RAM1_PETHY
ID RAM1_PETHY Reviewed; 695 AA.
AC A0A0M4FMK2;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 1.
DT 25-MAY-2022, entry version 20.
DE RecName: Full=GRAS family protein RAM1 {ECO:0000305};
DE AltName: Full=Protein ATYPICAL ARBUSCULE {ECO:0000303|PubMed:25971550};
DE AltName: Full=Protein REQUIRED FOR ARBUSCULAR MYCORRHIZATION 1 {ECO:0000303|PubMed:25971550};
DE Short=PhRAM1 {ECO:0000303|PubMed:25971550};
GN Name=RAM1 {ECO:0000303|PubMed:25971550};
GN Synonyms=ATA {ECO:0000303|PubMed:25971550};
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION
RP BY RHIZOPHAGUS IRREGULARIS.
RC STRAIN=cv. W138;
RX PubMed=25971550; DOI=10.1104/pp.15.00310;
RA Rich M.K., Schorderet M., Bapaume L., Falquet L., Morel P.,
RA Vandenbussche M., Reinhardt D.;
RT "The Petunia GRAS transcription factor ATA/RAM1 regulates symbiotic gene
RT expression and fungal morphogenesis in arbuscular mycorrhiza.";
RL Plant Physiol. 168:788-797(2015).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY RHIZOPHAGUS IRREGULARIS.
RC STRAIN=cv. W115;
RX PubMed=28789611; DOI=10.1186/s12864-017-3988-8;
RA Rich M.K., Courty P.-E., Roux C., Reinhardt D.;
RT "Role of the GRAS transcription factor ATA/RAM1 in the transcriptional
RT reprogramming of arbuscular mycorrhiza in Petunia hybrida.";
RL BMC Genomics 18:589-589(2017).
CC -!- FUNCTION: Transcription factor acting as a central regulator of
CC arbuscular mycorrhiza (AM)-related genes involved at later stages of
CC symbiosis (e.g. VAPYRIN, PT4, PT5, STR, STR2, RAM2, SBT and BCP) but
CC not required for early genes of AM (e.g. common symbiosis signaling
CC genes) (PubMed:25971550, PubMed:28789611). Required for the
CC morphogenesis of arbuscules upon symbiosis with AM fungi (e.g.
CC Rhizophagus irregularis, Simiglomus hoi and Acaulospora scrobiculata)
CC (PubMed:25971550, PubMed:28789611). Also involved in restricting
CC mycorrhizal colonization of the root meristem (PubMed:25971550).
CC {ECO:0000269|PubMed:25971550, ECO:0000269|PubMed:28789611}.
CC -!- SUBUNIT: Forms homodimer in nucleus and cytoplasm (By similarity).
CC Interacts with NSP2, RAD1 and TF80 (By similarity).
CC {ECO:0000250|UniProtKB:A0A145P7T2, ECO:0000250|UniProtKB:G7L166}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:G7L166}. Cytoplasm
CC {ECO:0000250|UniProtKB:A0A145P7T2}.
CC -!- INDUCTION: Accumulates after inoculation with Rhizophagus irregularis.
CC {ECO:0000269|PubMed:25971550, ECO:0000269|PubMed:28789611}.
CC -!- DISRUPTION PHENOTYPE: Ineffective symbiosis with arbuscular mycorrhiza
CC (AM) fungi (e.g. Rhizophagus irregularis, Simiglomus hoi and
CC Acaulospora scrobiculata), with rare colonizations characterized by
CC malformed arbuscules (PubMed:25971550, PubMed:28789611). Reduced AM
CC fungi-mediated induction of AM-related genes involved at later stages
CC of symbiosis (e.g. VAPYRIN, PT4, PT5, STR, STR2, RAM2, SBT and BCP)
CC (PubMed:25971550, PubMed:28789611). {ECO:0000269|PubMed:25971550,
CC ECO:0000269|PubMed:28789611}.
CC -!- SIMILARITY: Belongs to the GRAS family. {ECO:0000255|PROSITE-
CC ProRule:PRU01191}.
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DR EMBL; KR612264; ALC79554.1; -; mRNA.
DR AlphaFoldDB; A0A0M4FMK2; -.
DR SMR; A0A0M4FMK2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0036377; P:arbuscular mycorrhizal association; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0009610; P:response to symbiotic fungus; IMP:UniProtKB.
DR InterPro; IPR005202; TF_GRAS.
DR PANTHER; PTHR31636; PTHR31636; 1.
DR Pfam; PF03514; GRAS; 1.
DR PROSITE; PS50985; GRAS; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Transcription; Transcription regulation.
FT CHAIN 1..695
FT /note="GRAS family protein RAM1"
FT /id="PRO_0000450022"
FT REPEAT 105..139
FT /note="PFTA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00488"
FT DOMAIN 321..694
FT /note="GRAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 281..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..393
FT /note="Leucine repeat I (LRI)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 412..477
FT /note="VHIID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 487..518
FT /note="Leucine repeat II (LRII)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 528..616
FT /note="PFYRE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 619..694
FT /note="SAW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MOTIF 335..339
FT /note="LxCxE motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MOTIF 443..447
FT /note="VHIID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
SQ SEQUENCE 695 AA; 76811 MW; 1E41C251F2017FBE CRC64;
MGSLNNEVGS IKCEVGSLKS ENSFTKLPSE ESLASESKKV TPVSSDFELN CGSLAPTSLS
FPAMKFEDDI EIQSPDNSIW ESFFADHLEG DFMISSPVRN LPSPQPASSF SSSHNNGNNN
NNNYNIYAHR QGIHGQDMMM CSPPRSPLGL YNHPSHKGKG LSPLQKVFNS PNNQFMQIES
FNLPALESFL DDDYDKEEDL ASSYSTLKVS GTGVAGSSSE SFDALSVVPD DLLECLALPS
SLSNTSGGFM ESLLSDTSAV QVINPDDEIF RTGSIAPLSQ QLHQERQQEK QQKQRPVTHA
RPQQQQIINH NVLVPLAAAP DQEQDSGLQL VHLLLACAEA VSKEDYMLAR RYLHHLNRVV
TPLGDSMQRV ASCFTEALSA RLAATLATKP STSALKPFNP FPPNSLEILK IYQILYQACP
YVKFAHFTAN QAIFEAFEAE ERVHIIDLDI LQGYQWPAFM QALAARPGGA PFLRITGVGP
SPEAVRETGR CLTELAHSLH VPFEFHPVGE QLEDLKPHMF NRRVGEALAV NSVNRLHRVP
VNCIGNLLAM IRDQAPNIVT IVEQEASHNG PYFLGRFLEA LHYYSAIFDS LDATFPADSS
QRAKLEQYIF APEIMNIVSC EGPERVVRHE RLEKWRRLME GKGFKGVALS ANAVTQSKIL
LGLYSCDGYK LTEDDGCLLL GWQDRAILAA SAWRC