GLC_ARATH
ID GLC_ARATH Reviewed; 450 AA.
AC O80816; Q1PFG7; Q8LDZ6;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Acyltransferase GLAUCE {ECO:0000303|PubMed:17965055, ECO:0000303|PubMed:22872756};
DE EC=2.3.1.- {ECO:0000305};
GN Name=GLC {ECO:0000303|PubMed:17965055, ECO:0000303|PubMed:22872756};
GN OrderedLocusNames=At1g65450 {ECO:0000312|Araport:AT1G65450};
GN ORFNames=T8F5.23 {ECO:0000312|EMBL:AAC27152.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=17965055; DOI=10.1242/dev.007310;
RA Ngo Q.A., Moore J.M., Baskar R., Grossniklaus U., Sundaresan V.;
RT "Arabidopsis GLAUCE promotes fertilization-independent endosperm
RT development and expression of paternally inherited alleles.";
RL Development 134:4107-4117(2007).
RN [6]
RP ALTERNATIVE SPLICING, FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=22872756; DOI=10.1105/tpc.112.096420;
RA Leshem Y., Johnson C., Wuest S.E., Song X., Ngo Q.A., Grossniklaus U.,
RA Sundaresan V.;
RT "Molecular characterization of the glauce mutant: a central cell-specific
RT function is required for double fertilization in Arabidopsis.";
RL Plant Cell 24:3264-3277(2012).
CC -!- FUNCTION: Required for double fertilization of the egg cell and the
CC central cell by two sperm cells, resulting in the formation of the
CC embryo and the endosperm (PubMed:22872756, PubMed:17965055). Involved
CC in the regulation of embryonic expression of PHE1 (PubMed:17965055).
CC Essential in maternal tissues to ensure the paternal embryonic
CC expression of several genes, including RPS5a and FAC1, both of which
CC being essential for early embryo and endosperm development in
CC fertilized seeds (PubMed:17965055). {ECO:0000269|PubMed:17965055,
CC ECO:0000269|PubMed:22872756}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22872756}. Nucleus
CC {ECO:0000269|PubMed:22872756}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O80816-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O80816-2; Sequence=VSP_061484, VSP_061485;
CC Name=3;
CC IsoId=O80816-3; Sequence=VSP_061483;
CC -!- TISSUE SPECIFICITY: Restricted to the central cells of embryo sacs.
CC {ECO:0000269|PubMed:22872756}.
CC -!- DEVELOPMENTAL STAGE: [Isoform 2]: Observed throughout the embryo sac
CC and in sporophytic tissues including the funiculus and the placenta.
CC {ECO:0000269|PubMed:22872756}.
CC -!- DEVELOPMENTAL STAGE: [Isoform 3]: In the embryo sac, confined to
CC synergid cells (SCs) (PubMed:22872756). Observed in sporophytic tissues
CC including the micropylar end of integuments and placenta
CC (PubMed:22872756). {ECO:0000269|PubMed:22872756}.
CC -!- DISRUPTION PHENOTYPE: Female gametophytic mutant which exhibits embryo
CC development without any endosperm due to a successful sperm cell fusion
CC with the egg cell but an impaired fusion of the second sperm cell with
CC the central cell, thus resulting in single fertilization
CC (PubMed:22872756, PubMed:17965055). Embryos can develop up to the
CC globular stage in the absence of endosperm (PubMed:17965055).
CC {ECO:0000269|PubMed:17965055, ECO:0000269|PubMed:22872756}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {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; AC004512; AAC27152.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34376.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34377.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34378.1; -; Genomic_DNA.
DR EMBL; DQ446396; ABE65741.1; -; mRNA.
DR EMBL; AY085709; AAM62927.1; -; mRNA.
DR PIR; T02368; T02368.
DR RefSeq; NP_001185318.1; NM_001198389.2.
DR RefSeq; NP_001185319.1; NM_001198390.2.
DR RefSeq; NP_564853.2; NM_105220.3.
DR AlphaFoldDB; O80816; -.
DR SMR; O80816; -.
DR STRING; 3702.AT1G65450.1; -.
DR PaxDb; O80816; -.
DR PRIDE; O80816; -.
DR ProteomicsDB; 175185; -.
DR DNASU; 842857; -.
DR EnsemblPlants; AT1G65450.1; AT1G65450.1; AT1G65450. [O80816-1]
DR EnsemblPlants; AT1G65450.2; AT1G65450.2; AT1G65450. [O80816-2]
DR EnsemblPlants; AT1G65450.3; AT1G65450.3; AT1G65450. [O80816-3]
DR GeneID; 842857; -.
DR Gramene; AT1G65450.1; AT1G65450.1; AT1G65450. [O80816-1]
DR Gramene; AT1G65450.2; AT1G65450.2; AT1G65450. [O80816-2]
DR Gramene; AT1G65450.3; AT1G65450.3; AT1G65450. [O80816-3]
DR KEGG; ath:AT1G65450; -.
DR Araport; AT1G65450; -.
DR TAIR; locus:2206340; AT1G65450.
DR eggNOG; ENOG502QV0F; Eukaryota.
DR HOGENOM; CLU_014546_2_0_1; -.
DR InParanoid; O80816; -.
DR OMA; AIDWGEI; -.
DR OrthoDB; 1130893at2759; -.
DR PhylomeDB; O80816; -.
DR BioCyc; ARA:AT1G65450-MON; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O80816; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR GO; GO:0009567; P:double fertilization forming a zygote and endosperm; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 2: Evidence at transcript level;
KW Acyltransferase; Alternative splicing; Cytoplasm; Fertilization; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..450
FT /note="Acyltransferase GLAUCE"
FT /id="PRO_0000455300"
FT ACT_SITE 171
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9FI78"
FT ACT_SITE 394
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9FI78"
FT VAR_SEQ 1..164
FT /note="Missing (in isoform 3)"
FT /id="VSP_061483"
FT VAR_SEQ 155..166
FT /note="ITSFKCGGFAMG -> EERKKKSKVLSV (in isoform 2)"
FT /id="VSP_061484"
FT VAR_SEQ 167..450
FT /note="Missing (in isoform 2)"
FT /id="VSP_061485"
SQ SEQUENCE 450 AA; 50506 MW; 4D0D25ACB60AB1FC CRC64;
MGSSYQESPP LLLEDLKVTI KESTLIFPSE ETSERKSMFL SNVDQILNFD VQTVHFFRPN
KEFPPEMVSE KLRKALVKLM DAYEFLAGRL RVDPSSGRLD VDCNGAGAGF VTAASDYTLE
ELGDLVYPNP AFAQLVTSQL QSLPKDDQPL FVFQITSFKC GGFAMGISTN HTTFDGLSFK
TFLENLASLL HEKPLSTPPC NDRTLLKARD PPSVAFPHHE LVKFQDCETT TVFEATSEHL
DFKIFKLSSE QIKKLKERAS ETSNGNVRVT GFNVVTALVW RCKALSVAAE EGEETNLERE
STILYAVDIR GRLNPELPPS YTGNAVLTAY AKEKCKALLE EPFGRIVEMV GEGSKRITDE
YARSAIDWGE LYKGFPHGEV LVSSWWKLGF AEVEYPWGKP KYSCPVVYHR KDIVLLFPDI
DGDSKGVYVL AALPSKEMSK FQHWFEDTLC
