FH2_ARATH
ID FH2_ARATH Reviewed; 894 AA.
AC O22824;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Formin-like protein 2;
DE Short=AtFH2;
DE Short=AtFORMIN-2;
DE Flags: Precursor;
GN Name=FH2; OrderedLocusNames=At2g43800; ORFNames=F18O19.9;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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.
RX PubMed=11104517; DOI=10.1186/gb-2000-1-1-research001;
RA Cvrckova F.;
RT "Are plant formins integral membrane proteins?";
RL Genome Biol. 1:RESEARCH001.1-RESEARCH001.7(2000).
RN [4]
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 [5]
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}.
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; AC002333; AAB64026.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10328.1; -; Genomic_DNA.
DR PIR; F84870; F84870.
DR RefSeq; NP_181908.1; NM_129942.3.
DR AlphaFoldDB; O22824; -.
DR SMR; O22824; -.
DR STRING; 3702.AT2G43800.1; -.
DR iPTMnet; O22824; -.
DR PaxDb; O22824; -.
DR PRIDE; O22824; -.
DR ProteomicsDB; 230096; -.
DR EnsemblPlants; AT2G43800.1; AT2G43800.1; AT2G43800.
DR GeneID; 818984; -.
DR Gramene; AT2G43800.1; AT2G43800.1; AT2G43800.
DR KEGG; ath:AT2G43800; -.
DR Araport; AT2G43800; -.
DR TAIR; locus:2043989; AT2G43800.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_007699_0_0_1; -.
DR InParanoid; O22824; -.
DR OMA; FHGNSET; -.
DR OrthoDB; 1204639at2759; -.
DR PhylomeDB; O22824; -.
DR PRO; PR:O22824; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22824; baseline and differential.
DR Genevisible; O22824; 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 GO; GO:0051016; P:barbed-end actin filament capping; IDA:TAIR.
DR GO; GO:0010497; P:plasmodesmata-mediated intercellular transport; IMP:TAIR.
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 3: Inferred from homology;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..894
FT /note="Formin-like protein 2"
FT /id="PRO_0000308527"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 438..864
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT REGION 41..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..125
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..421
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 894 AA; 98320 MW; FA516602A240E233 CRC64;
MTTIPFCFLF VAFFFSSSTA DQRHHSRHLL HQPFFPVVTA APPPYQPPVS SQPPSPSPHT
HHHHKKHLTT TTPPPHEKHL FSSVANPPPP PPSPPHPNPF FPSSDPTSTA SHPPPAPPPP
ASLPTFPANI SSLLFPTHNK QSKPPSNGHI ARLVTITASV ISAAALLSLF AVFIIFIRRT
RHRRRSSPAD DTKSTRSDAL QLFNASPSDG SKKQKQHQQP PKYTSSHTSS EFLYLGTLVN
SRSNGLEQQK SPISLSGGIT GVLELPPPAS SSSSSSYSQY HKLGSPELRP LPPLPKLQSF
TPVYKSTEQL NPKRQDFDGD DNENDEFFSP RGSSGRKQSP TRVSDVDQID NRSINGSGSN
SCSPTNFAPS LNASPGTSLK PKSISPPVSL HSQISSNNGI PKRLCPARPP PPPPPPPQVS
EVPATMSHSL PGDDSDPEKK VETMKPKLKT LHWDKVRASS SRVMVWDQIK SNSFQVNEEM
IETLFKVNDP TSRTRDGVVQ SVSQENRFLD PRKSHNIAIL LRALNVTADE VCEALIEGNS
DTLGPELLEC LLKMAPTKEE EDKLKELKDD DDGSPSKIGP AEKFLKALLN IPFAFKRIDA
MLYIVKFESE IEYLNRSFDT LEAATGELKN TRMFLKLLEA VLKTGNRMNI GTNRGDAHAF
KLDTLLKLVD IKGADGKTTL LHFVVQEIIK FEGARVPFTP SQSHIGDNMA EQSAFQDDLE
LKKLGLQVVS GLSSQLINVK KAAAMDSNSL INETAEIARG IAKVKEVITE LKQETGVERF
LESMNSFLNK GEKEITELQS HGDNVMKMVK EVTEYFHGNS ETHPFRIFAV VRDFLTILDQ
VCKEVGRVNE RTVYGSMPLH SPSNQTATPL FPVVINNNSR LSPSGSLDDD DGSF