ID FBP1L_MOUSE Reviewed; 605 AA. AC Q8K012; Q3U901; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2006, sequence version 2. DT 08-NOV-2023, entry version 150. 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 Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-108 (ISOFORMS 1/2). RC STRAIN=C57BL/6J; TISSUE=Bone marrow; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 132-605 (ISOFORM 2). RC TISSUE=Eye; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-488; SER-501 AND RP SER-505, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and RC Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). 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-WASPIP complex, the predominant form of WASL/N-WASP CC in cells. Actin polymerization may promote the fission of membrane CC tubules to form endocytic vesicles. Essential for autophagy of CC intracellular bacterial pathogens (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homodimerizes, the dimers can polymerize end-to-end to form CC filamentous structures. Interacts with GTP-bound CDC42. Interacts with CC DAAM1, DIAPH1, DIAPH2, DNM1, DNM2 and WASL/N-WASP. Interacts with ATG3. CC Interacts (via SH3 domain) with ABI1, WASF2, CDC42 and WIPF1. CC {ECO:0000250, ECO:0000250|UniProtKB:Q5T0N5}. 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 -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8K012-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8K012-2; Sequence=VSP_021712, VSP_021713; 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=AAH34510.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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 EMBL; AC099584; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC138720; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK151930; BAE30806.1; -; mRNA. DR EMBL; AK152002; BAE30866.1; -; mRNA. DR EMBL; BC034510; AAH34510.1; ALT_INIT; mRNA. DR AlphaFoldDB; Q8K012; -. DR SMR; Q8K012; -. DR STRING; 10090.ENSMUSP00000124947; -. DR iPTMnet; Q8K012; -. DR PhosphoSitePlus; Q8K012; -. DR jPOST; Q8K012; -. DR MaxQB; Q8K012; -. DR PaxDb; 10090-ENSMUSP00000124947; -. DR PeptideAtlas; Q8K012; -. DR ProteomicsDB; 270957; -. [Q8K012-1] DR ProteomicsDB; 270958; -. [Q8K012-2] DR Pumba; Q8K012; -. DR DNASU; 214459; -. DR AGR; MGI:1925642; -. DR MGI; MGI:1925642; Fnbp1l. DR eggNOG; KOG3565; Eukaryota. DR InParanoid; Q8K012; -. DR PhylomeDB; Q8K012; -. DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis. DR ChiTaRS; Fnbp1l; mouse. DR PRO; PR:Q8K012; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q8K012; Protein. DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051020; F:GTPase binding; ISO:MGI. 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; ISO:MGI. DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISO:MGI. DR GO; GO:0010324; P:membrane invagination; ISO:MGI. DR GO; GO:0097320; P:plasma membrane tubulation; ISO:MGI. DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISO:MGI. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR GO; GO:0006900; P:vesicle budding from membrane; ISO:MGI. DR GO; GO:0016050; P:vesicle organization; ISO:MGI. DR GO; GO:0030050; P:vesicle transport along actin filament; ISO:MGI. 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 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_0000261435" 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 /evidence="ECO:0000250" FT REGION 482..538 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 522..605 FT /note="Interaction with DNM1" FT /evidence="ECO:0000250" FT REGION 541..605 FT /note="Interaction with DAAM1, DIAPH1 and DIAPH2" FT /evidence="ECO:0000250" FT REGION 541..597 FT /note="Interaction with DNM2 and WASL" FT /evidence="ECO:0000250" FT COILED 66..258 FT /evidence="ECO:0000250" FT COILED 392..484 FT /evidence="ECO:0000250" 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:19144319, FT ECO:0007744|PubMed:21183079" FT MOD_RES 488 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 501 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 505 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT VAR_SEQ 331..389 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_021712" FT VAR_SEQ 605 FT /note="S -> AVTYI (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_021713" SQ SEQUENCE 605 AA; 69885 MW; ABFE6744EF4241E1 CRC64; MSWGTELWDQ FDSLDKHTQW GIDFLERYAK FVKERIEIEQ NYAKQLRNLV KKYCPKRSSK DEEPRFTSCI AFFNILNELN DYAGQREVVA EEMAHRVYGE LMRYAHDLKT ERKMHLQEGR KAQQYLDMCW KQMDNSKKKF ERECREAEKA QQSYERLDND TNATKADVEK AKQQLNLRTH MADENKNEYA AQLQNFNGEQ HKHFYVVIPQ IYKQLQEMDE RRTIKLSECY RGFADSERKV IPIISKCLEG MILAAKSVDE RRDSQMVVDS FKSGFEPPGD FPFEDYSQHI YRTISDGTIS AAKQESGKMD SKSTVGKAKG KLWLFGKKPK PQSPPLTPTS LFTSSTPNGS QFLTLSIEPV HYCMNEIKTG KPRIPSFRSL KRGVSLIMGP ALEDFSHLPP EQRRKKLQQR IDELNRGLQK EADQKEALNK MKDVYEKNPQ MGDPGSLQPK LAETMNNIDR LRMEIHKNEA WLSEVEGKTG IRGDRRHSSD INHLVTQGRE SPEGSYTDDA NQEVRGPPQQ HGHHSEFDDE FEDDDPLPAI GHCKAIYPFD GHNEGTLAMK EGEVLYIIEE DKGDGWTRAR RQNGEEGYVP TTYIDVTLEK SSKGS //