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Database: UniProt
Entry: A0A3Q0D2J5_MESAU
LinkDB: A0A3Q0D2J5_MESAU
Original site: A0A3Q0D2J5_MESAU 
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}.
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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
//
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