ID A0A3Q0F3X8_VIGRR Unreviewed; 1298 AA.
AC A0A3Q0F3X8;
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 18 isoform X5 {ECO:0000313|RefSeq:XP_022638196.1};
GN Name=LOC106765231 {ECO:0000313|RefSeq:XP_022638196.1};
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_022638196.1};
RN [1] {ECO:0000313|RefSeq:XP_022638196.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_022638196.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the formin-like family. Class-II subfamily.
CC {ECO:0000256|ARBA:ARBA00006468}.
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DR RefSeq; XP_022638196.1; XM_022782475.1.
DR Proteomes; UP000087766; Chromosome 6.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1110; -; 2.
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:SF8; FORMIN-J; 1.
DR Pfam; PF02181; FH2; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
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.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000087766};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 264..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 199..385
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT REGION 521..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..956
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1030
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1073
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1119
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1298 AA; 141763 MW; 39E635BE4ABDF05F CRC64;
MALFRKFFYK KPPDGLLEIT ERVYVFDYCF TTDVMEEEEY RVYLGGIIGQ LRGHFPDASF
MVFNMREGDC QSQISNILCD YDMTVIDYPR QYEGCPLLTM EMIHHFLRSG ENWLELGHHN
VVLMHCERGG WPLLAFMLAA LLIYRKMFTG EQKTLDMIYK QAPRELLQLM SPLNPLPSQL
RYLQYISRRN VGSEWPPLDR ALTLDCVIIR LIPNMGGEGG CRPIFRIYGQ DPFIPADRTP
KVLFSTPKRS KLVRYCRQVV PKSFYPNLIC FLTPFILFLL PILRCSFHYM FLLPEMFFLF
SYLFQSDCEL VKIDIHCHVQ GDVVFECIHL HSDLEHEEMM FRVMFNTAFI RSNILMLNRD
EIDILWNAKD CFPKNFRVEV LFSDMDASTS VISIDLPHVE EKDGLPVEAF AKVKEIFSNV
DWLDSKEEVA SVLQQITSSN ILLERFESGV SAATSDLQKE SSEKSTAVLK AHSDTNIQAS
AVQGKHSTSS LGSSLDFAMG NKTEPLESKT LSKNDIETLE CSGQGNQPIH SFGLSKDSDS
TKRGTESSES KEKDIESLAS TDADSLAKKT DLLGSKEKTF ESLNSEAFLE NDSRFKCEPR
PLAEIDNSSG SAPMEKNNDP LELKVSPENT LKTSASTSQG KRLTPSFGLI SDSSSPKKPV
ESLDNAKVPT SMPLVAKSMP SIEPYKDAYS MTQDMGPLET KSLTDGNSIK EKMGQLEQIV
LSENDTKSVT STAQGKQYSP LLEQPVEAST IKTKIEPHEL QVSLQLPTQS KIISSPVRPA
VRSASASTSY FNSLKGSPVA ISRYRSAPSA LGITSVLQDH AAVDIKEVTH AVTVSPPASV
LPPSDSKVLN SVEPSPAAVP PASSSPLHPS LPLKTSVDAL KTTEKTFESL SPAVVTTSPP
PPPPSSQCDH TSNLMQSNAT QYPENTNEGK KPLVGPPPPP PSPSMLAPPT PSFSPAPSLP
ETSVSTTQGS CKGPPAPPPP PALSGFPSSL GINESVAIPG PPPPPPPPPP SLSSSAPPLA
PPPPPPPSAS AFQNSLSENS KNGPPVPPPP PPSLPGSTLS PSAPPPPPPP GSASQNSLSS
STNVPPVPPP PLSANGLSKP GVPGPPSVPG PPSAPGPPSA PFDAKGRGLM RANAKFQSKR
SNLKPYHWLK LTRAMQGSLW AETQKLDEFC RAPEFDMSEL ETLFSAASPA ASDGKGGKSN
RRASGQKVEK VQLIELRRAY NCEIMLTKVK IPLPDLMWFS WPVLQKPMQC DHCLSCTTVY
RCCGLHGGPL STWLMPQVAS LLLLRRFFLE YGCPYVGI
//
