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Protein

Formin-binding protein 1-like

Gene

Fnbp1l

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. May bind to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promote membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by activating the WASL-WASPIP complex, the predominant form of WASL/N-WASP in cells. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Essential for autophagy of intracellular bacterial pathogens (By similarity). May negatively regulate neurite extension and axon branching in developing neurons.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei165 – 1651Mediates end-to-end attachment of dimersBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Autophagy, Differentiation, Endocytosis, Neurogenesis

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Formin-binding protein 1-like
Alternative name(s):
Transducer of Cdc42-dependent actin assembly protein 1
Short name:
Toca-1
Gene namesi
Name:Fnbp1l
Synonyms:Toca1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1305386. Fnbp1l.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi51 – 522KK → QQ: Impairs membrane tubulation and suppression of neurite elongation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 605605Formin-binding protein 1-likePRO_0000261436Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei295 – 2951PhosphoserineBy similarity
Modified residuei488 – 4881PhosphoserineBy similarity
Modified residuei501 – 5011PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ2HWF0.
PRIDEiQ2HWF0.

PTM databases

PhosphoSiteiQ2HWF0.

Expressioni

Tissue specificityi

Isoform 1 is expressed in brain. Isoform 2 is expressed in brain, kidney and lung. Within the brain expression is seen in cortical neurons, hippocampal pyramidal neurons, hypothalamus and piriform cortex.1 Publication

Developmental stagei

Expression in brain declines from E18 to P8 and is undetectable from P14 onwards.1 Publication

Gene expression databases

GenevestigatoriQ2HWF0.

Interactioni

Subunit structurei

Homodimerizes, the dimers can polymerize end-to-end to form filamentous structures. Interacts with GTP-bound CDC42. Interacts with DAAM1, DIAPH1, DIAPH2, DNM1, DNM2 and WASL/N-WASP. Interacts with ATG3 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ2HWF0.
SMRiQ2HWF0. Positions 1-287, 542-597.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 263263F-BARPROSITE-ProRule annotationAdd
BLAST
Repeati409 – 48476REMAdd
BLAST
Domaini538 – 59962SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni245 – 535291Interaction with CDC42By similarityAdd
BLAST
Regioni522 – 60584Interaction with DNM1By similarityAdd
BLAST
Regioni541 – 60565Interaction with DAAM1, DIAPH1 and DIAPH2By similarityAdd
BLAST
Regioni541 – 59757Interaction with DNM2 and WASLBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili66 – 258193By similarityAdd
BLAST
Coiled coili392 – 48493By similarityAdd
BLAST

Domaini

The F-BAR domain binds the phospholipid membrane with its concave surface. The end-to-end polymerization of dimers of these domains provides a curved surface that fits best membranes with around 600 A diameter, and may drive tubulation (By similarity).By similarity

Sequence similaritiesi

Belongs to the FNBP1 family.Curated
Contains 1 F-BAR domain.PROSITE-ProRule annotation
Contains 1 REM (Hr1) repeat.Curated
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiNOG323796.
HOGENOMiHOG000231767.
HOVERGENiHBG002489.
InParanoidiQ2HWF0.
PhylomeDBiQ2HWF0.
TreeFamiTF351162.

Family and domain databases

InterProiIPR001060. FCH_dom.
IPR030116. FNBP1L.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR12602:SF35. PTHR12602:SF35. 1 hit.
PfamiPF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51741. F_BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q2HWF0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSWGTELWDQ FDSLDKHTQW GIDFLERYAK FVKERIEIEQ NYAKQLRNLV
60 70 80 90 100
KKYCPKRSSK DEEPRFTSCI AFFNILNELN DYAGQREVVA EEMAHRVYGE
110 120 130 140 150
LMRYAHDLKT ERKMHLQEGR KAQQYLDMCW KQMDNSKKKF ERECREAEKA
160 170 180 190 200
QQSYERLDND TNATKADVEK AKQQLNLRTH MADENKNEYA AQLQNFNGEQ
210 220 230 240 250
HKHFYVVIPQ IYKQLQEMDE RRTIKLSECY RGFADSERKV IPIISKCLEG
260 270 280 290 300
MILAAKSVDE RRDSQMVVDS FKSGFEPPGD FPFEDYSQHI YRTVSDGTIS
310 320 330 340 350
ASKQEGGKMD SKSTAGKAKG KLWLFGKKPK PQSPPLTPTS LFTSSPPNGS
360 370 380 390 400
QFLTLSIEPV HYCMNEIKTG KPRIPSFRSL KRGWSMKMGP ALEDFSHLPP
410 420 430 440 450
EQRRKKLQQR IDELNRGLQK ESDQKEALNK MKDVYEKNPQ MGDPGSLQPK
460 470 480 490 500
LAETMNNIDR LRMEIHKNEA WLSEVEGKTG VRGDRRHSSD INHLVTQGRE
510 520 530 540 550
SPEGSYTDDA NQEVRGPPQQ HGHHSEFDDE FEDDDPLPAI GHCKAIYPFD
560 570 580 590 600
GHNEGTLAMK EGEVLYIIEE DKGDGWTRAR RQNGEEGYVP TTYIDVTLEK

NSKGS

Note: Gene prediction based on EST data.

Length:605
Mass (Da):69,974
Last modified:November 28, 2006 - v2
Checksum:i6DF6AA35D562FAF7
GO
Isoform 2 (identifier: Q2HWF0-2) [UniParc]FASTAAdd to basket

Also known as: Long, L

The sequence of this isoform differs from the canonical sequence as follows:
     605-605: S → AVTYI

Show »
Length:609
Mass (Da):70,435
Checksum:iC862B6CFC596AA35
GO
Isoform 3 (identifier: Q2HWF0-3) [UniParc]FASTAAdd to basket

Also known as: Short, S

The sequence of this isoform differs from the canonical sequence as follows:
     331-388: Missing.
     605-605: S → AVTYI

Show »
Length:551
Mass (Da):63,947
Checksum:i6B93588F7274B088
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei331 – 38858Missing in isoform 3. 1 PublicationVSP_021714Add
BLAST
Alternative sequencei605 – 6051S → AVTYI in isoform 2 and isoform 3. 1 PublicationVSP_021715

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB250295 mRNA. Translation: BAE79635.1.
AB250296 mRNA. Translation: BAE79636.1.
AABR03012297 Genomic DNA. No translation available.
RefSeqiNP_001034698.1. NM_001039609.1. [Q2HWF0-2]
UniGeneiRn.213503.

Genome annotation databases

GeneIDi310839.
KEGGirno:310839.
UCSCiRGD:1305386. rat. [Q2HWF0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB250295 mRNA. Translation: BAE79635.1.
AB250296 mRNA. Translation: BAE79636.1.
AABR03012297 Genomic DNA. No translation available.
RefSeqiNP_001034698.1. NM_001039609.1. [Q2HWF0-2]
UniGeneiRn.213503.

3D structure databases

ProteinModelPortaliQ2HWF0.
SMRiQ2HWF0. Positions 1-287, 542-597.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ2HWF0.

Proteomic databases

PaxDbiQ2HWF0.
PRIDEiQ2HWF0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi310839.
KEGGirno:310839.
UCSCiRGD:1305386. rat. [Q2HWF0-1]

Organism-specific databases

CTDi54874.
RGDi1305386. Fnbp1l.

Phylogenomic databases

eggNOGiNOG323796.
HOGENOMiHOG000231767.
HOVERGENiHBG002489.
InParanoidiQ2HWF0.
PhylomeDBiQ2HWF0.
TreeFamiTF351162.

Miscellaneous databases

NextBioi662725.
PROiQ2HWF0.

Gene expression databases

GenevestigatoriQ2HWF0.

Family and domain databases

InterProiIPR001060. FCH_dom.
IPR030116. FNBP1L.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR12602:SF35. PTHR12602:SF35. 1 hit.
PfamiPF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51741. F_BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Regulation of neuronal morphology by Toca-1, an F-BAR/EFC protein that induces plasma membrane invagination."
    Kakimoto T., Katoh H., Negishi M.
    J. Biol. Chem. 281:29042-29053(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF 51-LYS-LYS-52.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.

Entry informationi

Entry nameiFBP1L_RAT
AccessioniPrimary (citable) accession number: Q2HWF0
Secondary accession number(s): Q2HWE9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: March 4, 2015
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.