ID A0A3Q0F6L3_VIGRR Unreviewed; 1039 AA.
AC A0A3Q0F6L3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Formin-like protein 13 isoform X6 {ECO:0000313|RefSeq:XP_022639562.1, ECO:0000313|RefSeq:XP_022639563.1};
GN Name=LOC106766484 {ECO:0000313|RefSeq:XP_022639562.1,
GN ECO:0000313|RefSeq:XP_022639563.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_022639563.1};
RN [1] {ECO:0000313|RefSeq:XP_022639562.1, ECO:0000313|RefSeq:XP_022639563.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_022639562.1,
RC ECO:0000313|RefSeq:XP_022639563.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the formin-like family. Class-II subfamily.
CC {ECO:0000256|ARBA:ARBA00006468}.
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 RefSeq; XP_022639562.1; XM_022783841.1.
DR RefSeq; XP_022639563.1; XM_022783842.1.
DR Proteomes; UP000087766; Chromosome 7.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1110; -; 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:SF20; FORMIN-LIKE PROTEIN 13; 1.
DR Pfam; PF02181; FH2; 1.
DR Pfam; PF10409; PTEN_C2; 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:UP000087766}.
FT DOMAIN 199..337
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 816..1039
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 393..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..637
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..783
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1039 AA; 114659 MW; A5789C51E6304988 CRC64;
MLRKLFFRKP PDGLLEICER VHVFDCCFTT DAWKEGNYNY KEYMDGIVGQ LKENSLDASI
LIFNFREEGT VSQMASIMSE HDITIMDYPL HYQGVPVLKM ELIHHFLRSS ESWLSLGQNN
VLLMHCEPGG WPVLAFMLAA LLIYRKAYTG EQRTLDIVYR QAPHELLHLL SPLNPIPSQL
RYLLYVSRRN VALDWPPLDR ALMLDCIILR LFPNFDSEGG CHPVFRIYGQ DPFDADKVHK
MLYSTPKRSK KVGAFKQGEC ELIKIDINCH IQGDVVIETI NFNGDMERER MMFRIMFNTA
FVRSNILMLN RDEIDILWDA KDHFPNDFRV EILFSEMDAA IVVADRASCF EEKDGLPMEA
FAKVQEIFSQ VDWMNPKADV ALNALQLISD STMNDSLDEK DPRTPQGNLN EEVRSSFSIK
TSPVTDMSRK EDNTNKFEGI PQQPGTPNNI CQESTRSSKR TSESNTCPTR PTNLDIKQQA
PHLAVSSTDT SFSPRTPPLR PQSTSAKEAH DSPRQTESPP SYYVVPLQSK HQSQDRSHSS
ISIPTPDTQL SSTFHSKSLA DTISCPSAST ITSTQSSPSL SSKNVDEIPP IKTRIESSPS
RPPTPPPPPT PPLNDHRRVR AAPPPPPPPP PIPPKKELHV KAGPHPSPLS HMNVEPQVRD
GPSPPLSLKE EQPTRFKPPC LSGQAAGFTI VPTPPPPPLS SEVLYSNCTN SSLQKSLAPS
PPPPPGAPAP PPPPGAPAPS SPPGAPAPPP PPGAPAPPPP PGAPAPPPPP GAPAAPPPPM
PFGKGGLKSG SPFPGSHSVN ARSSSPTNLK GVLSRTINSK NNTKRLKPLH WLKLSRAVQG
SLWAETPKSG EASKAPEIDM SELENLFSAA VPTSGIAKKS NVQSSAGPKS EKVQLIEHRR
AYNCEIMLSQ VKVPLHDLMT SVLTLEESAL DSDQVENLIK FCPTKEEMEL LKGYNGEREK
LGRCEQFLME LMKVPRVESK LRVFSFKIQF RSQVSDLRKS LVIVNAASEE IRNSVKLKRI
MHTILSLGNA LNQGTARGN
//