ID A0A2K5CA27_AOTNA Unreviewed; 1425 AA.
AC A0A2K5CA27;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Formin 1 {ECO:0000313|Ensembl:ENSANAP00000005566.1};
GN Name=FMN1 {ECO:0000313|Ensembl:ENSANAP00000005566.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000005566.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000005566.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the formin homology family. Cappuccino
CC subfamily. {ECO:0000256|ARBA:ARBA00005271}.
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DR RefSeq; XP_012320819.1; XM_012465396.1.
DR RefSeq; XP_012320826.1; XM_012465403.1.
DR STRING; 37293.ENSANAP00000005566; -.
DR Ensembl; ENSANAT00000023328.1; ENSANAP00000005566.1; ENSANAG00000020833.1.
DR GeneID; 105726103; -.
DR CTD; 342184; -.
DR GeneTree; ENSGT00940000154289; -.
DR OrthoDB; 53873at2759; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0005884; C:actin filament; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR GO; GO:0035136; P:forelimb morphogenesis; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0035137; P:hindlimb morphogenesis; IEA:Ensembl.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:0051127; P:positive regulation of actin nucleation; IEA:Ensembl.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IEA:Ensembl.
DR GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0072092; P:ureteric bud invasion; IEA:Ensembl.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR001265; Formin_Cappuccino_subfam.
DR PANTHER; PTHR13037; FORMIN; 1.
DR PANTHER; PTHR13037:SF11; FORMIN-1; 1.
DR Pfam; PF02181; FH2; 1.
DR PRINTS; PR00828; FORMIN.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51444; FH2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000233020}.
FT DOMAIN 978..1394
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 143..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1395..1425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1269..1333
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 295..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..966
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1395..1419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1425 AA; 158842 MW; 1675B3016CBFD368 CRC64;
MEGTHCTLQL HKPITELCYI SFYLPKGEVR GFSYKGTVTL DRSNKGFHNC YQVREESDII
SLSQEPDEHP GDIFFKQTPT KDILTELYKL TTERERLLAD LLSSDHILGI TMGNQEGKLP
ELSVSLAPED DCFQSAGNWQ GELPVGPLNK RSTHGNKKPR RFGGRRESFG ALPQKRTRRK
GRGCRESAPL MGKDQICSSN SLPLSRTRPN HWLLEERGNL LPNGALDSSL QRRESCPPDI
SRTPDTDLGF GSFETAFKDT GLGREVLPPD CSSTEAGENG FRRLPSGLEH QQTGLSENHQ
DREKHPESEK DKMQKPTKQT CKQKPVSKVV AKVQDLSSQV QRVVKTHSKG KERIAICPEA
QAEFVPKADL LTLLGAEAGA RGSRRRGKER QGNGSLKSPA REAASISSAP ASAKGAVNKV
LLKVIESEKL DEAPEGKRLG FPFHTSVPHT RPETRNKRRA GLPLSGHKSL FLDLPHKVGP
DSSQLRGDDK KSSPPAPAAL GKVFNNSSSQ SSTQKQTLPV PSPLSPRLHS PQQHHRILRL
PALPGEREAA LNDSPGRKSR VFPGCVSADS LEPPSSAKVT ETKGDSPAFL RAGQPRLVPG
ESLEKSLGPG KTTAEPQHQS PPGISSESFP WDGFNEQTLK DLPNRDGGTW VLGYRAGPAC
PFLLHEEREK SNRSELYLDL HPDHSPTEQD DRTPGRLQAV WPPPKTKDTE EKVGLRYTEA
EYQAAILHLK REHKEEIENL QAQFELRTFH IRGEHAVITA RLEETIENLK HELEHRWRGG
CEERKDACIS TDDDCPPKTY RNVCIQTDRE TFLKPSEGES KTTRSNQLVP KKLNISSLSQ
LSPTNDHKDI HAALQPMEGT ESNQQKAPPP PPAPPLPAFI PPPPPLPPGL GSLSPAPPMP
PVSAGPPPPP PPPPPPPPLP PPSSVGPPPP PPPPPLPNFP APPNPGGPPP APTPPGLAPP
PPPGLFFGLG SSSSQCPRKP AIEPSCPMKP LYWTRIQISD RSQNAAPTLW DSLEEPDIRD
PGEFEYLFSK DTTQQKKKPL SETYEKKNKV KKIIKLLDGK RSQTVGILIS SLHLEMKDIQ
QAIFNVDDSV VDLETLAALY ENRAQEDELV KIRKYYETSK EEELKLLDKP EQFLHELAQI
PNFAERAQCI IFRSIFSEGI TSLHRKVEII TRASKGLLHM KSVKDILALI LAFGNYMNGG
NRTRGQADGY SLEILPKLKD VKSRDNGINL VDYVVKYYLR YYDQEAGTEK SVFPLPEPQD
FFLASQVKFE DLIKDLRKLK RQLEASEKQM VVVCKESPKE YLQPFKDKLE EFFQKAKKEH
KMEESHLENA QKSFETTVGY FGMKPKSGEK EITPSYVFMV WYEFCSDFKT IWKRESKNIS
KERLKMAQES VSKLTSEKKV ETKKINPTAS LKERLRQKEA SVNTN
//
