ID A0A3Q0D2J5_MESAU Unreviewed; 1329 AA.
AC A0A3Q0D2J5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Formin-1 isoform X2 {ECO:0000313|RefSeq:XP_021086754.1};
GN Name=Fmn1 {ECO:0000313|RefSeq:XP_021086754.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021086754.1};
RN [1] {ECO:0000313|RefSeq:XP_021086754.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_021086754.1; XM_021231095.1.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005884; C:actin filament; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0045010; P:actin nucleation; IEA:InterPro.
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:UP000189706}.
FT DOMAIN 882..1298
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 144..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1309..1329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1173..1237
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 189..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..870
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1329 AA; 148366 MW; FD0F8A124A8E193C CRC64;
MEGTHCTLQL HNPITELCYI SFYLPKGEVR GFSYKGTVTL DRSNNAFHNC YQVREGPDIT
SLSQQPNEHP GDIFFKQTPT KDILTELYKL TAERERLLDS LLRSDHILGI SMGNQEGKLQ
ELSVSLAPED DCFQSAGSWS RELPVNSLIR RSTQGNKKPR RSGRRRESPE EHRQKKTRRK
GRGRQESSAP QMGKDQVCSS SSLPPARVRP NLRLLEERGN LVPQGTLTSS PRRRRESCPA
NILRTPDADL GFGSSGRTSE DTDLEGPLSP NGSPTEVGDA RIGRQFKSPR DWESPSLSES
HEKHSGAERV GTRKSKSLER TCRKKPVSKV VAKVQELSAQ VQRVVRTHPD DVGKVTFCSE
MQTEFIPKAD FFILPGAKDE TPSSRRLGEE QRGVKSLQPQ TTEIASIPNE PASTAGAVNK
VLRKVIDSEK LDEATEGKTL GFSLNTRATH TFSQTRSQRK AGLPQSDHKF LLLDLPHTVR
PDSPQPKCDE RKPTPQTPTA LGLVFNNSSP QSSARKRLSP VLLPLSPMCP SPQQHHRILP
LPPLPSEGES VFDECPSRKN SVSSGSPSAV TLEPSSFEKV TETKGGSPTS LRASHTWLVS
EEPSEKSLRP EKITAPPQHQ PPPEYQAAIL HLKREHKEEI ENLQAQFELK TFHMRGEHAL
ITARLEETIE NLKQQLDHRW GGGREEMRDA CISTDDDGPP KAFRNVCIQT DRETFLKTCE
SENKTARSNQ IVPKKLNISL TQLSPTKDSK DIHAPLQTVE GISSSQQKIS PPPPTPSLPP
PPIPPPPPLP TGLGPLPPAP PMSPMSAGPP PPPPPPPPPP PLPPSAGPPP PPPPPPLPSA
LALPNSGGLP PPPLPPPPPG LAPPPPPGLS FGLSSSSSQC PRKPAIEPSC PMKPLYWTRI
QINDKSQDAT PTLWDSLEEP HIRDTSEFEY LFSKDTTQQK KKPLSETYEK KSKVKKIIKL
LDGKRSQTVG ILISSLHLEM KDIQQAIFNV DDSVVDLETL AALYENRAQE DELTKIRKYY
ETSKEEDVKL LDKPEQFLHE LAQIPNFAER AQCIIFRAVF SEGVTSLHRK VEIVTRASKG
LLHMKSVKDI LALILAFGNY MNGGNRTRGQ ADGYSLEILP KLKDVKSRDN GMNLVDYVVK
YYLRYYDQEA GTDKSVFPLP EPQDFFLASQ VKFEDLIKDL RKLKRQLEAS EQQMKLVCKE
SPKEYLQPFK DKLEDFFQKA KKEHKMEESH LENAQKSFET TVGYFGMKPK TGEKEITPSY
VFMVWFEFCS DFKTIWKRES KNISKERLKM AQASVSKLTS EKKVETKKIN PTASLKERLR
QKEASVATS
//