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Q8K012 (FBP1L_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.

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 By similarity. Cytoplasmcytoskeleton By similarity. Cytoplasmcell cortex By similarity. Cytoplasmic vesicle By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity.

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.

Sequence caution

The sequence AAH34510.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAutophagy
Endocytosis
   Cellular componentCell membrane
Cytoplasm
Cytoplasmic vesicle
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
SH3 domain
   LigandLipid-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processautophagy

Inferred from electronic annotation. Source: UniProtKB-KW

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionlipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8K012-1)

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: Q8K012-2)

The sequence of this isoform differs from the canonical sequence as follows:
     331-389: Missing.
     605-605: S → AVTYI

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 605605Formin-binding protein 1-like
PRO_0000261435

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 Ref.5
Modified residue4881Phosphoserine By similarity
Modified residue5011Phosphoserine By similarity

Natural variations

Alternative sequence331 – 38959Missing in isoform 2.
VSP_021712
Alternative sequence6051S → AVTYI in isoform 2.
VSP_021713

Sequences

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

Last modified November 28, 2006. Version 2.
Checksum: ABFE6744EF4241E1

FASTA60569,885
        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 YRTISDGTIS 

       310        320        330        340        350        360 
AAKQESGKMD SKSTVGKAKG KLWLFGKKPK PQSPPLTPTS LFTSSTPNGS QFLTLSIEPV 

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

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

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

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


SSKGS 

« Hide

Isoform 2 [UniParc].

Checksum: 1645834302E8AABE
Show »

FASTA55063,918

References

[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-108 (ISOFORMS 1/2).
Strain: C57BL/6J.
Tissue: Bone marrow.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 132-605 (ISOFORM 2).
Tissue: Eye.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC099584 Genomic DNA. No translation available.
AC138720 Genomic DNA. No translation available.
AK151930 mRNA. Translation: BAE30806.1.
AK152002 mRNA. Translation: BAE30866.1.
BC034510 mRNA. Translation: AAH34510.1. Different initiation.
UniGeneMm.209491.
Mm.470230.

3D structure databases

ProteinModelPortalQ8K012.
SMRQ8K012. Positions 10-287, 393-478, 542-602.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8K012. 1 interaction.
MINTMINT-4116706.

PTM databases

PhosphoSiteQ8K012.

Proteomic databases

PaxDbQ8K012.
PRIDEQ8K012.

Protocols and materials databases

DNASU214459.
StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:1925642. Fnbp1l.

Phylogenomic databases

eggNOGNOG323796.
HOGENOMHOG000231767.
HOVERGENHBG002489.
InParanoidQ8K012.
PhylomeDBQ8K012.

Gene expression databases

CleanExMM_FNBP1L.
GenevestigatorQ8K012.

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

ChiTaRSFNBP1L. mouse.
NextBio374318.
PROQ8K012.
SOURCESearch...

Entry information

Entry nameFBP1L_MOUSE
AccessionPrimary (citable) accession number: Q8K012
Secondary accession number(s): Q3U901
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: April 16, 2014
This is version 104 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot