FBP1L_XENLA
ID FBP1L_XENLA Reviewed; 543 AA.
AC Q6DCZ7;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
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;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND INTERACTION WITH CDC42 AND WASL.
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).
CC -!- FUNCTION: Required to coordinate membrane tubulation with
CC reorganization of the actin cytoskeleton during endocytosis. Essential
CC for autophagy of intracellular bacterial pathogens (By similarity).
CC Promotes cdc42-induced actin polymerization by activating the wasl-
CC waspip complex, the predominant form of wasl/n-wasp in cells.
CC {ECO:0000250, ECO:0000269|PubMed:15260990}.
CC -!- SUBUNIT: Homodimerizes, the dimers can polymerize end-to-end to form
CC filamentous structures (By similarity). Interacts with GTP-bound cdc42
CC and wasl/n-wasp. {ECO:0000250, ECO:0000269|PubMed:15260990}.
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; BC077835; AAH77835.1; -; mRNA.
DR RefSeq; NP_001086967.1; NM_001093498.1.
DR AlphaFoldDB; Q6DCZ7; -.
DR SMR; Q6DCZ7; -.
DR GeneID; 446802; -.
DR KEGG; xla:446802; -.
DR CTD; 446802; -.
DR Xenbase; XB-GENE-17338248; fnbp1l.S.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 446802; Expressed in egg cell and 19 other 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; 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 Autophagy; Cell membrane; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Endocytosis; Lipid-binding; Membrane; Reference proteome;
KW SH3 domain.
FT CHAIN 1..543
FT /note="Formin-binding protein 1-like"
FT /id="PRO_0000261437"
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 424..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"
SQ SEQUENCE 543 AA; 63330 MW; 470DF29DC1D16932 CRC64;
MSWGTELWDQ FDNLEKHTQW GIDFLDKYAK FVKERLEIEQ NYAKQLRNLV KKFCPKRSAK
DEEPRFTSCL SFYNILNELN DYAGQREVVA EEIGHRVYAE IMRYSNDIKG ERKSHLHEGR
KAQQYLDMCL KQMDNSKRKF ERECREAEKA QQSYERLDND TNATKSDVEK AKQQLHLRTH
MADESKNEYA AQLQNYNAEQ HKHFYIVIPQ VYKHLQEMDE RRTIKLSECY KGFADAERKV
IPIISKCLEG MVQAAKSVDE RRDSQIVVDC FKSGFEPPGD FPFEDYSQHI YRTVSDGTIS
TPKQESLKPD PRMTVGKAKG KLWLFGKKPK GPALEDFSHL PPEQRRKRLQ QRIDELSREL
QKEMDQKDAL NKMKDVYEKN PQMGDPGSLH PKIAETTSNI ERLRMEIHKN EGWLSEVEGK
VSQRSERRHS AEANHLVAQG RESPEGSYTE DANQEGRVQP QHHAHPEFDD EFDDDEPLPA
IGHCKSLYPF DGNNEGTLAM KEGEVLYIIE EDKGDGWTRA RKQNGEEGYV PTSYIEITLE
KKQ
