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FH11_ARATH
ID   FH11_ARATH              Reviewed;         884 AA.
AC   Q9MA60;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Formin-like protein 11;
DE            Short=AtFH11;
DE   Flags: Precursor;
GN   Name=FH11; OrderedLocusNames=At3g05470; ORFNames=F22F7.8;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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   GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX   PubMed=12417149; DOI=10.1016/s1360-1385(02)02341-5;
RA   Deeks M.J., Hussey P.J., Davies B.;
RT   "Formins: intermediates in signal-transduction cascades that affect
RT   cytoskeletal reorganization.";
RL   Trends Plant Sci. 7:492-498(2002).
RN   [4]
RP   GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX   PubMed=15256004; DOI=10.1186/1471-2164-5-44;
RA   Cvrckova F., Novotny M., Pickova D., Zarsky V.;
RT   "Formin homology 2 domains occur in multiple contexts in angiosperms.";
RL   BMC Genomics 5:44-44(2004).
CC   -!- FUNCTION: Might be involved in the organization and polarity of the
CC       actin cytoskeleton. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the formin-like family. Class-I subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AC009606; AAF64546.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74244.1; -; Genomic_DNA.
DR   RefSeq; NP_187198.1; NM_111420.2.
DR   AlphaFoldDB; Q9MA60; -.
DR   SMR; Q9MA60; -.
DR   STRING; 3702.AT3G05470.1; -.
DR   iPTMnet; Q9MA60; -.
DR   PaxDb; Q9MA60; -.
DR   PRIDE; Q9MA60; -.
DR   ProteomicsDB; 230092; -.
DR   EnsemblPlants; AT3G05470.1; AT3G05470.1; AT3G05470.
DR   GeneID; 819712; -.
DR   Gramene; AT3G05470.1; AT3G05470.1; AT3G05470.
DR   KEGG; ath:AT3G05470; -.
DR   Araport; AT3G05470; -.
DR   TAIR; locus:2079807; AT3G05470.
DR   eggNOG; KOG1922; Eukaryota.
DR   HOGENOM; CLU_007699_2_0_1; -.
DR   InParanoid; Q9MA60; -.
DR   OMA; GMLDNVC; -.
DR   OrthoDB; 1204639at2759; -.
DR   PhylomeDB; Q9MA60; -.
DR   PRO; PR:Q9MA60; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9MA60; baseline and differential.
DR   Genevisible; Q9MA60; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; ISS:TAIR.
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; -; 1.
DR   InterPro; IPR015425; FH2_Formin.
DR   InterPro; IPR042201; FH2_Formin_sf.
DR   InterPro; IPR027643; Formin-like_plant.
DR   PANTHER; PTHR23213; PTHR23213; 1.
DR   Pfam; PF02181; FH2; 1.
DR   SMART; SM00498; FH2; 1.
DR   PROSITE; PS51444; FH2; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..884
FT                   /note="Formin-like protein 11"
FT                   /id="PRO_0000308536"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          461..884
FT                   /note="FH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT   REGION          89..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          307..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          416..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          512..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..132
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..346
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..381
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..438
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   884 AA;  98535 MW;  56CD20CBAFA1F9A6 CRC64;
     MVYFRQIFLM IIVVSLHCCK VRFFCIVANA KELDDWKVLT VENGERYRTH VGRYAGEEGG
     EKIKLRVLEK FRALLDLIKP STSRRRNLAE SASFSPWPAP SPSPFPNGGP IESPAYPPAP
     PRPIPPHLRR PLPQRTHPLE QPEIQRRKHE KGGTFKKILV PVVASTASAI GFVVCVVGVF
     CLCARRKRKM NGKTLSFKRK KGKSQSSTRK VSVNPTLDFL YLNSLGVDLE RQNSVSVKEI
     RETEKDLNGI NGGLLEEEVK RSIETEISHD WDNASSYSTK EIVSVHENDE EQTVNSVSVP
     VVVINDSSDD DESFHSVGGG SQYSNPRLSN ASSASGSVNV GSSQRFSEHK LDIPECSRSD
     FGISVSAPPP PPPPPPPLPQ FSNKRIHTLS SPETANLQTL SSQLCEKLCA SSSKTSFPIN
     VPNSQPRPPP PPPPPQQLQV AGINKTPPPP LSLDFSERRP LGKDGAPLPK LKPLHWDKVR
     ATPDRTMVWD KLRTSSFELD EEMIESLFGY TMQSSTKNEE GKSKTPSPGK HLLEPKRLQN
     FTILLKALNA TADQICSALG KGEGLCLQQL EALVKMVPTK EEELKLRSYK GAVDELGSAE
     KFLRALVGVP FAFQRAEAML YRETFEDEVV HLRNSFSMLE EACKELKSSR LFLKLLEAVL
     KTGNRMNVGT IRGGAKAFKL DALLKLSDVK GTDGKTTLLH FVVQEISRSE GIRVSDSIMG
     RIMNQRSNKN RTPEEKEEDY RRMGLDLVSG LNTELRNVKK TATIDLEGLV TSVSNLRDGL
     GQLSCLASEK LKGDEENRAF VSSMSSFLRY GEKSLEELRE DEKRIMERVG EIAEYFHGDV
     RGDEKNPLRI FVIVRDFLGM LDHVCRELRC VRVPNSPSPL APFR
 
 
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