DELA2_MEDTR
ID DELA2_MEDTR Reviewed; 533 AA.
AC A0A396GMX6; B7FFF7; I3TAC6;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=DELLA protein 2 {ECO:0000303|PubMed:24297892};
DE Short=MtDELLA2 {ECO:0000303|PubMed:24297892};
GN Name=DELLA2 {ECO:0000303|PubMed:24297892};
GN ORFNames=MtrunA17_Chr8g0376381 {ECO:0000312|EMBL:RHN42390.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B.,
RA Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H.,
RA Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F.,
RA De Mita S., Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K.,
RA Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A.T., Tang H.,
RA Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M.,
RA Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N.,
RA Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.-M.,
RA Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S.,
RA Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J.,
RA Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H.,
RA Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J.,
RA Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C.,
RA O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F.,
RA Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O.,
RA Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R.,
RA Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B.,
RA Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D.,
RA White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F.,
RA Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D.,
RA Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17;
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=30397259; DOI=10.1038/s41477-018-0286-7;
RA Pecrix Y., Staton S.E., Sallet E., Lelandais-Briere C., Moreau S.,
RA Carrere S., Blein T., Jardinaud M.F., Latrasse D., Zouine M., Zahm M.,
RA Kreplak J., Mayjonade B., Satge C., Perez M., Cauet S., Marande W.,
RA Chantry-Darmon C., Lopez-Roques C., Bouchez O., Berard A., Debelle F.,
RA Munos S., Bendahmane A., Berges H., Niebel A., Buitink J., Frugier F.,
RA Benhamed M., Crespi M., Gouzy J., Gamas P.;
RT "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL Nat. Plants 4:1017-1025(2018).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-232.
RA Moskal W., Chan A., Cheung F., Xiao Y., Town C.D.;
RT "Medicago truncatula full length cdna cloning project.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 227-453.
RA Krishnakumar V., Cheung F., Xiao Y., Chan A., Moskal W.A., Town C.D.;
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY PHOSPHATE DEPRIVATION AND
RP GLOMUS VERSIFORME.
RX PubMed=24297892; DOI=10.1073/pnas.1308973110;
RA Floss D.S., Levy J.G., Levesque-Tremblay V., Pumplin N., Harrison M.J.;
RT "DELLA proteins regulate arbuscule formation in arbuscular mycorrhizal
RT symbiosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E5025-E5034(2013).
CC -!- FUNCTION: Probable transcriptional regulator that acts as a repressor
CC of the gibberellin (GA) signaling pathway (By similarity). Probably
CC acts by participating in large multiprotein complexes that repress
CC transcription of GA-inducible genes (By similarity). Upon GA
CC application, it is degraded by the proteasome, allowing the GA
CC signaling pathway (By similarity). Together with DELLA1, required to
CC enable arbuscule development during arbuscular mycorrhizal (AM)
CC symbiosis with AM fungi (e.g. Glomus versiforme) via the regulation of
CC RAM1 which, in turn, regulates various AM genes (e.g. NSP1, NSP2, PT4,
CC LEC5, RAM2, EXO70I, STR and RAD1) (PubMed:24297892).
CC {ECO:0000250|UniProtKB:Q7G7J6, ECO:0000269|PubMed:24297892}.
CC -!- SUBUNIT: May be a homodimer. {ECO:0000250|UniProtKB:Q7G7J6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A0A396IUP1}.
CC -!- INDUCTION: Accumulates upon phosphate (Pi) deprivation
CC (PubMed:24297892). Expressed during arbuscular mycorrhizal (AM)
CC symbiosis with AM fungi (e.g. Glomus versiforme) (PubMed:24297892).
CC {ECO:0000269|PubMed:24297892}.
CC -!- DOMAIN: The DELLA motif is required for its GA-induced degradation.
CC {ECO:0000250|UniProtKB:Q7G7J6}.
CC -!- PTM: Ubiquitinated. Upon GA application it is ubiquitinated, leading to
CC its subsequent degradation. {ECO:0000250|UniProtKB:Q7G7J6}.
CC -!- DISRUPTION PHENOTYPE: The double mutant della1/della2 exhibit slender
CC shoots, early flowering and reduced root fresh weight
CC (PubMed:24297892). Impaired arbuscule formation during arbuscular
CC mycorrhizal (AM) symbiosis with AM fungi (e.g. Glomus versiforme) in
CC plant missing both DELLA1 and DELLA2 associated with a reduced
CC expression of AM genes (e.g. NSP1, NSP2, PT4 and LEC5); these
CC phenotypes are phenocopied by treatment with gibberellic acid (GA)
CC (PubMed:24297892). {ECO:0000269|PubMed:24297892}.
CC -!- SIMILARITY: Belongs to the GRAS family. DELLA subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFK49468.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CM001224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; PSQE01000008; RHN42390.1; -; Genomic_DNA.
DR EMBL; BT050678; ACJ83347.1; -; mRNA.
DR EMBL; BT149674; AFK49468.1; ALT_INIT; mRNA.
DR AlphaFoldDB; A0A396GMX6; -.
DR SMR; A0A396GMX6; -.
DR Proteomes; UP000002051; Chromosome 8.
DR Proteomes; UP000265566; Chromosome 8.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0036377; P:arbuscular mycorrhizal association; IMP:UniProtKB.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:UniProtKB.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:1903506; P:regulation of nucleic acid-templated transcription; IMP:UniProtKB.
DR GO; GO:0009610; P:response to symbiotic fungus; IEP:UniProtKB.
DR Gene3D; 1.10.10.1290; -; 1.
DR InterPro; IPR038088; DELLA_N_sf.
DR InterPro; IPR030006; TF_DELLA.
DR InterPro; IPR021914; TF_DELLA_N.
DR InterPro; IPR005202; TF_GRAS.
DR PANTHER; PTHR31636; PTHR31636; 2.
DR PANTHER; PTHR31636:SF247; PTHR31636:SF247; 2.
DR Pfam; PF12041; DELLA; 1.
DR Pfam; PF03514; GRAS; 1.
DR PROSITE; PS50985; GRAS; 1.
PE 2: Evidence at transcript level;
KW Gibberellin signaling pathway; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..533
FT /note="DELLA protein 2"
FT /id="PRO_0000450053"
FT DOMAIN 157..522
FT /note="GRAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..218
FT /note="Leucine repeat I (LRI)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 166..203
FT /note="Required for possible homodimerization"
FT /evidence="ECO:0000250|UniProtKB:Q7G7J6"
FT REGION 232..297
FT /note="VHIID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 311..343
FT /note="Leucine repeat II (LRII)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 355..443
FT /note="PFYRE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 446..522
FT /note="SAW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MOTIF 31..35
FT /note="DELLA motif"
FT /evidence="ECO:0000250|UniProtKB:A0A396IUP1"
FT MOTIF 171..175
FT /note="LxCxE motif; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MOTIF 263..267
FT /note="VHIID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MOTIF 363..367
FT /note="LXXLL motif; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT CONFLICT 159
FT /note="T -> A (in Ref. 4; ACJ83347)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="R -> G (in Ref. 4; ACJ83347)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="V -> G (in Ref. 5; AFK49468)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 533 AA; 58991 MW; 32E66922F8C59E39 CRC64;
MKREHKLEHE DMSSGSGKSG VCWEDDGGGM DELLAVVGYK VKSSDMAEVA QKLEQLEQAM
MGNNFHDHDE STIAQHLSND TVHYNPSDIS NWLQTMLSNF DPQPNNPSVN SDDNDLNAIP
GKAIYAADEF TSRKRVKRNE SVTVTTESTT TRPIMVVETQ EKGIRLVHSL MACAEAVEQN
NLKMAEALVK QIGYLAVSQE GAMRKVATYF AEGLARRIYG VFPQHSVSDS LQIHFYETCP
NLKFAHFTAN QAILEAFQGK SSVHVIDFSI NQGMQWPALM QALALRPGGP PAFRLTGIGP
PASDNSDHLQ QVGWRLAQFA QTIHVQFEYR GFVANSLADL DASMLELRSP ETESVAVNSV
FELHKLNARP GALEKVFSVI RQIRPEIVTV VEQEANHNGP AFLDRFTESL HYYSTLFDSL
EGSSVEPQDK AMSEVYLGKQ ICNVVACEGT DRVERHETLN QWRNRFNSAG FSPVHLGSNA
FKQASMLLAL FAGGDGYKVE ENDGCLMLGW HTRPLIATSA WKLAAANSVV VSH
