AG103_ARATH
ID AG103_ARATH Reviewed; 386 AA.
AC Q9LSB2;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Agamous-like MADS-box protein AGL103 {ECO:0000305};
GN Name=AGL103 {ECO:0000305};
GN OrderedLocusNames=At3g18650 {ECO:0000312|Araport:AT3G18650};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND INTERACTION WITH ME14/CBP1.
RX PubMed=26462908; DOI=10.1105/tpc.15.00370;
RA Li H.J., Zhu S.S., Zhang M.X., Wang T., Liang L., Xue Y., Shi D.Q., Liu J.,
RA Yang W.C.;
RT "Arabidopsis CBP1 is a novel regulator of transcription initiation in
RT central cell-mediated pollen tube guidance.";
RL Plant Cell 27:2880-2893(2015).
CC -!- FUNCTION: Probable transcription factor that may function in the
CC maintenance of the proper function of the central cell in pollen tube
CC attraction. {ECO:0000305|PubMed:26462908}.
CC -!- SUBUNIT: Interacts with MEE14/CBP1. {ECO:0000269|PubMed:26462908}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
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DR EMBL; AB026654; BAB01791.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76126.1; -; Genomic_DNA.
DR EMBL; BT029549; ABL66805.1; -; mRNA.
DR RefSeq; NP_188495.1; NM_112751.1.
DR AlphaFoldDB; Q9LSB2; -.
DR SMR; Q9LSB2; -.
DR IntAct; Q9LSB2; 18.
DR STRING; 3702.AT3G18650.1; -.
DR iPTMnet; Q9LSB2; -.
DR PaxDb; Q9LSB2; -.
DR PRIDE; Q9LSB2; -.
DR EnsemblPlants; AT3G18650.1; AT3G18650.1; AT3G18650.
DR GeneID; 821396; -.
DR Gramene; AT3G18650.1; AT3G18650.1; AT3G18650.
DR KEGG; ath:AT3G18650; -.
DR Araport; AT3G18650; -.
DR TAIR; locus:2093979; AT3G18650.
DR eggNOG; KOG0014; Eukaryota.
DR HOGENOM; CLU_764155_0_0_1; -.
DR InParanoid; Q9LSB2; -.
DR OMA; NMLTYNN; -.
DR OrthoDB; 1277849at2759; -.
DR PhylomeDB; Q9LSB2; -.
DR PRO; PR:Q9LSB2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LSB2; differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00266; MADS_SRF_like; 1.
DR Gene3D; 3.40.1810.10; -; 1.
DR InterPro; IPR033897; MADS_SRF-like.
DR InterPro; IPR002100; TF_MADSbox.
DR InterPro; IPR036879; TF_MADSbox_sf.
DR Pfam; PF00319; SRF-TF; 1.
DR PRINTS; PR00404; MADSDOMAIN.
DR SMART; SM00432; MADS; 1.
DR SUPFAM; SSF55455; SSF55455; 1.
DR PROSITE; PS50066; MADS_BOX_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..386
FT /note="Agamous-like MADS-box protein AGL103"
FT /id="PRO_0000435417"
FT DOMAIN 29..76
FT /note="MADS-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00251"
SQ SEQUENCE 386 AA; 43552 MW; D69F0A0C151F2B05 CRC64;
MASSSSSSLS FSTSKKNKTF FKKPNSAFSS SRATSLIKRQ QTVFKKAKEL SILCDIDVCV
ICYGSNGELK TWPEEREKVK AIARRYGELS ETKRRKGSVD LHEFLEKMNK DDPEKEEKKK
IKVRRVPKVK YPVWDPRFDN YSVEQLMGLV QSLERNLTRI QHRTCAVVEA QGQRRVQYTN
MANQELMMAN TMNQLQQHSN QVSMYLWNHG NGAFSQIPVS ALASNQTQSL APIPPELMIY
PNSDAGNYSG SLGVQGTGIN GLQNMNMLTY NNINSVNDFS KQFDQNSRAE SYSSLLGVHE
DGNNEFENPN MSSRNNFNVQ DCAGLLGMQG AGTNGLQSMN MHDYSNNNSI NSNGLSHQYV
QFPTYNSQHQ DRVFNLDQNG NNTRSL