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Database: UniProt
Entry: A0A2J6LU96_LACSA
LinkDB: A0A2J6LU96_LACSA
Original site: A0A2J6LU96_LACSA 
ID   A0A2J6LU96_LACSA        Unreviewed;       941 AA.
AC   A0A2J6LU96;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Formin-like protein {ECO:0000256|RuleBase:RU361260};
GN   ORFNames=LSAT_5X4561 {ECO:0000313|EMBL:PLY90784.1};
OS   Lactuca sativa (Garden lettuce).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC   Lactucinae; Lactuca.
OX   NCBI_TaxID=4236 {ECO:0000313|EMBL:PLY90784.1};
RN   [1] {ECO:0000313|EMBL:PLY90784.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28401891; DOI=10.1038/ncomms14953;
RA   Reyes-Chin-Wo S., Wang Z., Yang X., Kozik A., Arikit S., Song C., Xia L.,
RA   Froenicke L., Lavelle D.O., Truco M.J., Xia R., Zhu S., Xu C., Xu H.,
RA   Xu X., Cox K., Korf I., Meyers B.C., Michelmore R.W.;
RT   "Genome assembly with in vitro proximity ligation data and whole-genome
RT   triplication in lettuce.";
RL   Nat. Commun. 8:14953-14953(2017).
CC   -!- SIMILARITY: Belongs to the formin-like family. Class-I subfamily.
CC       {ECO:0000256|ARBA:ARBA00025793}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PLY90784.1}.
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DR   EMBL; NBSK01002330; PLY90784.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6LU96; -.
DR   STRING; 4236.A0A2J6LU96; -.
DR   EnsemblPlants; rna-gnl|WGS:NBSK|LSAT_5X4561_mrna; cds-PLY90784.1; gene-LSAT_5X4561.
DR   Gramene; rna-gnl|WGS:NBSK|LSAT_5X4561_mrna; cds-PLY90784.1; gene-LSAT_5X4561.
DR   OrthoDB; 623207at2759; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR   Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR   InterPro; IPR015425; FH2_Formin.
DR   InterPro; IPR042201; FH2_Formin_sf.
DR   InterPro; IPR027643; Formin-like_plant.
DR   PANTHER; PTHR23213:SF359; FORMIN-LIKE PROTEIN; 1.
DR   PANTHER; PTHR23213; FORMIN-RELATED; 1.
DR   Pfam; PF02181; FH2; 1.
DR   SMART; SM00498; FH2; 1.
DR   SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR   PROSITE; PS51444; FH2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..941
FT                   /note="Formin-like protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014372534"
FT   TRANSMEM        159..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          463..903
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   REGION          203..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          892..941
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..221
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..313
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..336
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..381
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..449
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        897..918
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   941 AA;  102724 MW;  C08D29BE0AD2BE21 CRC64;
     MGAKVVILFM TIIILLYPLA EAIESDRHRQ QLPPDNQMYL EETMDEDTAE LLWVNCGAEL
     MYTMEAFEDL EYCGCDKSIT GKERIIKAIN VQDPHVKKTI LDCLKEKRIV LSKLRKDKLS
     TRTSLYIEYL VSFLSNPNII IDHVHGRRKL GETVSQGTVV VAVIVTAIFT MCLAGLLFYC
     YIRKHGGIQN NDEKPLLSLS MGGFRRKSTD NQSNGQKNDS PMDARVSVDP DASGITNVND
     GSSLDPSMQQ PRVKESLRHT LKPRAVRAES SLRPTGKTEF ALRPSAGNTG SPVGVGGIES
     SPQLESSEQQ PPPTGSSLAP PALTADPPPP PAHVVPLVQL TEPKPSSDEP PPPQTQGAAP
     LPRTQGASPL PSQTQGAPPS PSQTQGAPPP PPPTGEAGGA PPPPPPVAEG SGAPPPPPPT
     GGSGSGAPPP PPKLGGNAGA PPPPPLRGSV ARPLSAALRL RRTEQVDASK AKLKPFFWDK
     VMAKPDQQMV WDKIRSGSFQ FNEEMIESLF GYQAAEKNKD QDTKNAATKN KDPPVHFVQI
     IDPKKAQNLS ILLKALNVTT EEVSAALIEG NELPLEIVQT LLKMAPTSEE ELKLRLYDGD
     LHRLGPAERF LKVLVEIPYA FRRLESLLFM CTLQDEESNI KESLETLEAA CVQLKKSRLF
     LKLLEAVLKT GNRMNVGTFR GSATAFKLDT LLKLSDVKGV DGKTTLLHFV VQEIMRSEGI
     RAVRSAKEGK SISSIKTEDL LLEPPPEEAD EHYCKLGLEV VSCLSSELED VKRAAIIDAD
     GLTSSVSKLG NALLKARESL NTDMKILEEQ LEEEADEFWL ILSTFVENAD KQITWMLEEE
     KRIMALVKST ADYFHGKSGK DEGLRLFTVV RDFLIILEKV VKEIQAAPIK PLKKKADMSS
     GTQKKEDMSS DPERKDDQNQ ATNGAPTLTR IPNCQIPSPP D
//
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