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Database: UniProt
Entry: A0A3P8SD35_AMPPE
LinkDB: A0A3P8SD35_AMPPE
Original site: A0A3P8SD35_AMPPE 
ID   A0A3P8SD35_AMPPE        Unreviewed;      1349 AA.
AC   A0A3P8SD35;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Formin 1 {ECO:0000313|Ensembl:ENSAPEP00000009995.1};
GN   Name=FMN1 {ECO:0000313|Ensembl:ENSAPEP00000009995.1};
OS   Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000009995.1, ECO:0000313|Proteomes:UP000265080};
RN   [1] {ECO:0000313|Ensembl:ENSAPEP00000009995.1, ECO:0000313|Proteomes:UP000265080}
RP   NUCLEOTIDE SEQUENCE.
RA   Lehmann R.;
RT   "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT   of the orange clownfish Amphiprion percula.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPEP00000009995.1}
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   STRING; 161767.ENSAPEP00000009995; -.
DR   Ensembl; ENSAPET00000010265.1; ENSAPEP00000009995.1; ENSAPEG00000007182.1.
DR   GeneTree; ENSGT00940000154289; -.
DR   OMA; RPKHIDF; -.
DR   Proteomes; UP000265080; Chromosome 11.
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:UP000265080}.
FT   DOMAIN          906..1319
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   REGION          197..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          235..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          281..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          622..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          813..914
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1325..1349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          671..724
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        197..213
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..313
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        813..837
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        838..901
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1325..1343
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1349 AA;  152080 MW;  EBAE191837BF2685 CRC64;
     MESTHTDIHL YRPISERCCM SPLLSLCRGS CFPSKASLSC HQRLTSEHEE EGPAEVMNQS
     QADKFGLKAF KETLQALDDS SEIRWLTELL QLCSECHAFM RMGNQQGTKL NCHSYAESWD
     ALSKSHRIQI PQKRRRRAEG LLYTDNLHRD LKMTPRTPRV PLKARKLTKL QMTGSPSFGK
     WDFEEERPII CTPAARRKRA IGREREDKSA STQEFKSAWK VKLPDASSAS FSKLYSNNGS
     FSPRKDSSVK EDDDPADSDT DISEYDNEMY STFISHTNVE AKSTKTVSQK PEEKNAENVE
     TKPSQQRFEE LGRRTAAQRV MGRIEEVEGI IRRVSLTSAD WIKEHSDRED GPQFVPDRCA
     GEDVSSGALQ QLHVLQQKCQ DELSTQSWLE DQDSDSNKDK QLLLEELRAL GEALSQSLQQ
     ALRMETATKE NEACTEIKKS FCEQSHVTKS PLNPSHFPSA VLNNPLLQSI SADGEVSPTR
     SSSLSAVLDV SSRTSSSLER LSPILSPLLT FNLKVTEQQE ADVPEYHRVW TDSVEDALFS
     LEAGGCESTT TVNGRRENDQ RNTAGLQLKE EHLFSSDEAL QRQEEIWQQE VEESLSLCRS
     LFHPSRPKHI DFLRITALDD DIIDTPTPTP LPRELRSETS TPGEGEERTP GRLQAVWPPL
     KEEKVGLKYT EAEHQAALLQ LKRECKEELE RLQEDYSQEL SRLRVENEDN VARLEITVAE
     LQAKLSQVWT HRPGEVRDVA VSTADDSLHK SFRTVCIQTD RETFVKTPED ACMSPQQQKV
     TPKKLDLTSI SFSLAGQKDD TLYFSSAVPS FQTLPPGDSL PQSEQPPASS TALPTKADTL
     SPPPPPPPPP PPPPCVSPPI NHTQSSNGPP PPPPQPPPPP PSMPGLPPPP PPPPPVGGLI
     VDKPPRKPAV EPSRPMKPLY WTRIQIQDNN KSTLWNVLEE PNIVNTSEFE DLFAKTTTQS
     KRKLLSEAYE KKAKAKKIIK LLDGKRSQAV GILISSLHLE MKDIQQAVLT VDHSVVDLET
     IEALYENRAQ PEELERIQKH YETSEEEEVK LLDKPEQFLY ELSQIPDFSG RACCIIFQSV
     FIDGIASIQS KLNTLSSVCK ALLESDSVRE VMGLVLALGN HMNGGSRTRG QADGYGLEIL
     PKLKDVKSRD NRISLVDYVV SYYLHNVDKN AGTDKSMFPL PEPQDVFLAA QVKFDDLNRD
     LRQLGRDLTK CEKDVQRVCS DSPEEHLQPF QDKMEAFVLS ARKEHTDASY QLMTVQKSFQ
     DLVLYFGLKP KTGEKEVTTG HFFILWFEFC ADFKARWKRE NKNISKERLK EAQLSVKRIT
     GEKKVETRKI NPNSLKERLR QKEASMSST
//
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