FBP1L_HUMAN
ID FBP1L_HUMAN Reviewed; 605 AA.
AC Q5T0N5; J3QSS4; Q5T0N6; Q6B097; Q6P653; Q6R4Q4; Q9NXG1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 3.
DT 03-AUG-2022, entry version 160.
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=C1orf39, TOCA1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH CDC42
RP AND WASL, AND MUTAGENESIS OF 441-MET--ASP-443 AND TRP-576.
RC TISSUE=Fetal brain;
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 GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 134-605 (ISOFORM 4), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 208-605 (ISOFORM 3).
RC TISSUE=Lung, and Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 200-605 (ISOFORM 3).
RC TISSUE=Hepatoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP FUNCTION, AND INTERACTION WITH DNM1 AND WASL.
RX PubMed=16326391; DOI=10.1016/j.devcel.2005.11.005;
RA Itoh T., Erdmann K.S., Roux A., Habermann B., Werner H., De Camilli P.;
RT "Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane
RT invagination by BAR and F-BAR proteins.";
RL Dev. Cell 9:791-804(2005).
RN [6]
RP INTERACTION WITH DAAM1; DIAPH1 AND DIAPH2.
RX PubMed=16630611; DOI=10.1016/j.yexcr.2006.03.013;
RA Aspenstroem P., Richnau N., Johansson A.-S.;
RT "The diaphanous-related formin DAAM1 collaborates with the Rho GTPases RhoA
RT and Cdc42, CIP4 and Src in regulating cell morphogenesis and actin
RT dynamics.";
RL Exp. Cell Res. 312:2180-2194(2006).
RN [7]
RP INTERACTION WITH DNM2 AND WASL.
RX PubMed=16418535; DOI=10.1083/jcb.200508091;
RA Tsujita K., Suetsugu S., Sasaki N., Furutani M., Oikawa T., Takenawa T.;
RT "Coordination between the actin cytoskeleton and membrane deformation by a
RT novel membrane tubulation domain of PCH proteins is involved in
RT endocytosis.";
RL J. Cell Biol. 172:269-279(2006).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=16757518; DOI=10.1242/jcs.03005;
RA Kovacs E.M., Makar R.S., Gertler F.B.;
RT "Tuba stimulates intracellular N-WASP-dependent actin assembly.";
RL J. Cell Sci. 119:2715-2726(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-488 AND SER-501, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP FUNCTION IN AUTOPHAGY, AND INTERACTION WITH ATG3.
RX PubMed=19342671; DOI=10.4049/jimmunol.0803050;
RA Huett A., Ng A., Cao Z., Kuballa P., Komatsu M., Daly M.J., Podolsky D.K.,
RA Xavier R.J.;
RT "A novel hybrid yeast-human network analysis reveals an essential role for
RT FNBP1L in antibacterial autophagy.";
RL J. Immunol. 182:4917-4930(2009).
RN [12]
RP INTERACTION WITH ABI1; WASF2; CDC42 AND WIPF1.
RX PubMed=19798448; DOI=10.1371/journal.pgen.1000675;
RA Giuliani C., Troglio F., Bai Z., Patel F.B., Zucconi A., Malabarba M.G.,
RA Disanza A., Stradal T.B., Cassata G., Confalonieri S., Hardin J.D.,
RA Soto M.C., Grant B.D., Scita G.;
RT "Requirements for F-BAR proteins TOCA-1 and TOCA-2 in actin dynamics and
RT membrane trafficking during Caenorhabditis elegans oocyte growth and
RT embryonic epidermal morphogenesis.";
RL PLoS Genet. 5:E1000675-E1000675(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-488 AND SER-501, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-488 AND SER-501, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-488 AND SER-501, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-488 AND SER-501, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Required to coordinate membrane tubulation with
CC reorganization of the actin cytoskeleton during endocytosis. May bind
CC to lipids such as phosphatidylinositol 4,5-bisphosphate and
CC phosphatidylserine and promote membrane invagination and the formation
CC of tubules. Also promotes CDC42-induced actin polymerization by
CC activating the WASL/N-WASP-WASPIP/WIP complex, the predominant form of
CC WASL/N-WASP in cells. Actin polymerization may promote the fission of
CC membrane tubules to form endocytic vesicles. Essential for autophagy of
CC intracellular bacterial pathogens. {ECO:0000269|PubMed:15260990,
CC ECO:0000269|PubMed:16326391, ECO:0000269|PubMed:19342671}.
CC -!- SUBUNIT: Homodimerizes, the dimers can polymerize end-to-end to form
CC filamentous structures (By similarity). Interacts with GTP-bound CDC42
CC (PubMed:15260990). Interacts with DAAM1, DIAPH1, DIAPH2, DNM1, DNM2 and
CC WASL/N-WASP (PubMed:16326391, PubMed:16630611, PubMed:16418535).
CC Interacts with ATG3 (PubMed:19342671). Interacts (via SH3 domain) with
CC ABI1, WASF2, CDC42 and WIPF1 (PubMed:19798448). {ECO:0000250,
CC ECO:0000269|PubMed:15260990, ECO:0000269|PubMed:16326391,
CC ECO:0000269|PubMed:16418535, ECO:0000269|PubMed:16630611,
CC ECO:0000269|PubMed:19342671, ECO:0000269|PubMed:19798448}.
CC -!- INTERACTION:
CC Q5T0N5; P78325: ADAM8; NbExp=2; IntAct=EBI-714058, EBI-2625954;
CC Q5T0N5; Q9Y4D1: DAAM1; NbExp=2; IntAct=EBI-714058, EBI-2817289;
CC Q5T0N5-3; Q8X482: espF(U); Xeno; NbExp=3; IntAct=EBI-4403262, EBI-22229752;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16757518}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex
CC {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q5T0N5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T0N5-2; Sequence=VSP_021710;
CC Name=3;
CC IsoId=Q5T0N5-3; Sequence=VSP_021709;
CC Name=4;
CC IsoId=Q5T0N5-4; Sequence=VSP_021709, VSP_021711;
CC Name=5;
CC IsoId=Q5T0N5-5; Sequence=VSP_021710, VSP_021711;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91051.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY514449; AAR98814.1; -; mRNA.
DR EMBL; AC095034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL109613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC062477; AAH62477.1; -; mRNA.
DR EMBL; BC074891; AAH74891.1; -; mRNA.
DR EMBL; BC074892; AAH74892.1; -; mRNA.
DR EMBL; AK000282; BAA91051.1; ALT_INIT; mRNA.
DR CCDS; CCDS53343.1; -. [Q5T0N5-1]
DR CCDS; CCDS53344.1; -. [Q5T0N5-4]
DR CCDS; CCDS60192.1; -. [Q5T0N5-3]
DR RefSeq; NP_001020119.1; NM_001024948.2. [Q5T0N5-4]
DR RefSeq; NP_001157945.1; NM_001164473.2. [Q5T0N5-1]
DR RefSeq; NP_060207.2; NM_017737.4. [Q5T0N5-3]
DR AlphaFoldDB; Q5T0N5; -.
DR SMR; Q5T0N5; -.
DR BioGRID; 120222; 37.
DR IntAct; Q5T0N5; 22.
DR MINT; Q5T0N5; -.
DR STRING; 9606.ENSP00000271234; -.
DR iPTMnet; Q5T0N5; -.
DR MetOSite; Q5T0N5; -.
DR PhosphoSitePlus; Q5T0N5; -.
DR BioMuta; FNBP1L; -.
DR DMDM; 118572313; -.
DR EPD; Q5T0N5; -.
DR jPOST; Q5T0N5; -.
DR MassIVE; Q5T0N5; -.
DR MaxQB; Q5T0N5; -.
DR PaxDb; Q5T0N5; -.
DR PeptideAtlas; Q5T0N5; -.
DR PRIDE; Q5T0N5; -.
DR ProteomicsDB; 64183; -. [Q5T0N5-1]
DR ProteomicsDB; 64184; -. [Q5T0N5-2]
DR ProteomicsDB; 64185; -. [Q5T0N5-3]
DR ProteomicsDB; 64186; -. [Q5T0N5-4]
DR ProteomicsDB; 64187; -. [Q5T0N5-5]
DR Antibodypedia; 33658; 176 antibodies from 30 providers.
DR DNASU; 54874; -.
DR Ensembl; ENST00000260506.12; ENSP00000260506.8; ENSG00000137942.18. [Q5T0N5-4]
DR Ensembl; ENST00000271234.13; ENSP00000271234.7; ENSG00000137942.18. [Q5T0N5-1]
DR Ensembl; ENST00000370253.6; ENSP00000359275.2; ENSG00000137942.18. [Q5T0N5-3]
DR GeneID; 54874; -.
DR KEGG; hsa:54874; -.
DR MANE-Select; ENST00000271234.13; ENSP00000271234.7; NM_001164473.3; NP_001157945.1.
DR UCSC; uc001dpv.4; human. [Q5T0N5-1]
DR CTD; 54874; -.
DR DisGeNET; 54874; -.
DR GeneCards; FNBP1L; -.
DR HGNC; HGNC:20851; FNBP1L.
DR HPA; ENSG00000137942; Low tissue specificity.
DR MIM; 608848; gene.
DR neXtProt; NX_Q5T0N5; -.
DR OpenTargets; ENSG00000137942; -.
DR PharmGKB; PA128394675; -.
DR VEuPathDB; HostDB:ENSG00000137942; -.
DR eggNOG; KOG3565; Eukaryota.
DR GeneTree; ENSGT00950000183047; -.
DR HOGENOM; CLU_023320_0_1_1; -.
DR InParanoid; Q5T0N5; -.
DR OMA; AEKAQQC; -.
DR PhylomeDB; Q5T0N5; -.
DR TreeFam; TF351162; -.
DR PathwayCommons; Q5T0N5; -.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR SignaLink; Q5T0N5; -.
DR BioGRID-ORCS; 54874; 6 hits in 1076 CRISPR screens.
DR ChiTaRS; FNBP1L; human.
DR GeneWiki; FNBP1L; -.
DR GenomeRNAi; 54874; -.
DR Pharos; Q5T0N5; Tbio.
DR PRO; PR:Q5T0N5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5T0N5; protein.
DR Bgee; ENSG00000137942; Expressed in cortical plate and 207 other tissues.
DR ExpressionAtlas; Q5T0N5; baseline and differential.
DR Genevisible; Q5T0N5; HS.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:BHF-UCL.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IDA:BHF-UCL.
DR GO; GO:0010324; P:membrane invagination; IDA:BHF-UCL.
DR GO; GO:0097320; P:plasma membrane tubulation; IDA:BHF-UCL.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IDA:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0006900; P:vesicle budding from membrane; IDA:BHF-UCL.
DR GO; GO:0016050; P:vesicle organization; IDA:BHF-UCL.
DR GO; GO:0030050; P:vesicle transport along actin filament; IDA:BHF-UCL.
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; 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; 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 Alternative splicing; Autophagy; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Endocytosis; Lipid-binding; Membrane;
KW Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..605
FT /note="Formin-binding protein 1-like"
FT /id="PRO_0000261434"
FT DOMAIN 1..263
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 397..474
FT /note="REM-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 538..599
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 245..535
FT /note="Interaction with CDC42"
FT REGION 476..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..605
FT /note="Interaction with DNM1"
FT /evidence="ECO:0000269|PubMed:16326391"
FT REGION 541..605
FT /note="Interaction with DAAM1, DIAPH1 and DIAPH2"
FT /evidence="ECO:0000269|PubMed:16630611"
FT REGION 541..597
FT /note="Interaction with DNM2 and WASL"
FT /evidence="ECO:0000269|PubMed:16418535"
FT COILED 66..258
FT /evidence="ECO:0000250"
FT COILED 392..484
FT /evidence="ECO:0000250"
FT COMPBIAS 476..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 165
FT /note="Mediates end-to-end attachment of dimers"
FT /evidence="ECO:0000250"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K012"
FT VAR_SEQ 331..388
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15260990, ECO:0000303|PubMed:15489334"
FT /id="VSP_021709"
FT VAR_SEQ 384..388
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_021710"
FT VAR_SEQ 605
FT /note="S -> AVTYI (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021711"
FT MUTAGEN 441..443
FT /note="MGD->IST: Impairs interaction with CDC42 and reduces
FT CDC42-induced actin assembly."
FT /evidence="ECO:0000269|PubMed:15260990"
FT MUTAGEN 576
FT /note="W->K: Impairs interaction with WASL and reduces
FT CDC42-induced actin assembly."
FT /evidence="ECO:0000269|PubMed:15260990"
SQ SEQUENCE 605 AA; 70065 MW; 1D9237185C3006ED CRC64;
MSWGTELWDQ FDSLDKHTQW GIDFLERYAK FVKERIEIEQ NYAKQLRNLV KKYCPKRSSK
DEEPRFTSCV AFFNILNELN DYAGQREVVA EEMAHRVYGE LMRYAHDLKT ERKMHLQEGR
KAQQYLDMCW KQMDNSKKKF ERECREAEKA QQSYERLDND TNATKADVEK AKQQLNLRTH
MADENKNEYA AQLQNFNGEQ HKHFYVVIPQ IYKQLQEMDE RRTIKLSECY RGFADSERKV
IPIISKCLEG MILAAKSVDE RRDSQMVVDS FKSGFEPPGD FPFEDYSQHI YRTISDGTIS
ASKQESGKMD AKTTVGKAKG KLWLFGKKPK PQSPPLTPTS LFTSSTPNGS QFLTFSIEPV
HYCMNEIKTG KPRIPSFRSL KRGWSVKMGP ALEDFSHLPP EQRRKKLQQR IDELNRELQK
ESDQKDALNK MKDVYEKNPQ MGDPGSLQPK LAETMNNIDR LRMEIHKNEA WLSEVEGKTG
GRGDRRHSSD INHLVTQGRE SPEGSYTDDA NQEVRGPPQQ HGHHNEFDDE FEDDDPLPAI
GHCKAIYPFD GHNEGTLAMK EGEVLYIIEE DKGDGWTRAR RQNGEEGYVP TSYIDVTLEK
NSKGS
