ID FBP1L_RAT Reviewed; 605 AA. AC Q2HWF0; Q2HWE9; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2006, sequence version 2. DT 24-JAN-2024, entry version 123. 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 Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF RP 51-LYS-LYS-52. RX PubMed=16885158; DOI=10.1074/jbc.m604025200; RA Kakimoto T., Katoh H., Negishi M.; RT "Regulation of neuronal morphology by Toca-1, an F-BAR/EFC protein that RT induces plasma membrane invagination."; RL J. Biol. Chem. 281:29042-29053(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway; RX PubMed=15057822; DOI=10.1038/nature02426; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 AND SER-501, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). 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). May negatively CC regulate neurite extension and axon branching in developing neurons. CC {ECO:0000250, ECO:0000269|PubMed:16885158}. 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:0000269|PubMed:16885158}. 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}. Note=Localized to the cell body, axons and neurites CC of differentiating neurons. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q2HWF0-1; Sequence=Displayed; CC Name=2; Synonyms=Long, L; CC IsoId=Q2HWF0-2; Sequence=VSP_021715; CC Name=3; Synonyms=Short, S; CC IsoId=Q2HWF0-3; Sequence=VSP_021714, VSP_021715; CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in brain. Isoform 2 is CC expressed in brain, kidney and lung. Within the brain expression is CC seen in cortical neurons, hippocampal pyramidal neurons, hypothalamus CC and piriform cortex. {ECO:0000269|PubMed:16885158}. CC -!- DEVELOPMENTAL STAGE: Expression in brain declines from 18 dpc to P8 and CC is undetectable from P14 onwards. {ECO:0000269|PubMed:16885158}. 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 --------------------------------------------------------------------------- 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; AB250295; BAE79635.1; -; mRNA. DR EMBL; AB250296; BAE79636.1; -; mRNA. DR EMBL; AABR03012297; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001034698.1; NM_001039609.1. [Q2HWF0-2] DR AlphaFoldDB; Q2HWF0; -. DR SMR; Q2HWF0; -. DR STRING; 10116.ENSRNOP00000052531; -. DR iPTMnet; Q2HWF0; -. DR PhosphoSitePlus; Q2HWF0; -. DR PaxDb; 10116-ENSRNOP00000052531; -. DR Ensembl; ENSRNOT00000104633.1; ENSRNOP00000090789.1; ENSRNOG00000013798.9. [Q2HWF0-2] DR Ensembl; ENSRNOT00000116752.1; ENSRNOP00000083605.1; ENSRNOG00000013798.9. [Q2HWF0-3] DR GeneID; 310839; -. DR KEGG; rno:310839; -. DR UCSC; RGD:1305386; rat. [Q2HWF0-1] DR AGR; RGD:1305386; -. DR CTD; 54874; -. DR RGD; 1305386; Fnbp1l. DR VEuPathDB; HostDB:ENSRNOG00000013798; -. DR eggNOG; KOG3565; Eukaryota. DR GeneTree; ENSGT00950000183047; -. DR HOGENOM; CLU_023320_2_0_1; -. DR InParanoid; Q2HWF0; -. DR OMA; YADGWWE; -. DR OrthoDB; 2995634at2759; -. DR PhylomeDB; Q2HWF0; -. DR TreeFam; TF351162; -. DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis. DR PRO; PR:Q2HWF0; -. DR Proteomes; UP000002494; Chromosome 2. DR Bgee; ENSRNOG00000013798; Expressed in lung and 19 other cell types or tissues. DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051020; F:GTPase binding; ISO:RGD. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0060271; P:cilium assembly; ISO:RGD. DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISO:RGD. DR GO; GO:0010324; P:membrane invagination; ISO:RGD. DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW. DR GO; GO:0097320; P:plasma membrane tubulation; ISO:RGD. DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISO:RGD. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR GO; GO:0006900; P:vesicle budding from membrane; ISO:RGD. DR GO; GO:0016050; P:vesicle organization; ISO:RGD. DR GO; GO:0030050; P:vesicle transport along actin filament; ISO:RGD. 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. DR Genevisible; Q2HWF0; RN. PE 1: Evidence at protein level; KW Alternative splicing; Autophagy; Cell membrane; Coiled coil; Cytoplasm; KW Cytoplasmic vesicle; Cytoskeleton; Developmental protein; Differentiation; KW Endocytosis; Lipid-binding; Membrane; Neurogenesis; Phosphoprotein; KW Reference proteome; SH3 domain. FT CHAIN 1..605 FT /note="Formin-binding protein 1-like" FT /id="PRO_0000261436" 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 325..345 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 480..539 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:22673903" FT MOD_RES 488 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5T0N5" FT MOD_RES 501 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 505 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8K012" FT VAR_SEQ 331..388 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16885158" FT /id="VSP_021714" FT VAR_SEQ 605 FT /note="S -> AVTYI (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:16885158" FT /id="VSP_021715" FT MUTAGEN 51..52 FT /note="KK->QQ: Impairs membrane tubulation and suppression FT of neurite elongation." FT /evidence="ECO:0000269|PubMed:16885158" SQ SEQUENCE 605 AA; 69974 MW; 6DF6AA35D562FAF7 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 YRTVSDGTIS ASKQEGGKMD SKSTAGKAKG KLWLFGKKPK PQSPPLTPTS LFTSSPPNGS QFLTLSIEPV HYCMNEIKTG KPRIPSFRSL KRGWSMKMGP ALEDFSHLPP EQRRKKLQQR IDELNRGLQK ESDQKEALNK MKDVYEKNPQ MGDPGSLQPK LAETMNNIDR LRMEIHKNEA WLSEVEGKTG VRGDRRHSSD INHLVTQGRE SPEGSYTDDA NQEVRGPPQQ HGHHSEFDDE FEDDDPLPAI GHCKAIYPFD GHNEGTLAMK EGEVLYIIEE DKGDGWTRAR RQNGEEGYVP TTYIDVTLEK NSKGS //