FBP1L_RAT
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 03-AUG-2022, entry version 116.
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 E18 to P8 and is
CC 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}.
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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; Q2HWF0; -.
DR PRIDE; Q2HWF0; -.
DR Ensembl; ENSRNOT00000104633; ENSRNOP00000090789; ENSRNOG00000013798. [Q2HWF0-2]
DR Ensembl; ENSRNOT00000116752; ENSRNOP00000083605; ENSRNOG00000013798. [Q2HWF0-3]
DR GeneID; 310839; -.
DR KEGG; rno:310839; -.
DR UCSC; RGD:1305386; rat. [Q2HWF0-1]
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; AEKAQQC; -.
DR OrthoDB; 348563at2759; -.
DR PhylomeDB; Q2HWF0; -.
DR TreeFam; TF351162; -.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013409; RHOJ GTPase cycle.
DR PRO; PR:Q2HWF0; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000013798; Expressed in lung and 19 other tissues.
DR Genevisible; Q2HWF0; RN.
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: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; 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; 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
