ID A0A2K6E1Q7_MACNE Unreviewed; 608 AA.
AC A0A2K6E1Q7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Formin-binding protein 1-like {ECO:0000256|ARBA:ARBA00019975};
DE AltName: Full=Transducer of Cdc42-dependent actin assembly protein 1 {ECO:0000256|ARBA:ARBA00032854};
GN Name=FNBP1L {ECO:0000313|Ensembl:ENSMNEP00000042095.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000042095.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000042095.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}. Cytoplasmic vesicle
CC {ECO:0000256|ARBA:ARBA00004541}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}. Vesicle
CC {ECO:0000256|ARBA:ARBA00004373}.
CC -!- SIMILARITY: Belongs to the FNBP1 family.
CC {ECO:0000256|ARBA:ARBA00009426}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A2K6E1Q7; -.
DR Ensembl; ENSMNET00000066597.1; ENSMNEP00000042095.1; ENSMNEG00000043720.1.
DR GeneTree; ENSGT00950000183047; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000043720; Expressed in lung and 12 other cell types or tissues.
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:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd07675; F-BAR_FNBP1L; 1.
DR CDD; cd11628; HR1_CIP4_FNBP1L; 1.
DR CDD; cd12072; SH3_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; IPR035494; FNBP1L_F-BAR.
DR InterPro; IPR035493; FNBP1L_SH3.
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 Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01077}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000233120};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..259
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 396..473
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 537..598
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 475..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 126..170
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 403..437
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 475..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 608 AA; 70355 MW; D158E15A6ACC064F CRC64;
PWLKCSHDLL DKHTQWGIDF LERYAKFVKE RIEIEQNYAK QLRNLVKKYC PKRSSKDEEP
RFTSCVAFFN ILNELNDYAG QREVVAEEMA HRVYGELMRY AHDLKTERKM HLQEGRKAQQ
YLDMCWKQMD NSKKKFEREC REAEKAQQSY ERLDNDTNAT KADVEKAKQQ LNLRTHMADE
NKNEYAAQLQ NFNGEQHKHF YVVIPQIYKQ LQEMDERRTI KLSECYRGFA DSERKVIPII
SKCLEGMILA AKSVDERRDS QMVVDSFKSG FEPPGDFPFE DYSQHIYRTI SDGTISASKQ
ESGKMDAKTT VGKAKGKLWL FGKKPKVKVI KFLYPQSPPL TPTSLFTSST PNGSQFLTFS
IEPVHYCMNE IKTGKPRIPS FRSLKRGGPA LEDFSHLPPE QRRKKLQQRI DELNRELQKE
SDQKDALNKM KDVYEKNPQM GDPGSLQPKL AETMNNIDRL RMEIHKNEAW LSEVEGKTGG
RGDRRHSSDI NHLVTQGRES PEGSYTDDAN QEVRGPPQQH GHHSEFDDEF EDDDPLPAIG
HCKAIYPFDG HNEGTLAMKE GEVLYIIEED KGDGWTRARR QNGEEGYVPT SYIDVTLEKN
SKGAVTYI
//
