ID A0A175YD06_DAUCS Unreviewed; 1526 AA.
AC A0A175YD06;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Formin-like protein {ECO:0000256|RuleBase:RU361260};
GN ORFNames=DCAR_032308 {ECO:0000313|EMBL:KZM80712.1};
OS Daucus carota subsp. sativus (Carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=79200 {ECO:0000313|EMBL:KZM80712.1, ECO:0000313|Proteomes:UP000077755};
RN [1] {ECO:0000313|EMBL:KZM80712.1, ECO:0000313|Proteomes:UP000077755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH1 {ECO:0000313|Proteomes:UP000077755};
RC TISSUE=Leaf {ECO:0000313|EMBL:KZM80712.1};
RX PubMed=27158781; DOI=10.1038/ng.3565;
RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT "A high-quality carrot genome assembly provides new insights into
RT carotenoid accumulation and asterid genome evolution.";
RL Nat. Genet. 48:657-666(2016).
CC -!- SIMILARITY: Belongs to the formin-like family. Class-II subfamily.
CC {ECO:0000256|ARBA:ARBA00006468}.
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:KZM80712.1}.
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DR EMBL; LNRQ01000045; KZM80712.1; -; Genomic_DNA.
DR STRING; 79200.A0A175YD06; -.
DR EnsemblPlants; KZM80712; KZM80712; DCAR_032308.
DR Gramene; KZM80712; KZM80712; DCAR_032308.
DR Proteomes; UP000077755; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1110; -; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 2.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
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 PANTHER; PTHR45733; FORMIN-J; 1.
DR PANTHER; PTHR45733:SF10; FORMIN-LIKE PROTEIN 15A-RELATED; 1.
DR Pfam; PF02181; FH2; 2.
DR Pfam; PF10409; PTEN_C2; 1.
DR SMART; SM00498; FH2; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51444; FH2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000077755}.
FT DOMAIN 381..521
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1128..1514
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 647..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1493..1526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1395..1450
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 650..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..906
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..932
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1125
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1493..1520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1526 AA; 170291 MW; EA2143710EB788C3 CRC64;
MEFLMYSITG TAYGISFSDV EVVTSKQMAM DLDKQYNDLA KNYLHSNDTG FEIGFGFHQS
VIKLENIVHS KVENLHKPIV KWFNFEDSRI TNASSDEGAF LVASRELKFQ FCKRTQSSIS
VRERHPFSTG YIKRELKLLN LLDFTSKRKV RDEDGKIWLL CKGAGSRSPR GYKYSVVLKI
LAKSDRRLFY RKPPDRLLEI TDKVYVFDCC LSRNVMEEDE YKVYLGGIVA ELQDYYEDDA
SYMVFNFKQG DNTSLVSSFL SSYGMTIMEY PQHFEGTPLL PLETIHKILH FCQSWLSLTG
HHVLLMHCEY GGWPLLAFML AALLLYRKQY DSEHKTLEMI YNQAPRELLY LFSPLNPHPS
HLRYLQYMSH TTLGLHWALV DTPLALDCII FRLLPLFDGG KGCRPVVRVY GHVPSSASTN
KSSKLLFSTL KTRENARLYR QEECQLVKLD FHIRVQGDVI LECVHLAEDL IREEMMFRVM
FHTAFIRLNV LMLERDQIDV LWDVKVHFSK DFFAKVLFSD ADVPPSIINT QVPSTLETES
ESASPDEFFE VEELFSDIVD AHDVKGDVLD TRLIKDNSPN EVAWKEDLEP YAFQDCASED
GNHKQDDLLN SDIFHELKPL FLDNISGELY ITRHDNDTPC SLETEISDVS GMSEIEKEQP
REPDHLERFR NKNLQKKSDV DASKQERESD HLFTKGTFRS KSVTDSPNSF KTNSQGSQNS
SLRQAKADKL SPSNKGPYAN SLHVSHLPSR HNSAPPILVH AKDTQFKGDS HTLFCMISKM
TCIDNIHRKN TSCPPVLAVS NHITYEPLAR PPHSSCPSIP LTHDVERPPI PTLGSSSQCP
TPSVLVAQPH TSTFMVSSQP LETSFHKFCE PGSRPGDYGP QPPPPPHKTV VNELGPPPPP
PNLIISTFPP ESGQGPSSPG PAPPPLPKVV PRSIPPLGAR FRRMYGRKHL GPRKNSMKPL
RSSTQSPTPS VPTVPQPQPH VPTFIVSSQP LEPPLPKHGE TRSPPHVSPP PPPNPPSRVD
GNGPPPCPAP PPPDGGLGPP PPPPPPGVGP APAPPSPPPG VGPAPPPPPP PPGASPAPPL
PPSAGPPLPP PPGSGLAPPP PGPAPPPPPS VGAGPRPPPP SGTGPGSQNN GPSAPASKGL
QRWKHLGPRK TNLKPLHWSK VTRALHGSVW EELQKSEDPQ NEREFDVSEI ETLFSAALPK
PKNSKKSDGH NSATKMETVQ LIEHRRAYNT EIMLTKIKMG LHDMTDAILT MDDTILDADQ
VEILIKFCPT KEEIELLNNY TGDKERLGRC EQISDFKNNL NVVIVVCEEV RNSRKLKEIM
SKILFVGNTL NQGTARGSAV GFKLDSLLKL TETRSTNNKM TLMHYLCKVF ADKLPHLLDF
YEDLISLETA SKIQLKVLAE EMQAINKGLE RVKQELDASK SDGPVSEVFV KTLEEFVQGA
EREVASVQNL YTVAGSNADA LALYFNEDPT RFPFEQVTTT LLNFVRMFRK AHDENRKQDE
LEKKRKQKEV EMEKARGTNK TKGPVK
//
