ID A0A452E559_CAPHI Unreviewed; 1457 AA.
AC A0A452E559;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=FH2 domain-containing protein {ECO:0000259|PROSITE:PS51444};
GN Name=FMN2 {ECO:0000313|Ensembl:ENSCHIP00000007126.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000007126.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000007126.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000007126.1}
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 EMBL; LWLT01000030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9925.ENSCHIP00000007126; -.
DR Ensembl; ENSCHIT00000014866.1; ENSCHIP00000007126.1; ENSCHIG00000010730.1.
DR GeneTree; ENSGT00940000161899; -.
DR OMA; CNQNAQS; -.
DR Proteomes; UP000291000; Chromosome 28.
DR Bgee; ENSCHIG00000010730; Expressed in prefrontal cortex and 15 other cell types or tissues.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0006974; P:DNA damage response; IEA:Ensembl.
DR GO; GO:0070649; P:formin-nucleated actin cable assembly; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IEA:Ensembl.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR PANTHER; PTHR13037; FORMIN; 1.
DR PANTHER; PTHR13037:SF16; FORMIN-2; 1.
DR Pfam; PF02181; FH2; 1.
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:UP000291000}.
FT DOMAIN 1025..1434
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 587..614
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 161..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..233
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..803
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..983
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1457 AA; 154663 MW; 46E89247060CBF2D CRC64;
MGNQDAKPKR SAGDVPHGGG GGEDAAVPRE AEGTKKAGGG KKAPGRHGKG GGGAEPGRKK
SRSDPRASVF SNLRIRKTLS KGRGTGGSRE DVLDPQALQA GELDSAHSLV TKTPDLSLSA
DETGLSDTEC ADPFEVTRPG GPSLARVGGP AVAEYSETAA GAQDGQRTSS GSDTDLYSFH
SAAEQEDLLS DIQQAIRLQQ LQQQSPGPES PPVSLPSPAP LPGALPGLDR PPPGPSAEAA
LSAPLDRPAA AEPPAATAFA SPGSVPGERG AADTDEEGEE DAFEDAPRDS PGVECGLAAG
EAPRTPGATR EEGAPKPVFP VTASPPRSPA HSPRRPRARP LLAPCYVRTT TRQLSSPGPS
PSPSPSHSPR VQRRPESSLG RGSGATAAPA AAPARKPRAG RSRSADWTAE LGRAPGAGVS
AHLVQRGAGG LQGVFAGENA SICIQRIKGR RTLLEKLFSQ QENGPPEEAE KFCSRIIAMG
LLLPFSDCFR EPCGQNAQSS SVPFDQDRLY TWAAVSQPTH SLDYVEGQFP RRVPAAWPPS
KPPDEEQRPK DADTDSQSAV LETPKKCSDA AQQEVCDMKS EGQATVIQRL EQTIEDLKTK
IAELEKQYPA LDTGLEALKL GEKDVGYERI VQAKSIQTSP MEDGGVLARP PGGAPLVGPL
PLTAHGESAG LPLPLGPQTM FCSEISLVVS PRRISVQLDA QPSLQPPPPA SLPWSDSHGQ
AGSQPSHPLH TGFETSQEHS AFPSSGNGCD IPTAPPLPPE TSPLMPGVGT EASPAPLTPG
APGPALPSPA GLSPPPCLGP EMLPPPPLPL PGVGIPPAPP LPGVGIPPAP PLPGVGIPPA
PPLPGVGIPP APPLPGVGIP PAPPLPGVGI PPAPPLPGVG IPPAPLFPGW GSLPPPLFPG
WGSLPPPLFP GWGSLPPRLF PGWGSLPPRM GIPPTPPLPG VGISPPPPLS SEGIPPAPPP
PPPPPGVGIP PPLTPPPLPT AGSGLPLPRQ VGSSTLPTPQ VCGFLPPPLP LGLFGFGMNQ
EKGSRKQPVE PCRPMKPLYW TRIQLHSRRD SSASLIWEKI EEPSIDCHEF EELFSKSTVK
ERKKPISDTI TKTKAKQVVK LLSNKRSQAV GILMSSLHLD MKDIQHAVVN LDNSVVDLET
LQALYENRAQ SDELEKIEKH GRSSKDKENA KSLDKPEQFL YELSLIPNFS ERVFCILFQS
TFSESICSIR RKLELLQKLC ETLKHGSGVM QVLGLVLAFG NYMNGGNNTR GQADGFGLDI
LPKLKDVKSS DNSRSLLSYI VSYYLRNFDE DAGKEQCVFP LPEPQDLFQA SQMKFEDFQK
DLRKLKKDLR ACEVEAGKVY QVSSKEHIQP FKENMEQFII QGKFCKDAAL PSLFLETTAY
FFMRPKLGEK EVSPNVFFGI WHEFSSDFKD FWKKENKLIL QERVKEAEEV CRQKKGKSLY
KIKPRHDSGI VSIYSVF
//
