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Database: UniProt
Entry: A0A1S3PBP7_SALSA
LinkDB: A0A1S3PBP7_SALSA
Original site: A0A1S3PBP7_SALSA 
ID   A0A1S3PBP7_SALSA        Unreviewed;       615 AA.
AC   A0A1S3PBP7;
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 X4 {ECO:0000313|RefSeq:XP_014024997.1};
GN   Name=LOC106584338 {ECO:0000313|RefSeq:XP_014024997.1};
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_014024997.1};
RN   [1] {ECO:0000313|RefSeq:XP_014024997.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014024997.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC       {ECO:0000256|ARBA:ARBA00004544}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the FNBP1 family.
CC       {ECO:0000256|ARBA:ARBA00009426}.
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DR   RefSeq; XP_014024997.1; XM_014169522.1.
DR   AlphaFoldDB; A0A1S3PBP7; -.
DR   STRING; 8030.ENSSSAP00000118674; -.
DR   PaxDb; 8030-ENSSSAP00000118674; -.
DR   OrthoDB; 2995634at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa23.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd11628; HR1_CIP4_FNBP1L; 1.
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:SF14; FORMIN-BINDING PROTEIN 1-LIKE; 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|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW   ProRule:PRU01077}; Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
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..262
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          398..475
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          544..605
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          278..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          326..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          405..439
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        285..303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..532
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   615 AA;  70913 MW;  AB24AFE6F8AFCBC0 CRC64;
     MTWGTELWDQ FENLDKHTQW GIDFLERYAK FVKERLEIEQ TYAKQLRNLV KKYCPKRSKD
     DEPRFSSCLS FYSILNELND YAGQREVVAE EMGHNVYGEL MRYSQDLKSE RKHHLQEGRK
     AQQYLDQCWK HMDNSKKKFE RECKEAEKSQ ISYDRLDNDI NATKSEVEKA KSQLYLRTHS
     ADESKNEYAA QLQNFNGEQW KHFNVAIPQI FKNLQDMDER RTVKLGETYR SFADVERRVV
     PIISKCLEGM VTAAKAVDQR KDSAIVVESF KSGFEPPGDF PFEDYSQNLS RTGSDNTIST
     PKNEGVVKPD PKHSISKAAK NKLWLFGKKP KSPPSSPPPA PHRPDLATGS HCQSPKFASD
     PIAFCLSEMR TVKPRIASFR GLKRGWSVKA PSLEDFSHLP PEQRRKRLQA RIDELSKELQ
     KEVDQRDALN KMKDVYEKNP QMGDPQSLQP KISETMCNME KLRSEIHKNE SWLSEVEGKV
     STRGDRRPSA DVNHHTPHGR ESPEGSYTDD PSQEHRSPPH QPDPRQAHQP DEFDDEFDDD
     DPLPVLGHCK ALYSFDGQNE GTLLMKEDDV LFIIEEDKGD GWTRARKQSG EEGYVPTSYV
     EITMEKNSKG AVTYI
//
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