GenomeNet

Database: UniProt
Entry: A0A3Q0F6L3_VIGRR
LinkDB: A0A3Q0F6L3_VIGRR
Original site: A0A3Q0F6L3_VIGRR 
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
//
DBGET integrated database retrieval system