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Database: UniProt
Entry: A0A251UT83_HELAN
LinkDB: A0A251UT83_HELAN
Original site: A0A251UT83_HELAN 
ID   A0A251UT83_HELAN        Unreviewed;      1158 AA.
AC   A0A251UT83;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Formin-like protein {ECO:0000256|RuleBase:RU361260};
GN   ORFNames=HannXRQ_Chr05g0148691 {ECO:0000313|EMBL:OTG25531.1};
OS   Helianthus annuus (Common sunflower).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Helianthus.
OX   NCBI_TaxID=4232 {ECO:0000313|EMBL:OTG25531.1, ECO:0000313|Proteomes:UP000215914};
RN   [1] {ECO:0000313|Proteomes:UP000215914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RX   PubMed=28538728; DOI=10.1038/nature22380;
RA   Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA   Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA   Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA   Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA   Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA   Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA   Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA   Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA   Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA   Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA   Vincourt P., Rieseberg L.H., Langlade N.B.;
RT   "The sunflower genome provides insights into oil metabolism, flowering and
RT   Asterid evolution.";
RL   Nature 546:148-152(2017).
CC   -!- SIMILARITY: Belongs to the formin-like family. Class-II subfamily.
CC       {ECO:0000256|ARBA:ARBA00006468}.
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DR   EMBL; CM007894; OTG25531.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A251UT83; -.
DR   STRING; 4232.A0A251UT83; -.
DR   InParanoid; A0A251UT83; -.
DR   OMA; NTQWPPL; -.
DR   Proteomes; UP000215914; Chromosome 5.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.1110; -; 1.
DR   Gene3D; 6.10.30.50; -; 1.
DR   Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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   PANTHER; PTHR45733; FORMIN-J; 1.
DR   PANTHER; PTHR45733:SF16; FORMIN-LIKE PROTEIN; 1.
DR   Pfam; PF02181; FH2; 1.
DR   Pfam; PF10409; PTEN_C2; 1.
DR   PRINTS; PR01217; PRICHEXTENSN.
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   Reference proteome {ECO:0000313|Proteomes:UP000215914}.
FT   DOMAIN          308..447
FT                   /note="C2 tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51182"
FT   DOMAIN          713..1120
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   REGION          524..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          587..752
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1108..1158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..705
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1158 AA;  129283 MW;  6CBCF2B7839ABBE3 CRC64;
     MALLRKLLSK KLPENLVFVF ERIYGKKKAK QKTEIQSQWE QPLYPPGIDV RFTPITPSLN
     PTNSSTISWI MLGTHVCLFI DMASLSLFPL VQQFSSWHCR FSVLLKKITG HYPLQKKKIR
     TYFSLIFGVY IVFDCCFTTG AWEQDYKAYV GKVITQQKEM YPECSIMILD FREADEENRI
     ASALADYDHI TIMDYPRHYE GCPLLSLEVI HHFLKSTESW LSVAQQNILI MHSEIGGWPV
     LALMAAALAL YRKYFTVETK ALEIVYKQAP IALSNMSPIN PMPSQLRYLQ YVSRRNANAA
     DSEWPPADKA LTLDCVIMRM IPDFDGKGGC CPVFRIYGRD PLLHVDKTPK LLFSTPRRRK
     NIRYYNQADS ELVKIDINCH VQGDVVLECI SLHDDMVKEK IMYRAIFNTA FIKSNMLILS
     RDEIDIHWDA KDQFHKDFRA ELLFSEMDPS TSMVPVDLSC FEEEGLPVEA FAKVQDMFGS
     GDWLVPKSDD ALNRLHQMPL SDVVNEMLET SYQRTESRNL LQTLTKRNNN QDKEITVGPR
     SISLPRQLPS SSTQSPTDAS KKSLSLSSSM PPHIILTCAH PSLSEKLRET AAAASSPPLP
     PPDGKANAPP PPPPPLPNKA GGAPPPPPPN AGGGPPPPPP PAPPAPKAPA PPAPPPPKPK
     AAPPPPPPAA PSSNGNAKGG APPPPPPGLS KESGVAAPSP PPPTKGRALS RTSAVKSQPT
     KKLKPLHWSK INKPAQGSMW AESQKHGEAS RAPEIDMSEL ENLFSASNPN ADKAAKLKTG
     AANKPEKISL VINKSNSIEH RRAYNCEIML SKVKTPLNEL MDAVLALDEA EMDLERVDNL
     IKFCPTKEEM EQIKGFKGDK ELLGKCELFF MELMKVPRSE AKLRVFSYKI QFSTQVSDLS
     KSLNYVFLSV EQVRSSVKLR RVMQTILSLG NALNQGTARG SAVGFRLDSI LKLNETRARN
     NKMTLMHYLC KVLADKLPEL LDFSKELGSL EPASKVISIQ LKLLAEEMQS ITKGLEKVIH
     EKKLCKKDGH VSKRFRKSLK KFLSSAESEV KALATQYSGV GKSVDGLILY FGEDPAKCPY
     EQVISTLLSF VRMFNHAHEE NLQQIEAEKK KAQKEAEQEK LKLQNQARKE SEVLRNNNEE
     SEQKESELIR KTPIKNAD
//
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