ID A0A1S3BCS6_CUCME Unreviewed; 1293 AA.
AC A0A1S3BCS6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Formin-like protein {ECO:0000256|RuleBase:RU361260};
GN Name=LOC103488255 {ECO:0000313|RefSeq:XP_008445164.1};
GN Synonyms=103488255 {ECO:0000313|EnsemblPlants:MELO3C002002.2.1};
OS Cucumis melo (Muskmelon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_008445164.1};
RN [1] {ECO:0000313|Proteomes:UP000089565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT "The genome of melon (Cucumis melo L.).";
RL Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN [2] {ECO:0000313|EnsemblPlants:MELO3C002002.2.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2023) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_008445164.1}
RP IDENTIFICATION.
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_008445164.1; XM_008446942.2.
DR EnsemblPlants; MELO3C002002.2.1; MELO3C002002.2.1; MELO3C002002.2.
DR GeneID; 103488255; -.
DR Gramene; MELO3C002002.2.1; MELO3C002002.2.1; MELO3C002002.2.
DR KEGG; cmo:103488255; -.
DR eggNOG; KOG1922; Eukaryota.
DR InParanoid; A0A1S3BCS6; -.
DR OrthoDB; 396031at2759; -.
DR Proteomes; UP000089565; Unplaced.
DR Proteomes; UP000596662; Unplaced.
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:SF10; FORMIN-LIKE PROTEIN 15A-RELATED; 1.
DR Pfam; PF02181; FH2; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000089565}.
FT DOMAIN 200..339
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 897..1293
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 642..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..740
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..782
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..810
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..852
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1293 AA; 144624 MW; F8FFE844C3F8D3E3 CRC64;
MALFRKLFYR KPPDRLLEIA ERVYVFDCCF SNEVLEEDEY KVYLASIIPK LQDHFPDASF
MVFNFSERKR KTKTSDILSQ YGMTVMEYPL QYEGCSLLPL EMIHHFIRSS ESWLSLERQK
NVLLMNCERG GWPILAFMLS AILLYRKQYE GEQKTLEMVY RQAPRELFQV LSPVNSQPSQ
MRYLQYISRR NLGSDWPPPD APLILDCLIL RELPMLNGGK GWRPIIRIYG QDPLTPRNRS
PKLVFSSAKM EGHGRQYLQV ASRLVKVDVH CHVQGDVVLE CIRLGGDLIH AEVMFRFMFH
TAFVDSNSLK LNRDEVDVLW DARDQFPKDF RAEVLFRDAD HVVPNHSTTA RSDDKIENES
NSTEEFFEVE EIFSNIIDVQ EVKKDYDVQM VHTNETDYID HQAVWEDADP PTFQRCKSLG
GSQNFDKKMD FNVEAVKDIT VDDITFKTGE KVDSGLQAVK DIVVDYGDKK PNPLLFSVNV
LRRMAIKELI DDAYDKLEGV QHKGYGEDTA IAHSESKLPL KKLEADAWRV EYEKLQSASR
KQPSSTVKLM NHTIVAKQKT KQPEDQNFLV KQAKLNTLSR WTSHDKESCP NSMHLFYPSS
RQTLASPTSI SSHTKDSYSY STAKSASASA TSGLLLSDAV DEQKSNNATP KKPLSSATEI
LTSRPQSPLD SPRPLPNTVL HQELPSPTTL LQPPALQANA SFFQASSPKS SLSPSSYFHK
NARPPPPAPP PPPPPPSNHV APKSSLLLCG NKPKQNAPPA PPPPPVRRAH QQLPPPRPLP
SHGALLSPRL SDAGALPPPP PPPPPIQRTA PPHLTQGQQA LTATACVVSS SLPSPICEAP
SPPQPTTGPL PKVPSSSQPS GGVSPHLEAK GVSSSTDLKT APIVRGRGFL RSMGMGVATT
GPQRSSLKPL HWSKVTRVLQ GSLWEELQRC GESESVPEFD VSELETLFSV IVPKPMADSG
GKSGGRRKSV GSKLDKVHLI DIRRANNTEI MLTKVRMPLS DMMAAVLSMD ESVLDVDQVE
NLIKFCPTKE EMELLKGYSG DKDKLGKCEQ YFLEMMQVPR VESKLRVFSF KIHFSSQIVE
FKKSLNTVNS VCQEVKNSRK LKEILKKILC LGNMLNQGTA RGSAIGFRLD SLSKLTDTRA
SNNKLTLMHY LCKVLASKSP SLLDFHLDLG SLEAASKIQL KSLAEEMQAI TKGLEKVKQE
LIASESDGPI SENFHKILEG FVTLAEREVE SVTVLYSVAG RNADALALYF GEDPSRCPFE
QVTGTLFHFT RSFLKAHEEN CKQLEMEMRK LRK
//
