RAM2_MEDTR
ID RAM2_MEDTR Reviewed; 526 AA.
AC K7PEY4; A0A067XGS7; G7IDH7;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Glycerol-3-phosphate acyltransferase RAM2 {ECO:0000305};
DE EC=2.3.1.15 {ECO:0000305};
DE AltName: Full=Protein REQUIRED FOR ARBUSCULAR MYCORRHIZATION 2 {ECO:0000303|PubMed:23122843};
GN Name=RAM2 {ECO:0000303|PubMed:23122843};
GN Synonyms=AMBAE {ECO:0000312|EMBL:AKN52402.1};
GN OrderedLocusNames=MTR_1g040500 {ECO:0000312|EMBL:AES60108.1};
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 [GENOMIC DNA / MRNA], FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23122843; DOI=10.1016/j.cub.2012.09.043;
RA Wang E., Schornack S., Marsh J.F., Gobbato E., Schwessinger B.,
RA Eastmond P., Schultze M., Kamoun S., Oldroyd G.E.;
RT "A common signaling process that promotes mycorrhizal and oomycete
RT colonization of plants.";
RL Curr. Biol. 23:2242-2246(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Duvvuru Muni R.R., Chen Y., Li G., Chen R.;
RT "Medicago truncatula AMBAE1 is required for appressorium development of
RT arbuscular mycorrhizal (AM) Fungi.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP INDUCTION.
RX PubMed=23122845; DOI=10.1016/j.cub.2012.09.044;
RA Gobbato E., Marsh J.F., Vernie T., Wang E., Maillet F., Kim J.,
RA Miller J.B., Sun J., Bano S.A., Ratet P., Mysore K.S., Denarie J.,
RA Schultze M., Oldroyd G.E.;
RT "A GRAS-type transcription factor with a specific function in mycorrhizal
RT signaling.";
RL Curr. Biol. 22:2236-2241(2012).
RN [6]
RP INDUCTION BY RAM1 AND GLOMUS VERSIFORME.
RX PubMed=26511916; DOI=10.1104/pp.15.01155;
RA Park H.-J., Floss D.S., Levesque-Tremblay V., Bravo A., Harrison M.J.;
RT "Hyphal branching during arbuscule development requires reduced arbuscular
RT mycorrhiza1.";
RL Plant Physiol. 169:2774-2788(2015).
CC -!- FUNCTION: Involved in the production of cutin monomers
CC (PubMed:23122843). Esterifies acyl-group from acyl-ACP to the sn-2
CC position of glycerol-3-phosphate, a step in cutin biosynthesis
CC (Probable). Required for colonization of the root by mycorrhizal fungi,
CC and appropriate hyphopodia and arbuscule formation (PubMed:23122843).
CC Cutin monomers act as plant signals that promote colonization by
CC arbuscular mycorrhizal fungi (PubMed:23122843). This signaling function
CC has been recruited by pathogenic oomycetes to facilitate appressoria
CC formation and their own invasion (PubMed:23122843).
CC {ECO:0000269|PubMed:23122843, ECO:0000305|PubMed:23122843}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC Evidence={ECO:0000305};
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Accumulates in roots, in a RAM1-dependent manner, during
CC colonization by arbuscular mycorrhizal fungi (e.g. Glomus versiforme)
CC (PubMed:23122845, PubMed:26511916). Triggered by RAM1
CC (PubMed:26511916). {ECO:0000269|PubMed:23122845,
CC ECO:0000269|PubMed:26511916}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:23122843). Unable to be colonized by arbuscular
CC mycorrhizal fungi, with a defect in hyphopodia formation on the surface
CC of the root (PubMed:23122843). Defects in colonization by an oomycete
CC pathogen, with the absence of appressoria formation (PubMed:23122843).
CC {ECO:0000269|PubMed:23122843}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AES60108.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AET87503.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; JN254632; AET87503.1; ALT_INIT; Genomic_DNA.
DR EMBL; JN572682; AFK81970.1; -; Genomic_DNA.
DR EMBL; JN572684; AFK81972.1; -; mRNA.
DR EMBL; KM656467; AKN52402.1; -; Genomic_DNA.
DR EMBL; KX774513; APF29092.1; -; mRNA.
DR EMBL; CM001217; AES60108.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_003589857.1; XM_003589809.1.
DR AlphaFoldDB; K7PEY4; -.
DR SMR; K7PEY4; -.
DR STRING; 3880.AES60108; -.
DR EnsemblPlants; AES60108; AES60108; MTR_1g040500.
DR Gramene; AES60108; AES60108; MTR_1g040500.
DR KEGG; mtr:MTR_1g040500; -.
DR eggNOG; ENOG502QQTS; Eukaryota.
DR HOGENOM; CLU_028504_1_0_1; -.
DR OrthoDB; 500365at2759; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000002051; Chromosome 1.
DR ExpressionAtlas; K7PEY4; differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0090447; F:glycerol-3-phosphate 2-O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0036377; P:arbuscular mycorrhizal association; IMP:UniProtKB.
DR GO; GO:0010143; P:cutin biosynthetic process; IBA:GO_Central.
DR GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009610; P:response to symbiotic fungus; IEP:UniProtKB.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..526
FT /note="Glycerol-3-phosphate acyltransferase RAM2"
FT /id="PRO_0000447241"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 332..337
FT /note="HXXXXD motif"
FT /evidence="ECO:0000305"
SQ SEQUENCE 526 AA; 57604 MW; 64ACBA6B7251A43B CRC64;
MHPCLVETES VSLLQEEITI ITMASSTFPT VNKCTSIGRE KHTVVADMDG TLLIGRSSFP
YFALIAFEVG GVLRLLIYLL ASPIAAILYY FISESAGIQV LVFASMAGMK LSSIESVARA
VLPKFYSSDL HPETWRVFSS CGKRCVLTAN PRIMVEPFLK EFLGADMVLG TEIASYKGRA
TGLICKPGIL VGDKKAQVLK KTFGDEKPDI GLGDRVTDAP FMALCKEGYI VPAKPKVTTV
TSDKLPKPII FHDGRLVQKP TPLMALLIIL WIPIGFPLAC LRIAAGSLLP MKFVYCAFKA
LGVRVIVKGT PPPPVETSKT NHQSGVLFIC SHRTLLDPIF LSTALGRAIP AVTYSVSRLS
EIISPIKTVR LSRDRATDAA MIKKLLQEGD LAICPEGTTC REPFLLRFSA LFAELTDELV
PVAMVNRMSM FHGTTARGWK GMDPFYFFMN PSPVYEVTFL NKLPKELTCG SGKTSHEVAN
YIQRVVASTL SYECTSFTRR DKYRALAGND GTVVEKTNKA NKVMGC
