GCP2_ARATH
ID GCP2_ARATH Reviewed; 705 AA.
AC Q9M1S8; B5X581;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Probable glutamate carboxypeptidase AMP1 {ECO:0000305};
DE EC=3.4.17.21 {ECO:0000305};
DE AltName: Full=Probable glutamate carboxypeptidase 2 {ECO:0000305};
DE AltName: Full=Probable glutamate carboxypeptidase II {ECO:0000305};
DE AltName: Full=Protein ALTERED MERISTEM PROGRAM 1 {ECO:0000303|PubMed:17006669};
DE Short=AtAMP1 {ECO:0000303|PubMed:23603279};
DE AltName: Full=Protein CONSTITUTIVE MORPHOGENESIS 2;
DE AltName: Full=Protein HAUPTLING {ECO:0000305};
DE AltName: Full=Protein MULTIFOLIA {ECO:0000305};
DE AltName: Full=Protein PRIMORDIA TIMING;
GN Name=AMP1 {ECO:0000303|PubMed:11549767};
GN Synonyms=COP2 {ECO:0000305}, HPT {ECO:0000305}, MFO1 {ECO:0000305},
GN PT {ECO:0000303|PubMed:11549767};
GN OrderedLocusNames=At3g54720 {ECO:0000312|Araport:AT3G54720};
GN ORFNames=T5N23_80 {ECO:0000312|EMBL:CAB77592.1};
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], TISSUE SPECIFICITY, AND MUTAGENESIS OF GLU-404.
RC STRAIN=cv. Landsberg erecta; TISSUE=Silique;
RX PubMed=11549767; DOI=10.2307/3871431;
RA Helliwell C.A., Chin-Atkins A.N., Wilson I.W., Chapple R., Dennis E.S.,
RA Chaudhury A.;
RT "The Arabidopsis AMP1 gene encodes a putative glutamate carboxypeptidase.";
RL Plant Cell 13:2115-2125(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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;
RA De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=17553903; DOI=10.1242/dev.006759;
RA Vidaurre D.P., Ploense S., Krogan N.T., Berleth T.;
RT "AMP1 and MP antagonistically regulate embryo and meristem development in
RT Arabidopsis.";
RL Development 134:2561-2567(2007).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF GLY-545.
RX PubMed=17006669; DOI=10.1007/s00425-006-0395-9;
RA Saibo N.J., Vriezen W.H., De Grauwe L., Azmi A., Prinsen E.,
RA Van der Straeten D.;
RT "A comparative analysis of the Arabidopsis mutant amp1-1 and a novel weak
RT amp1 allele reveals new functions of the AMP1 protein.";
RL Planta 225:831-842(2007).
RN [7]
RP FUNCTION.
RX PubMed=21637772; DOI=10.1371/journal.pone.0020408;
RA Griffiths J., Barrero J.M., Taylor J., Helliwell C.A., Gubler F.;
RT "ALTERED MERISTEM PROGRAM 1 is involved in development of seed dormancy in
RT Arabidopsis.";
RL PLoS ONE 6:E20408-E20408(2011).
RN [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=23621575; DOI=10.1111/nph.12275;
RA Shi Y., Wang Z., Meng P., Tian S., Zhang X., Yang S.;
RT "The glutamate carboxypeptidase AMP1 mediates abscisic acid and abiotic
RT stress responses in Arabidopsis.";
RL New Phytol. 199:135-150(2013).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=23603279; DOI=10.1016/j.plaphy.2013.03.016;
RA Shi H., Ye T., Wang Y., Chan Z.;
RT "Arabidopsis ALTERED MERISTEM PROGRAM 1 negatively modulates plant
RT responses to abscisic acid and dehydration stress.";
RL Plant Physiol. Biochem. 67:209-216(2013).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25673776; DOI=10.1104/pp.114.254623;
RA Huang W., Pitorre D., Poretska O., Marizzi C., Winter N., Poppenberger B.,
RA Sieberer T.;
RT "ALTERED MERISTEM PROGRAM1 suppresses ectopic stem cell niche formation in
RT the shoot apical meristem in a largely cytokinin-independent manner.";
RL Plant Physiol. 167:1471-1486(2015).
RN [11]
RP FUNCTION.
RX PubMed=27743891; DOI=10.1016/j.bbrc.2016.10.025;
RA Lee M.W., Seo R., Lee Y.J., Bae J.H., Park J.K., Yoon J.H., Lee J.W.,
RA Jung H.W.;
RT "ALTERED MERISTEM PROGRAM1 has conflicting effects on the tolerance to heat
RT shock and symptom development after Pseudomonas syringae infection.";
RL Biochem. Biophys. Res. Commun. 480:296-301(2016).
CC -!- FUNCTION: May modulate the level of one or more small signaling
CC molecules that have a role in regulating meristem function. May play a
CC role in balancing and restricting the meristem-promoting activity of
CC auxin signaling (PubMed:17553903). Involved in ethylene and giberellin
CC (GA) signaling pathways or in a parallel pathway controlling cell and
CC hypocotyl elongation and cellular organization (PubMed:17006669).
CC Involved in abscisic acid (ABA) signaling pathway. Plays a negative
CC role in ABA-mediated seed germination and seedling development
CC (PubMed:23603279). Acts in association with LAMP1 to suppress ectopic
CC stem cell niche formation in the shoot apical meristem (SAM)
CC independently of cytokinin signaling pathway (PubMed:25673776).
CC Modulates responses to ABA, oxidative stress and abotic stress
CC (PubMed:23621575). Acts as negative regulator of the ABA signaling
CC pathway to modulate freezing and drought stress responses. Mediates
CC carbon and amino acid metabolism (PubMed:23621575, PubMed:23603279).
CC May be involved in the acquisition and/or maintenance of seed dormancy
CC (PubMed:21637772). Involved in the regulation of response to heat shock
CC and plant defense (PubMed:27743891). {ECO:0000269|PubMed:17006669,
CC ECO:0000269|PubMed:17553903, ECO:0000269|PubMed:21637772,
CC ECO:0000269|PubMed:23603279, ECO:0000269|PubMed:23621575,
CC ECO:0000269|PubMed:25673776, ECO:0000269|PubMed:27743891}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an unsubstituted, C-terminal glutamyl residue,
CC typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.;
CC EC=3.4.17.21; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q04609};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q04609};
CC -!- INTERACTION:
CC Q9M1S8; O04379: AGO1; NbExp=2; IntAct=EBI-6912802, EBI-6912745;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:25673776}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in all plant parts. Highest levels in the
CC bolt stem, inflorescence, root and silique. Low level in leaves.
CC {ECO:0000269|PubMed:11549767}.
CC -!- INDUCTION: Down-regulated by abscisic acid (ABA).
CC {ECO:0000269|PubMed:23603279, ECO:0000269|PubMed:23621575}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB77592.1; 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; AF357217; AAL03993.1; -; mRNA.
DR EMBL; AL138650; CAB77592.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79270.1; -; Genomic_DNA.
DR EMBL; BT046200; ACI49799.1; -; mRNA.
DR PIR; T47631; T47631.
DR RefSeq; NP_567007.1; NM_115329.3.
DR AlphaFoldDB; Q9M1S8; -.
DR SMR; Q9M1S8; -.
DR BioGRID; 9953; 1.
DR IntAct; Q9M1S8; 1.
DR STRING; 3702.AT3G54720.1; -.
DR MEROPS; M28.007; -.
DR PaxDb; Q9M1S8; -.
DR PRIDE; Q9M1S8; -.
DR ProteomicsDB; 222174; -.
DR EnsemblPlants; AT3G54720.1; AT3G54720.1; AT3G54720.
DR GeneID; 824637; -.
DR Gramene; AT3G54720.1; AT3G54720.1; AT3G54720.
DR KEGG; ath:AT3G54720; -.
DR Araport; AT3G54720; -.
DR TAIR; locus:2102470; AT3G54720.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_005688_2_1_1; -.
DR InParanoid; Q9M1S8; -.
DR OMA; IEFVSWD; -.
DR OrthoDB; 804230at2759; -.
DR BRENDA; 3.4.17.21; 399.
DR PRO; PR:Q9M1S8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1S8; baseline and differential.
DR Genevisible; Q9M1S8; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0004180; F:carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IMP:UniProtKB.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0009908; P:flower development; IGI:TAIR.
DR GO; GO:0010305; P:leaf vascular tissue pattern formation; IGI:TAIR.
DR GO; GO:0048507; P:meristem development; IMP:TAIR.
DR GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
DR GO; GO:0006508; P:proteolysis; IMP:UniProtKB.
DR GO; GO:0010080; P:regulation of floral meristem growth; IMP:UniProtKB.
DR GO; GO:0010081; P:regulation of inflorescence meristem growth; IMP:UniProtKB.
DR GO; GO:0010082; P:regulation of root meristem growth; IMP:UniProtKB.
DR GO; GO:0048364; P:root development; IGI:TAIR.
DR Gene3D; 1.20.930.40; -; 1.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR InterPro; IPR034308; VPS70.
DR PANTHER; PTHR10404; PTHR10404; 1.
DR PANTHER; PTHR10404:SF46; PTHR10404:SF46; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF47672; SSF47672; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..705
FT /note="Probable glutamate carboxypeptidase AMP1"
FT /id="PRO_0000174126"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 25..42
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..705
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 255..548
FT /note="Catalytic"
FT /evidence="ECO:0000305"
FT ACT_SITE 403
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 404
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 432
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 514
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 404
FT /note="E->K: In PT; shows pleiotropic phenotypes, including
FT altered shoot apical meristems, increased cell
FT proliferation, polycotyly, constitutive photomorphogenesis,
FT early flowering time, increased levels of endogenous
FT cytokinin, and increased cyclin cycD3 expression."
FT /evidence="ECO:0000269|PubMed:11549767"
FT MUTAGEN 545
FT /note="G->E: In amp1-7; weak allele showing some
FT pleiotropic phenotypes, including altered shoot apical
FT meristem, increased cell proliferation, serrated leaves
FT prior to full expansion, early flowering and increased
FT levels of endogenous cytokinin."
FT /evidence="ECO:0000269|PubMed:17006669"
FT CONFLICT 563
FT /note="D -> E (in Ref. 1; AAL03993)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 705 AA; 77153 MW; 8F4310FA19F5C22B CRC64;
MSQPLTTRPT VTGISIIPFR QPPPLCSFLF VIVLFVATFY TLHHPDAVTP PLLFSRNAYN
ALRLRRLFLS SASNATISSY LRELTRHPHL AGTKPSLDTL HYVFNHFQSL GLETHVAEYE
ALLSYPTHIS VTASFSNTTT LEFDLNDVPG DSPVVRPYHA YSPSGSAQGN VVFVNHGEER
DYHALESIGV SVKGCVVLAR KGENLGRGAI VKIAEAKGAL GVLIYAENDG GGFGGIERGT
VMRGIGDPVS PGWPGVVGGE KLSLDDELVT RRFPKIPSLP LSLRNAEIIL ASLGGARAPL
EWRNSGRVGP GQRVGPGRMV INMTFQGEMK MKKINNVVVT IRGSEEADRY VILGNHRDAW
TYGAVDPNSG TSALLDISRR FALLLKSGWR PRRTILLCSW DAEEFGMIGS TEWIEENVLN
LGASAVAYLN VDCAVQGSGF FAGATPQLDG LLVDVLKLVQ DPDAVGLTVE ETFKSQNNII
QRLSRVDSDF SGFLHHAGIP SIDMYYGADY PVYHTAFDSY DWMIHNADPL FHRHVAMAGI
WGLLGILLAD EPLIPFDYIS YADQLQAHRD KLSKLLEGKV SVNPLSMAIQ EFSLVAKEAA
DEAKKLKGKS YSKNDVAAAA KRRELNDRLM LVERGFLDAE GIKGKEWFKH LVYGPAAEPE
SKLGFFPGIA DAIAMNASEG IIEHEIWRVA RAIQRASKAL KGGFT
