FBP1L_XENTR
ID FBP1L_XENTR Reviewed; 550 AA.
AC Q6GUF4; Q28GK4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Formin-binding protein 1-like;
DE AltName: Full=Transducer of Cdc42-dependent actin assembly protein 1;
DE Short=Toca-1;
GN Name=fnbp1l; Synonyms=toca1; ORFNames=TEgg061f15.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15260990; DOI=10.1016/j.cell.2004.06.027;
RA Ho H.-Y.H., Rohatgi R., Lebensohn A.M., Ma L., Li J., Gygi S.P.,
RA Kirschner M.W.;
RT "Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-
RT WIP complex.";
RL Cell 118:203-216(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 262-550.
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required to coordinate membrane tubulation with
CC reorganization of the actin cytoskeleton during endocytosis. Promotes
CC cdc42-induced actin polymerization by activating the wasl-waspip
CC complex, the predominant form of wasl/n-wasp in cells. Essential for
CC autophagy of intracellular bacterial pathogens (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimerizes, the dimers can polymerize end-to-end to form
CC filamentous structures. Interacts with GTP-bound cdc42 and wasl/n-wasp
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasmic
CC vesicle {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- DOMAIN: The F-BAR domain binds the phospholipid membrane with its
CC concave surface. The end-to-end polymerization of dimers of these
CC domains provides a curved surface that fits best membranes with around
CC 600 A diameter, and may drive tubulation (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FNBP1 family. {ECO:0000305}.
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DR EMBL; AY640054; AAT57673.1; -; mRNA.
DR EMBL; BC080954; AAH80954.1; -; mRNA.
DR EMBL; CR761355; CAJ81365.1; -; mRNA.
DR RefSeq; NP_001005148.1; NM_001005148.1.
DR PDB; 5FRG; NMR; -; A=330-426.
DR PDBsum; 5FRG; -.
DR AlphaFoldDB; Q6GUF4; -.
DR SMR; Q6GUF4; -.
DR PRIDE; Q6GUF4; -.
DR DNASU; 448740; -.
DR Ensembl; ENSXETT00000076363; ENSXETP00000077632; ENSXETG00000008227.
DR GeneID; 448740; -.
DR KEGG; xtr:448740; -.
DR CTD; 54874; -.
DR Xenbase; XB-GENE-489112; fnbp1l.
DR InParanoid; Q6GUF4; -.
DR OrthoDB; 348563at2759; -.
DR Reactome; R-XTR-9013148; CDC42 GTPase cycle.
DR Reactome; R-XTR-9013409; RHOJ GTPase cycle.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000008227; Expressed in 4-cell stage embryo and 12 other tissues.
DR ExpressionAtlas; Q6GUF4; baseline.
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; cd12072; SH3_FNBP1L; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR030116; FNBP1L.
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:SF14; PTHR15735:SF14; 2.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS51860; REM_1; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Endocytosis; Lipid-binding; Membrane;
KW Reference proteome; SH3 domain.
FT CHAIN 1..550
FT /note="Formin-binding protein 1-like"
FT /id="PRO_0000261438"
FT DOMAIN 1..263
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 339..416
FT /note="REM-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 479..540
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 423..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 66..258
FT /evidence="ECO:0000250"
FT COILED 334..426
FT /evidence="ECO:0000250"
FT SITE 165
FT /note="Mediates end-to-end attachment of dimers"
FT /evidence="ECO:0000250"
FT HELIX 342..379
FT /evidence="ECO:0007829|PDB:5FRG"
FT HELIX 386..389
FT /evidence="ECO:0007829|PDB:5FRG"
FT HELIX 390..417
FT /evidence="ECO:0007829|PDB:5FRG"
SQ SEQUENCE 550 AA; 64010 MW; 916E4A525DFCFF9B CRC64;
MSWGTELWDQ FDNLEKHTQW GIDFLDKYAK FVKERLEIEQ NYAKQLRNLV KKYCPKRSAK
DEEPRFTSCL SFYNILNELN DYAGQREVVA EEMGHRVYAE IMRYSNDIKG ERKSHLQEGR
KAQQYLDMCL KQMDNSKRKF ERECREAEKA QQTYERLDND SNATKSDVEK AKQQLHLRTH
MADESKNEYA AQLQNYNAEQ HKHFYIVIPQ VYKHLQEMDE RRTVKLSECY KGFADAERKV
IPIISKCLEG MVQAAKSVDE RRDSQIVVDC FKSGFEPNGD YPFEDYSQHI YRTVSDGTIS
TPKQESLKPD PRVTVGKAKG KLWLFGKKPK GPALEDFSHL PPEQRRKRLQ QRIDELSREL
QKEMDQKDAL NKMKDVYEKN PQMGDPSSLH PKIAETTSNI ERLRMEIHKN EAWLSEVEGK
VSQRSERRHS AEANHLVAQG RESPEGSYTE DANQEGRVQP QPHAHPEFDD EFDDDEPLPA
IGHCKSLYPF DGNNEGTLAM KEGEVLYIIE EDKGDGWTRA RKQNGEEGYV PTSYIDITLE
KNSKGAVTYI
