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Database: UniProt
Entry: A0A1S3LW59_SALSA
LinkDB: A0A1S3LW59_SALSA
Original site: A0A1S3LW59_SALSA 
ID   A0A1S3LW59_SALSA        Unreviewed;       639 AA.
AC   A0A1S3LW59;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Formin-binding protein 1-like isoform X2 {ECO:0000313|RefSeq:XP_013994824.1};
GN   Name=LOC106568736 {ECO:0000313|RefSeq:XP_013994824.1};
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_013994824.1};
RN   [1] {ECO:0000313|RefSeq:XP_013994824.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_013994824.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC       {ECO:0000256|ARBA:ARBA00004544}.
CC   -!- SIMILARITY: Belongs to the FNBP1 family.
CC       {ECO:0000256|ARBA:ARBA00009426}.
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DR   RefSeq; XP_013994824.1; XM_014139349.1.
DR   AlphaFoldDB; A0A1S3LW59; -.
DR   STRING; 8030.ENSSSAP00000114176; -.
DR   PaxDb; 8030-ENSSSAP00000114176; -.
DR   OrthoDB; 2995634at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa01.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 6.10.140.470; -; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR031160; F_BAR.
DR   InterPro; IPR001060; FCH_dom.
DR   InterPro; IPR011072; HR1_rho-bd.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR   PANTHER; PTHR15735:SF13; FORMIN-BINDING PROTEIN 1; 1.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS51860; REM_1; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077, ECO:0000256|SAM:Coils};
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          2..270
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          414..491
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          568..629
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          301..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          341..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          421..448
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        345..365
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..544
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   639 AA;  73187 MW;  99C6B428119A8760 CRC64;
     MMEERMGNCW SYTKDQFDNL EKHTQSGIEF VERYSKFVKE RSEIEISYAK QIRNLSKKYQ
     PKKNSREEEE NKYTSCRAFL STLNELNDYA GQHEVIAENL TSQIITELSR YLTELKAERK
     SHFHDGRKAQ QQIESSWKQL ESSKRRFERD CKEADRAQQY FERMDADINV TKADVEKARQ
     QAQMRHQIAA DSKTEYSNYL TKFNQEQNEH YYTLIPNIFQ KLQEMEERRI ERVGVSMKTY
     AEVDREVLPI VGKCLDGMTK AAESIEPKTD SKQVVESYKS GFEPPGDVEF EDYGPGQTIK
     RTVSETSLSN SRGEAKERPG GGKSKGKLWP FIKNKNKLMS LLTSPHQPPP APPASSPPSP
     CAVPNDPQSP KQNKEPLSNR FNEFMASKPK MTCLRSLRRG LSLKLGSGPE DFSHLPPEQR
     RKKLQAKIDD INKDIQKEMD QKDALTKMKG VYEKNPQMGD PASVDPRLVE MSMNIEKLQS
     EVQKFEGWLA EVEGRLPSRS DPPRRQSGLY ESQHSNSTMV DNNCAQDRES PDGSYTEEQS
     SETQVKVAIA NTPEFDDEFD DGDEETLPTI GTCKAVYSFE GHNEGTISVT EGELLFVIEQ
     DKGDGWTRVR RNEEEEGYVP TSYVEVFLET NAKGAMTYI
//
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