MFP1_ARATH
ID MFP1_ARATH Reviewed; 726 AA.
AC Q9LW85; Q7Y1Z5;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=MAR-binding filament-like protein 1;
GN Name=MFP1; OrderedLocusNames=At3g16000; ORFNames=MSL1.4;
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
CC -!- FUNCTION: Binds DNA. Interacts with chromatin via matrix attachment
CC regions (MARs). Likely to participate in nuclear architecture by
CC connecting chromatin with the nuclear matrix and potentially with the
CC nuclear envelope (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02666.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB012247; BAB02666.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75761.1; -; Genomic_DNA.
DR EMBL; BT008690; AAP40496.1; -; mRNA.
DR RefSeq; NP_188221.2; NM_112470.3.
DR AlphaFoldDB; Q9LW85; -.
DR SMR; Q9LW85; -.
DR STRING; 3702.AT3G16000.1; -.
DR iPTMnet; Q9LW85; -.
DR PaxDb; Q9LW85; -.
DR PRIDE; Q9LW85; -.
DR ProteomicsDB; 250621; -.
DR EnsemblPlants; AT3G16000.1; AT3G16000.1; AT3G16000.
DR GeneID; 820845; -.
DR Gramene; AT3G16000.1; AT3G16000.1; AT3G16000.
DR KEGG; ath:AT3G16000; -.
DR Araport; AT3G16000; -.
DR TAIR; locus:2093462; AT3G16000.
DR eggNOG; ENOG502QZ3X; Eukaryota.
DR HOGENOM; CLU_022159_0_0_1; -.
DR InParanoid; Q9LW85; -.
DR OMA; DEMNNSA; -.
DR OrthoDB; 374786at2759; -.
DR PhylomeDB; Q9LW85; -.
DR PRO; PR:Q9LW85; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LW85; baseline and differential.
DR Genevisible; Q9LW85; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0042646; C:plastid nucleoid; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0010581; P:regulation of starch biosynthetic process; IMP:TAIR.
DR GO; GO:0019252; P:starch biosynthetic process; IMP:TAIR.
PE 2: Evidence at transcript level;
KW Coiled coil; DNA-binding; Nucleus; Reference proteome.
FT CHAIN 1..726
FT /note="MAR-binding filament-like protein 1"
FT /id="PRO_0000096460"
FT REGION 678..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 139..691
FT /evidence="ECO:0000255"
FT COMPBIAS 699..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 726 AA; 81973 MW; A7353BD1C93D460C CRC64;
MGFLIGGSCF VPSVPLHSRF LSSPSSSSSS SPSSSQFGLL CSSNVAKFKR RRPTLASLNQ
EDGYEYDVAS AKRRAFLLVG ISVLPFLQLR SPALADERGN EIKTSKVDLE TEVAVVSEGT
SPNPFLALLN GLGIFSAGVL GALYALARQD TKAAEETIES LKNQLKDRER ALVLKEKDFE
AKLQHEQEER KKEVEKAKEE QLSLINQLNS AKDLVTELGR ELSSEKKLCE KLKDQIESLE
NSLSKAGEDK EALETKLREK LDLVEGLQDR INLLSLELKD SEEKAQRFNA SLAKKEAELK
ELNSIYTQTS RDLAEAKLEI KQQKEELIRT QSELDSKNSA IEELNTRITT LVAEKESYIQ
KLDSISKDYS ALKLTSETQA AADAELISRK EQEIQQLNEN LDRALDDVNK SKDKVADLTE
KYEDSKRMLD IELTTVKNLR HELEGTKKTL QASRDRVSDL ETMLDESRAL CSKLESELAI
VHEEWKEAKE RYERNLDAEK QKNEISASEL ALEKDLRRRV KDELEGVTHE LKESSVKNQS
LQKELVEIYK KVETSNKELE EEKKTVLSLN KEVKGMEKQI LMEREARKSL ETDLEEAVKS
LDEMNKNTSI LSRELEKVNT HASNLEDEKE VLQRSLGEAK NASKEAKENV EDAHILVMSL
GKEREVLEKK VKKLEEDLGS AKGEILRMRS QPDSVKAVNS TDNKEKSDNT VTVKKVVRRR
KSSTSS
