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Database: UniProt
Entry: A0A3P8ZEW1_ESOLU
LinkDB: A0A3P8ZEW1_ESOLU
Original site: A0A3P8ZEW1_ESOLU 
ID   A0A3P8ZEW1_ESOLU        Unreviewed;       618 AA.
AC   A0A3P8ZEW1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 2.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Formin binding protein 1b {ECO:0000313|Ensembl:ENSELUP00000027235.2};
GN   Name=FNBP1 {ECO:0000313|Ensembl:ENSELUP00000027235.2};
OS   Esox lucius (Northern pike).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC   Esocidae; Esox.
OX   NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000027235.2, ECO:0000313|Proteomes:UP000265140};
RN   [1] {ECO:0000313|Ensembl:ENSELUP00000027235.2, ECO:0000313|Proteomes:UP000265140}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25069045;
RA   Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA   von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT   "The genome and linkage map of the northern pike (Esox lucius): conserved
RT   synteny revealed between the salmonid sister group and the Neoteleostei.";
RL   PLoS ONE 9:e102089-e102089(2014).
RN   [2] {ECO:0000313|Ensembl:ENSELUP00000027235.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A3P8ZEW1; -.
DR   Ensembl; ENSELUT00000016453.2; ENSELUP00000027235.2; ENSELUG00000003481.2.
DR   GeneTree; ENSGT00950000183047; -.
DR   Proteomes; UP000265140; LG14.
DR   Bgee; ENSELUG00000003481; Expressed in head kidney and 15 other cell types or tissues.
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   CDD; cd11629; HR1_FBP17; 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: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};
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:UP000265140};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          9..285
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          551..612
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          278..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          391..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          479..549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..329
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..534
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   618 AA;  71092 MW;  1CB325068484E1D6 CRC64;
     MVGPWLVFQR WDNGVLACRR LNAMLPLRRD QFDNLEKHTQ SGIEFVERYT KFVKERTEIE
     ISYAKQIRNL SKKYQPKKNS REEEENKYTS CRAFLSTLNE LNDYAGQHEV IAENLSSQII
     AELSRYLTEL KAERKSHFQD GRKAQQHMES SWKQLESSKR RFERDCKEAD RAQQYFEKMD
     NDINVTKADV EKARQQAQMR HQMAADSKTE YSNFLTKFNQ EQNEHYYTVI PSIFQKLQEM
     EERRIERVGM SMKTYADVDR DVLPIVGKCL DGMTKAAESI EPKTDSKQVV DSYKSGFEPP
     GDLEFEDYGP GQAMKRTVSE TSLSNSRGEG KERPSGGKSK GKLWPFIKNK NKSPKQSKEP
     ISNRFNEFMA SKPKMTCLRS LRRGLSLKLG SGPEDFSHLP PEQRRKKLQA KIDDLNKDIQ
     KEMDQKDALT KMKGVYEKNP QMGDPASVDP RLAEIAQNIE KLQFEVQKFE GWLAEVEGRL
     PSKSDPPRRQ SGLYETQNSN SSTVGNNCAQ DRESPDGSYT EEQSSETQAK VTISNPPEVD
     DEFDDDEETL PTIGTCKAIY PFEGHNEGTI SVTEGELLYV IEEDKGDGWT RVRRNEDEEG
     YVPTSYVEVF LETNAKDS
//
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