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Database: UniProt
Entry: A0A1S3S5L8_SALSA
LinkDB: A0A1S3S5L8_SALSA
Original site: A0A1S3S5L8_SALSA 
ID   A0A1S3S5L8_SALSA        Unreviewed;      1093 AA.
AC   A0A1S3S5L8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Formin-like protein 1 {ECO:0000313|RefSeq:XP_014059635.1};
GN   Name=LOC106607317 {ECO:0000313|RefSeq:XP_014059635.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014059635.1};
RN   [1] {ECO:0000313|RefSeq:XP_014059635.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014059635.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the formin homology family.
CC       {ECO:0000256|ARBA:ARBA00023449}.
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DR   RefSeq; XP_014059635.1; XM_014204160.1.
DR   AlphaFoldDB; A0A1S3S5L8; -.
DR   STRING; 8030.ENSSSAP00000012910; -.
DR   PaxDb; 8030-ENSSSAP00000012910; -.
DR   GeneID; 106607317; -.
DR   KEGG; sasa:106607317; -.
DR   OrthoDB; 471257at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa06.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0022604; P:regulation of cell morphogenesis; IEA:InterPro.
DR   Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR014767; DAD_dom.
DR   InterPro; IPR015425; FH2_Formin.
DR   InterPro; IPR042201; FH2_Formin_sf.
DR   InterPro; IPR010472; FH3_dom.
DR   InterPro; IPR043592; FMNL_animal.
DR   InterPro; IPR014768; GBD/FH3_dom.
DR   InterPro; IPR010473; GTPase-bd.
DR   PANTHER; PTHR45857; FORMIN-LIKE PROTEIN; 1.
DR   PANTHER; PTHR45857:SF2; FORMIN-LIKE PROTEIN 1; 1.
DR   Pfam; PF06367; Drf_FH3; 1.
DR   Pfam; PF06371; Drf_GBD; 2.
DR   Pfam; PF02181; FH2; 1.
DR   SMART; SM01139; Drf_FH3; 1.
DR   SMART; SM01140; Drf_GBD; 1.
DR   SMART; SM00498; FH2; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR   PROSITE; PS51231; DAD; 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT   DOMAIN          43..478
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          639..1030
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   DOMAIN          1060..1093
FT                   /note="DAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51231"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          175..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          543..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1011..1093
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          414..459
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        471..499
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..630
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1011..1041
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1049..1070
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1093 AA;  121596 MW;  28308BFCBA837425 CRC64;
     MGNAAGGIEQ ADGREAKHSV GSGTGLSDPT PTLQKKQPAP PKLPVPPEEE LEERFSVVLS
     YMNLPPDKLN LLSQYDNEKK WELICDQERF QVKNPPSTYL TKIKSFYQDQ GGVTRRFKRR
     VQESTQVLRE LEISLRTNHI GWAQEFLNEE NQGLDVLVDY LSYAQCDASF DLEGAENGGT
     LSERGKPAER SMEDLNKSAG SSPTHGMTRA ARALTVRITS LAQSRKTQKI SRLASQRDDV
     HVCIMCLRAI MNYQSGFNQV MTHPRCVNEI TLSLNNKNPR TKALVLELLA AVCLVRGGHD
     IILAAFDNLK EVSGEKNRFE KLMEYFSNDD SNIDFMVACM QFINIVVHSV ENMNFRVHLQ
     YEFTHHGLDQ YLESLKLTES EKLQVQIQAY LDNVFDVGAL LEDAENRGGV LEHVDELQEH
     NSQLSARLEE IESQSAERMA ELEKQLLQAT KETELLKESL RDSCSQVSSL QQREREREMS
     QERERDRERL SQPSSELELK VQELQDRGLI RLGRTPSGAL DLQVVPVTII EYAPAPASEC
     LLSSTGPTAP GPEVPDATPS SAISAVPPPP PPPPPPPGPG GRAPPPPPPS PCGSGGPPPP
     PPPPPPGGGP PPPPPPPGGG PPPPPGGPPS GDSQAGGKSR KPIQTKFRMP LLNWQALKPN
     QVTGTVFHEL DDEQVLGELN MDAFEEQFKT KAQGPPAALS TLKVKVAQKA PSKVNLIEGN
     KAKNLAITLR KGGRSPTDIC TAIETYDQQA LGLDFLELLE RFVPSDYELK LLQNYEKEGR
     PLDDLAEEDR FMMRFGKIPR LAQRISTLTF MGNFPESVKR LQPQLNSIIT ASMSIKSSAK
     LKKMLEIILA FGNYMNSSKR GAAYGFRLQS LDLLLDTKST DRSQTLLHFI SSIVQEKYPE
     LNNFHTELHF VDKAGLVSLD SILQDIRSLE RGMEVTKKEF LVQEDNTVLK DFVKTNSELL
     DSLLKDSKTA QEAYGSVVEY FGENPKTTQP SMFFPLFVRF MKAYKQAEKD NEQRMRLEAK
     SSENQAESPS PRKKEAAGHK SPMMPKMDLI AELKKRQVKP QVKDGALEDI ITDLRNSPFR
     ATDGRRPAQR QDT
//
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