FH14_ARATH
ID FH14_ARATH Reviewed; 1230 AA.
AC Q9C6S1;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 3.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Formin-like protein 14;
DE Short=AtFH14;
GN Name=FH14; OrderedLocusNames=At1g31810; ORFNames=F5M6.18;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 -!- SIMILARITY: Belongs to the formin-like family. Class-II subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG50715.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC079041; AAG50715.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31395.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58758.1; -; Genomic_DNA.
DR PIR; G86441; G86441.
DR RefSeq; NP_001321171.1; NM_001332980.1.
DR RefSeq; NP_174461.3; NM_102915.4.
DR AlphaFoldDB; Q9C6S1; -.
DR SMR; Q9C6S1; -.
DR BioGRID; 25302; 1.
DR IntAct; Q9C6S1; 1.
DR STRING; 3702.AT1G31810.1; -.
DR iPTMnet; Q9C6S1; -.
DR PaxDb; Q9C6S1; -.
DR PRIDE; Q9C6S1; -.
DR ProteomicsDB; 230417; -.
DR EnsemblPlants; AT1G31810.1; AT1G31810.1; AT1G31810.
DR EnsemblPlants; AT1G31810.2; AT1G31810.2; AT1G31810.
DR GeneID; 840068; -.
DR Gramene; AT1G31810.1; AT1G31810.1; AT1G31810.
DR Gramene; AT1G31810.2; AT1G31810.2; AT1G31810.
DR KEGG; ath:AT1G31810; -.
DR Araport; AT1G31810; -.
DR TAIR; locus:2034471; AT1G31810.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_002558_0_1_1; -.
DR InParanoid; Q9C6S1; -.
DR OMA; CELGGIS; -.
DR OrthoDB; 1204639at2759; -.
DR PRO; PR:Q9C6S1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C6S1; baseline and differential.
DR Genevisible; Q9C6S1; AT.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; IDA:TAIR.
DR GO; GO:0009574; C:preprophase band; IDA:TAIR.
DR GO; GO:0005819; C:spindle; IDA:TAIR.
DR GO; GO:0003779; F:actin binding; ISS:TAIR.
DR GO; GO:0051015; F:actin filament binding; IDA:TAIR.
DR GO; GO:0008017; F:microtubule binding; IDA:TAIR.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:TAIR.
DR GO; GO:0009556; P:microsporogenesis; IMP:TAIR.
DR Gene3D; 1.20.58.2220; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR014020; Tensin_C2-dom.
DR Pfam; PF02181; FH2; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR SMART; SM00498; FH2; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
PE 3: Inferred from homology;
KW Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..1230
FT /note="Formin-like protein 14"
FT /id="PRO_0000308539"
FT DOMAIN 1..194
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT DOMAIN 200..339
FT /note="C2 tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT DOMAIN 809..1207
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT REGION 412..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..578
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..651
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..771
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..794
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 127
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
SQ SEQUENCE 1230 AA; 135515 MW; DECDDB3B8B78A701 CRC64;
MSLLSRFFYK RPPDGLLEFA DRVYVFDSCF CTEVLADSLY QIFLHEVIND LHEEFPESSF
LAFNFREGEK KSVFAETLCE YDVTVLEYPR QYEGCPMLPL SLIQHFLRVC ESWLARGNRQ
DVILLHCERG GWPLLAFILA SFLIFRKVHS GERRTLEIVH REAPKGLLQL LSPLNPFPSQ
LRYLQYVARR NINSEWPPPE RALSLDCVII RGIPNFDSQH GCRPIIRIFG RNYSSKSGLS
TEMVYSMSDK KKPLRHYRQA ECDVIKIDIQ CWVQGDVVLE CVHMDLDPER EVMMFRVMFN
TAFIRSNILM LNSDNLDILW EAKDHYPKGF RAEVLFGEVE NASPQKVPTP IVNGDETGGL
PIEAFSRVQE LFSGVDLAEN GDDAALWLLK QLAAINDAKE FTRFRHKGSF YFNSPDSEEE
TNTSSAADSS DEGFEAIQRP RIHIPFDNDD TDDITLSVAH ESSEEPHEFS HHHHHEIPAK
DSVDNPLNLP SDPPSSGDHV TLLPPPPPPP PPPLFTSTTS FSPSQPPPPP PPPPLFMSTT
SFSPSQPPPP PPPPPLFTST TSFSPSQPPP PPPLPSFSNR DPLTTLHQPI NKTPPPPPPP
PPPLPSRSIP PPLAQPPPPR PPPPPPPPPS SRSIPSPSAP PPPPPPPPSF GSTGNKRQAQ
PPPPPPPPPP TRIPAAKCAP PPPPPPPTSH SGSIRVGPPS TPPPPPPPPP KANISNAPKP
PAPPPLPPSS TRLGAPPPPP PPPLSKTPAP PPPPLSKTPV PPPPPGLGRG TSSGPPPLGA
KGSNAPPPPP PAGRGRASLG LGRGRGVSVP TAAPKKTALK PLHWSKVTRA AKGSLWADTQ
KQENQPRAPE IDISELESLF SAVSDTTAKK STGRRGSSIS KPEKVQLVDL RRANNCEIML
TKIKIPLPDM LSAVLALDSL ALDIDQVENL IKFCPTKEEM ELLRNYTGDK EMLGKCEQFF
MELMKVPRIE AKLRVFGFKI TFASQVEELK SCLNTINAAT KEVKESAKLR QIMQTILTLG
NALNQGTARG SAVGFKLDSL LKLSDTRARN NKMTLMHYLC KLVGEKMPEL LDFANDLVHL
EAASKIELKT LAEEMQAATK GLEKVEQELM ASENDGAISL GFRKVLKEFL DMADEEVKTL
ASLYSEVGRN ADSLSHYFGE DPARCPFEQV TKILTLFMKT FIKSREENEK QAEAEKKKLE
KEAIKEKSAT KKDGVDNDND LIQQIHRHRT
