor GTPase-activating protein
FT                   AGD5"
FT                   /id="PRO_0000352497"
FT   DOMAIN          16..130
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   ZN_FING         31..54
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   REGION          123..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          238..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          434..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..310
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..471
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         34
FT                   /note="C->Y: In nev-9; impaired floral organ shedding."
FT                   /evidence="ECO:0000269|PubMed:19429787"
FT   MUTAGEN         51
FT                   /note="C->Y: In nev-1; impaired floral organ shedding."
FT                   /evidence="ECO:0000269|PubMed:19429787"
FT   MUTAGEN         59
FT                   /note="R->K: In nev-3; impaired floral organ shedding."
FT                   /evidence="ECO:0000269|PubMed:19429787"
FT   MUTAGEN         59
FT                   /note="R->Q: Impaired ARF-GTPase activity toward ARF1 at
FT                   trans-Golgi network."
FT                   /evidence="ECO:0000269|PubMed:21105926"
FT   CONFLICT        145
FT                   /note="R -> T (in Ref. 5; AAM67219)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   483 AA;  52593 MW;  7698FA235CCB50B4 CRC64;
     MNEKANVSKE LNARHRKILE GLLKHPENRE CADCKTKGPR WASVNLGIFI CMQCSGIHRS
     LGVHISKVRS ATLDTWLPEQ VAFIQSMGND KANSYWEAEL PPNYDRVGIE NFIRAKYEEK
     RWVSRGEKAR SPPRVEQERR KSVERSGPGY EHGHSSSPVN LFEERKTIPA SRTRNNVAAT
     RINLPVPPQG PSQVIKPQQK MESAATPVER EKQAVNVAPA SDPPKVDFAT DLFNMLSMDD
     STTNTSEATP GDTPADDNSW AGFQSAGSGQ TAEKIVTAKP AESSSPPASS SDFEDLFKDT
     PNLTTQQAPK DVKGDIMSLF EKTNIVSPFA MHQQQVAMLA QQQALYMAAA KAAGGTPNGV
     NQQAIANALN VASANWSNPG GYQIPGMTNP VGGQADLQKL MQNMNMNANM NTRPAQPQEN
     TLQYPSSSFY TMGQANQVNG MTPNSTGKPQ SSSATQPTST TPSSQSGKDF DFSSLMDGMF
     TKH
 
 
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