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Q2HWF0 (FBP1L_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Formin-binding protein 1-like
Alternative name(s):
Transducer of Cdc42-dependent actin assembly protein 1
Short name=Toca-1
Gene names
Name:Fnbp1l
Synonyms:Toca1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length605 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Subunit structure

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.

Subcellular location

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

Tissue specificity

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. Ref.1

Developmental stage

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

Domain

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.

Sequence similarities

Belongs to the FNBP1 family.

Contains 1 FCH domain.

Contains 1 REM (Hr1) repeat.

Contains 1 SH3 domain.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q2HWF0-1)

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.
Note: Gene prediction based on EST data.
Isoform 2 (identifier: Q2HWF0-2)

Also known as: Long; L;

The sequence of this isoform differs from the canonical sequence as follows:
     605-605: S → AVTYI
Isoform 3 (identifier: Q2HWF0-3)

Also known as: Short; S;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 605605Formin-binding protein 1-like
PRO_0000261436

Regions

Domain1 – 6565FCH
Repeat409 – 48476REM
Domain538 – 59962SH3
Region1 – 287287F-BAR domain By similarity
Region245 – 535291Interaction with CDC42 By similarity
Region522 – 60584Interaction with DNM1 By similarity
Region541 – 60565Interaction with DAAM1, DIAPH1 and DIAPH2 By similarity
Region541 – 59757Interaction with DNM2 and WASL By similarity
Coiled coil66 – 258193 By similarity
Coiled coil392 – 48493 By similarity

Sites

Site1651Mediates end-to-end attachment of dimers By similarity

Amino acid modifications

Modified residue2951Phosphoserine By similarity
Modified residue4881Phosphoserine By similarity
Modified residue5011Phosphoserine By similarity

Natural variations

Alternative sequence331 – 38858Missing in isoform 3.
VSP_021714
Alternative sequence6051S → AVTYI in isoform 2 and isoform 3.
VSP_021715

Experimental info

Mutagenesis51 – 522KK → QQ: Impairs membrane tubulation and suppression of neurite elongation. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 28, 2006. Version 2.
Checksum: 6DF6AA35D562FAF7

FASTA60569,974
        10         20         30         40         50         60 
MSWGTELWDQ FDSLDKHTQW GIDFLERYAK FVKERIEIEQ NYAKQLRNLV KKYCPKRSSK 

        70         80         90        100        110        120 
DEEPRFTSCI AFFNILNELN DYAGQREVVA EEMAHRVYGE LMRYAHDLKT ERKMHLQEGR 

       130        140        150        160        170        180 
KAQQYLDMCW KQMDNSKKKF ERECREAEKA QQSYERLDND TNATKADVEK AKQQLNLRTH 

       190        200        210        220        230        240 
MADENKNEYA AQLQNFNGEQ HKHFYVVIPQ IYKQLQEMDE RRTIKLSECY RGFADSERKV 

       250        260        270        280        290        300 
IPIISKCLEG MILAAKSVDE RRDSQMVVDS FKSGFEPPGD FPFEDYSQHI YRTVSDGTIS 

       310        320        330        340        350        360 
ASKQEGGKMD SKSTAGKAKG KLWLFGKKPK PQSPPLTPTS LFTSSPPNGS QFLTLSIEPV 

       370        380        390        400        410        420 
HYCMNEIKTG KPRIPSFRSL KRGWSMKMGP ALEDFSHLPP EQRRKKLQQR IDELNRGLQK 

       430        440        450        460        470        480 
ESDQKEALNK MKDVYEKNPQ MGDPGSLQPK LAETMNNIDR LRMEIHKNEA WLSEVEGKTG 

       490        500        510        520        530        540 
VRGDRRHSSD INHLVTQGRE SPEGSYTDDA NQEVRGPPQQ HGHHSEFDDE FEDDDPLPAI 

       550        560        570        580        590        600 
GHCKAIYPFD GHNEGTLAMK EGEVLYIIEE DKGDGWTRAR RQNGEEGYVP TTYIDVTLEK 


NSKGS 

« Hide

Isoform 2 (Long) (L) [UniParc].

Checksum: C862B6CFC596AA35
Show »

FASTA60970,435
Isoform 3 (Short) (S) [UniParc].

Checksum: 6B93588F7274B088
Show »

FASTA55163,947

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB250295 mRNA. Translation: BAE79635.1.
AB250296 mRNA. Translation: BAE79636.1.
AABR03012297 Genomic DNA. No translation available.
RefSeqNP_001034698.1. NM_001039609.1. [Q2HWF0-2]
UniGeneRn.213503.

3D structure databases

ProteinModelPortalQ2HWF0.
SMRQ2HWF0. Positions 1-287, 542-597.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ2HWF0.

Proteomic databases

PaxDbQ2HWF0.
PRIDEQ2HWF0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID310839.
KEGGrno:310839.
UCSCRGD:1305386. rat. [Q2HWF0-1]

Organism-specific databases

CTD54874.
RGD1305386. Fnbp1l.

Phylogenomic databases

eggNOGNOG323796.
HOGENOMHOG000231767.
HOVERGENHBG002489.
PhylomeDBQ2HWF0.
TreeFamTF351162.

Gene expression databases

GenevestigatorQ2HWF0.

Family and domain databases

InterProIPR001060. FCH_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio662725.
PROQ2HWF0.

Entry information

Entry nameFBP1L_RAT
AccessionPrimary (citable) accession number: Q2HWF0
Secondary accession number(s): Q2HWE9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: May 14, 2014
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families