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Q2HWF0

- FBP1L_RAT

UniProt

Q2HWF0 - FBP1L_RAT

Protein

Formin-binding protein 1-like

Gene

Fnbp1l

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 2 (28 Nov 2006)
      Previous versions | rss
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    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

    1. lipid binding Source: UniProtKB-KW

    GO - Biological processi

    1. autophagy Source: UniProtKB-KW
    2. cell differentiation Source: UniProtKB-KW
    3. endocytosis Source: UniProtKB-KW
    4. nervous system development Source: UniProtKB-KW

    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: Unplaced

    Organism-specific databases

    RGDi1305386. Fnbp1l.

    Subcellular locationi

    Cytoplasm 1 Publication. Cytoplasmcytoskeleton By similarity. Cytoplasmcell cortex By similarity. Cytoplasmic vesicle By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
    Note: Localized to the cell body, axons and neurites of differentiating neurons.

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB-SubCell
    2. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
    3. cytoskeleton Source: UniProtKB-SubCell
    4. plasma membrane Source: UniProtKB-SubCell

    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 – 6565FCHPROSITE-ProRule annotationAdd
    BLAST
    Repeati409 – 48476REMAdd
    BLAST
    Domaini538 – 59962SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 287287F-BAR domainBy similarityAdd
    BLAST
    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 FCH 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.
    PhylomeDBiQ2HWF0.
    TreeFamiTF351162.

    Family and domain databases

    InterProiIPR001060. FCH_dom.
    IPR001452. SH3_domain.
    [Graphical view]
    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.
    PROSITEiPS50133. FCH. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    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

    MSWGTELWDQ FDSLDKHTQW GIDFLERYAK FVKERIEIEQ NYAKQLRNLV    50
    KKYCPKRSSK DEEPRFTSCI AFFNILNELN DYAGQREVVA EEMAHRVYGE 100
    LMRYAHDLKT ERKMHLQEGR KAQQYLDMCW KQMDNSKKKF ERECREAEKA 150
    QQSYERLDND TNATKADVEK AKQQLNLRTH MADENKNEYA AQLQNFNGEQ 200
    HKHFYVVIPQ IYKQLQEMDE RRTIKLSECY RGFADSERKV IPIISKCLEG 250
    MILAAKSVDE RRDSQMVVDS FKSGFEPPGD FPFEDYSQHI YRTVSDGTIS 300
    ASKQEGGKMD SKSTAGKAKG KLWLFGKKPK PQSPPLTPTS LFTSSPPNGS 350
    QFLTLSIEPV HYCMNEIKTG KPRIPSFRSL KRGWSMKMGP ALEDFSHLPP 400
    EQRRKKLQQR IDELNRGLQK ESDQKEALNK MKDVYEKNPQ MGDPGSLQPK 450
    LAETMNNIDR LRMEIHKNEA WLSEVEGKTG VRGDRRHSSD INHLVTQGRE 500
    SPEGSYTDDA NQEVRGPPQQ HGHHSEFDDE FEDDDPLPAI GHCKAIYPFD 550
    GHNEGTLAMK EGEVLYIIEE DKGDGWTRAR RQNGEEGYVP TTYIDVTLEK 600
    NSKGS 605

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB250295 mRNA. Translation: BAE79635.1 .
    AB250296 mRNA. Translation: BAE79636.1 .
    AABR03012297 Genomic DNA. No translation available.
    RefSeqi NP_001034698.1. NM_001039609.1. [Q2HWF0-2 ]
    UniGenei Rn.213503.

    3D structure databases

    ProteinModelPortali Q2HWF0.
    SMRi Q2HWF0. Positions 1-287, 542-597.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q2HWF0.

    Proteomic databases

    PaxDbi Q2HWF0.
    PRIDEi Q2HWF0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 310839.
    KEGGi rno:310839.
    UCSCi RGD:1305386. rat. [Q2HWF0-1 ]

    Organism-specific databases

    CTDi 54874.
    RGDi 1305386. Fnbp1l.

    Phylogenomic databases

    eggNOGi NOG323796.
    HOGENOMi HOG000231767.
    HOVERGENi HBG002489.
    PhylomeDBi Q2HWF0.
    TreeFami TF351162.

    Miscellaneous databases

    NextBioi 662725.
    PROi Q2HWF0.

    Gene expression databases

    Genevestigatori Q2HWF0.

    Family and domain databases

    InterProi IPR001060. FCH_dom.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF00611. FCH. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    SMARTi SM00055. FCH. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS50133. FCH. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 65 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