ID A0A1S3LW50_SALSA Unreviewed; 640 AA.
AC A0A1S3LW50;
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-binding protein 1-like isoform X1 {ECO:0000313|RefSeq:XP_013994814.1};
GN Name=LOC106568736 {ECO:0000313|RefSeq:XP_013994814.1};
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_013994814.1};
RN [1] {ECO:0000313|RefSeq:XP_013994814.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013994814.1};
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_013994814.1; XM_014139339.1.
DR AlphaFoldDB; A0A1S3LW50; -.
DR GeneID; 106568736; -.
DR KEGG; sasa:106568736; -.
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 1..271
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 415..492
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 569..630
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 302..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 422..449
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 346..366
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 640 AA; 73153 MW; 4D6E0568B8EEB702 CRC64;
MESGRATLLK EQQLKDQFDN LEKHTQSGIE FVERYSKFVK ERSEIEISYA KQIRNLSKKY
QPKKNSREEE ENKYTSCRAF LSTLNELNDY AGQHEVIAEN LTSQIITELS RYLTELKAER
KSHFHDGRKA QQQIESSWKQ LESSKRRFER DCKEADRAQQ YFERMDADIN VTKADVEKAR
QQAQMRHQIA ADSKTEYSNY LTKFNQEQNE HYYTLIPNIF QKLQEMEERR IERVGVSMKT
YAEVDREVLP IVGKCLDGMT KAAESIEPKT DSKQVVESYK SGFEPPGDVE FEDYGPGQTI
KRTVSETSLS NSRGEAKERP GGGKSKGKLW PFIKNKNKLM SLLTSPHQPP PAPPASSPPS
PCAVPNDPQS PKQNKEPLSN RFNEFMASKP KMTCLRSLRR GLSLKLGSGP EDFSHLPPEQ
RRKKLQAKID DINKDIQKEM DQKDALTKMK GVYEKNPQMG DPASVDPRLV EMSMNIEKLQ
SEVQKFEGWL AEVEGRLPSR SDPPRRQSGL YESQHSNSTM VDNNCAQDRE SPDGSYTEEQ
SSETQVKVAI ANTPEFDDEF DDGDEETLPT IGTCKAVYSF EGHNEGTISV TEGELLFVIE
QDKGDGWTRV RRNEEEEGYV PTSYVEVFLE TNAKGAMTYI
//
