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Database: UniProt
Entry: A0A2K6DRP2_MACNE
LinkDB: A0A2K6DRP2_MACNE
Original site: A0A2K6DRP2_MACNE 
ID   A0A2K6DRP2_MACNE        Unreviewed;      1068 AA.
AC   A0A2K6DRP2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Formin like 2 {ECO:0000313|Ensembl:ENSMNEP00000038593.1};
GN   Name=FMNL2 {ECO:0000313|Ensembl:ENSMNEP00000038593.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000038593.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000038593.1}
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; A0A2K6DRP2; -.
DR   Ensembl; ENSMNET00000063074.1; ENSMNEP00000038593.1; ENSMNEG00000042052.1.
DR   GeneTree; ENSGT00940000155515; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000042052; Expressed in cerebellum and 12 other cell types or tissues.
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; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR014767; DAD_dom.
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:SF5; FORMIN-LIKE PROTEIN 2; 1.
DR   Pfam; PF06367; Drf_FH3; 1.
DR   Pfam; PF06371; Drf_GBD; 2.
DR   Pfam; PF02181; FH2; 1.
DR   PRINTS; PR00049; WILMSTUMOUR.
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; PS51231; DAD; 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:UP000233120}.
FT   DOMAIN          1..441
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          592..983
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   DOMAIN          1015..1054
FT                   /note="DAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51231"
FT   REGION          485..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          353..450
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          957..988
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        494..509
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        518..571
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1068 AA;  121495 MW;  71E5EDBCA0ED2275 CRC64;
     APLKELPIWK PNAMNLPPDK ARLLRQYDNE KKWELICDQE RFQVKNPPHT YIQKLKGYLD
     PAVTRKKFRR RVQESTQVLR ELEISLRTNH IGWVREFLNE ENKGLDVLVE YLSFAQYAVT
     FDFESVESTV ESSVDKSKPW SRSIEDLHRG SNLPSPVGNS VSRSGRHSAL RYNTLPSRRT
     LKNSRLVSKK DDVHVCIMCL RAIMNYQYGF NMVMSHPHAV NEIALSLNNK NPRTKALVLE
     LLAAVCLVRG GHEIILSAFD NFKEVCGEKQ RFEKLMEHFR NEDNNIDFMV ASMQFINIVV
     HSVEDMNFRV HLQYEFTKLG LDEYLDKLKH TESDKLQVQI QAYLDNVFDV GALLEDAETK
     NAALERVEEL EENISHLSEK LQDTENEAMS KIVELEKQLM QRNKELDVVR EIYKDANTQV
     HTLRKMVKEK EEAIQRQSTL EKKIHELEKQ GTIKIQKKGD GDIAILPVVA SGTLSMGSEV
     VAGNSVGPTT GAASSGPLPP PPPPLPLSSD TPETVQNGPV TPPMPPPPPP PPPPPPPPPP
     PPPPPPPLPG PVAETVPAPP LAPPLPSAPP LPGTSSPTVV FNSGLAGKTV KIKKPIKTKF
     RMPVFNWVAL KPNQINGTVF NEIDDERILE DLNVDEFEEI FKTKAQGPAI DLSSSKQKIP
     QKGSNKVTLL EANRAKNLAI TLRKAGKTAD EICKAIHVFD LKTLPVDFVE CLMRFLPTEN
     EVKVLRLYER ERKPLENLSD EDRFMMQFSK IERLMQKMTI MAFIGNFAES IQMLTPQLHA
     IIAASVSIKS SQKLKKILEI ILALGNYMNS SKRGAVYGFK LQSLDLLLDT KSTDRKQTLL
     HYISNVVKEK YHQVSLFYNE LHYVEKAAAV SLENVLLDVK ELQRGMDLTK REYTMHDHNT
     LLKEFILNNE GKLKKLQDDA KIAQDAFDDV VKYFGENPKT TPPSVFFPVF VRFVKAYKQA
     EEENELRKKQ EQALMEKLLE QEALMEQQDP KSPSHKSKRQ QQELIAELRR RQVKDNRHVY
     EGKDGAIEDI ITDLRNQPYR RADAVRRSVR RRFDDQNLRS VNGAEITM
//
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