ID A0A2K6FDG7_PROCO Unreviewed; 1020 AA.
AC A0A2K6FDG7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Formin like 3 {ECO:0000313|Ensembl:ENSPCOP00000012014.1};
GN Name=FMNL3 {ECO:0000313|Ensembl:ENSPCOP00000012014.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000012014.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000012014.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the formin homology family.
CC {ECO:0000256|ARBA:ARBA00023449}.
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DR AlphaFoldDB; A0A2K6FDG7; -.
DR Ensembl; ENSPCOT00000022606.1; ENSPCOP00000012014.1; ENSPCOG00000017512.1.
DR GeneTree; ENSGT00940000159962; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IEA:InterPro.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR043592; FMNL_animal.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR PANTHER; PTHR45857; FORMIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR45857:SF3; FORMIN-LIKE PROTEIN 3; 1.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00022707};
KW Myristate {ECO:0000256|ARBA:ARBA00022707};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160}.
FT DOMAIN 26..464
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 553..943
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 383..456
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 917..946
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 504..534
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1020 AA; 116314 MW; 3E2E5DC0689B6AA9 CRC64;
MGNLESAEGG PGEPPSVPLL LPPGKMPMPE PCELEERFAL VLSSMNLPPD KARLLRQYDN
EKKWDLICDQ ERFQVKNPPH TYIQKLQSFL DPSVTRKKFR RRVQESTKVL RELEISLRTN
HIGWVREFLN DENKGLDVLV DYLSFAQCSV MFDFEGLESG DDGAFDKLRS WSRSIEDLQP
PSALSAPFTN SLARSARQSV LRYSTLPGRR ALKNSRLVSQ KDDVHVCILW LAGRSLLHHQ
GPLLLSFPFL NNKNPRTKAL VLELLAAVCL VRGGHEIILA AFDNFKEVCK ELHRFEKLME
YFRNEDSNID FMVACMQFIN IVVHSVEDMN FRVHLQYEFT KLGLEEFLQK SRHTESEKLQ
VQIQAYLDNV FDVGGLLEDA ETKNVALEKV EELEEHVSHL TEKLLDLENE NMMRVAELEK
QLLQREKELE SIKETYENTN HQVHTLRRLI KEKEEAFQRR CRLEPSARGL ESMGSEALAR
VGPTELSEGM PPSDLDILAP DPTPEEVLPL PPPPAPPLPP PPPPLPDKCP PAPPLPGTAP
SVVLTVGLSA IRIKKPIKTK FRLPVFNWTA LKPNQISGTV FSELDDEKIL EDLDLDKFEE
LFKTKAQGPA LDLICSKNKT AQKAASKVTL LEANRAKNLA ITLRKAGRSA EEICRAIHTF
DLQTLPVDFV ECLMRFLPTE AEVKLLRQYE RERQPLEELA AEDRFMLLFS KVERLTQRMA
GMAFLGNFQD NLQMLTPQLN AIIAASASVK SSQKLKQMLE IILALGNYMN SSKRGAVYGF
KLQSLDLLLD TKSTDRKMTL LHFIALTVKE KYPDLANFWH ELHFVEKAAA VSLENVLLDV
KELGRGMELI RRECSIHDNS VLRSFLSTNE GKLDKLQRDA KTAEEAYNAV VRYFGESPKT
TPPSVFFPVF VRFIRSYKEA EQENEARKKQ EEVMREKQLA QEAKKLDAKT PSQRNKWQQQ
ELIAELRRRQ AKEHRPVYEG KDGTIEDIIT VLKSVPFTAR TAKRGSRFFC DAAHHDESNC
//