Q8K012 (FBP1L_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	605 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › cytoskeleton By similarity. Cytoplasm › cell 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 process	Autophagy Endocytosis
Cellular component	Cell membrane Cytoplasm Cytoplasmic vesicle Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing
Domain	Coiled coil SH3 domain
Ligand	Lipid-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	autophagy Inferred from electronic annotation. Source: UniProtKB-KW endocytosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cell 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_function	lipid 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 605	605	Formin-binding protein 1-like		PRO_0000261435
Regions
	Domain	1 – 65	65	FCH
	Repeat	409 – 484	76	REM
	Domain	538 – 599	62	SH3
	Region	1 – 287	287	F-BAR domain By similarity
	Region	245 – 535	291	Interaction with CDC42 By similarity
	Region	522 – 605	84	Interaction with DNM1 By similarity
	Region	541 – 605	65	Interaction with DAAM1, DIAPH1 and DIAPH2 By similarity
	Region	541 – 597	57	Interaction with DNM2 and WASL By similarity
	Coiled coil	66 – 258	193	By similarity
	Coiled coil	392 – 484	93	By similarity
Sites
	Site	165	1	Mediates end-to-end attachment of dimers By similarity
Amino acid modifications
	Modified residue	295	1	Phosphoserine By similarity
	Modified residue	488	1	Phosphoserine By similarity
	Modified residue	501	1	Phosphoserine Ref.4 Ref.5 Ref.6
Natural variations
	Alternative sequence	331 – 389	59	Missing in isoform 2.		VSP_021712
	Alternative sequence	605	1	S → AVTYI in isoform 2.		VSP_021713

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 28, 2006. Version 2. Checksum: ABFE6744EF4241E1	FASTA	605	69,885
	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
	Isoform 2 [UniParc]. Checksum: 1645834302E8AABE	FASTA	550	63,918
	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 PALEDFSHLP PEQRRKKLQQ RIDELNRGLQ 370 380 390 400 410 420 KEADQKEALN KMKDVYEKNP QMGDPGSLQP KLAETMNNID RLRMEIHKNE AWLSEVEGKT 430 440 450 460 470 480 GIRGDRRHSS DINHLVTQGR ESPEGSYTDD ANQEVRGPPQ QHGHHSEFDD EFEDDDPLPA 490 500 510 520 530 540 IGHCKAIYPF DGHNEGTLAM KEGEVLYIIE EDKGDGWTRA RRQNGEEGYV PTTYIDVTLE 550 KSSKGAVTYI

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. , 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. , 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]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, MASS SPECTROMETRY. Tissue: Brain cortex.
[6]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, MASS SPECTROMETRY. Tissue: Liver.
+	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.
IPI	IPI00970332. IPI00970419.
RefSeq	NP_001108137.1. NM_001114665.1. NP_694758.2. NM_153118.2.
UniGene	Mm.209491. Mm.470230.
3D structure databases
HSSP	HSSP built from PDB template 2CT4 based on UniProtKB Q15642.
ProteinModelPortal	Q8K012.
SMR	Q8K012. Positions 10-287, 393-478, 542-602.
ModBase	Search...
PTM databases
PhosphoSite	Q8K012.
Proteomic databases
PaxDb	Q8K012.
PRIDE	Q8K012.
Protocols and materials databases
DNASU	214459.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	214459.
KEGG	mmu:214459.
UCSC	uc008rer.2. mouse. uc008res.2. mouse.
Organism-specific databases
CTD	54874.
MGI	MGI:1925642. Fnbp1l.
Phylogenomic databases
eggNOG	NOG323796.
HOGENOM	HOG000231767.
HOVERGEN	HBG002489.
InParanoid	Q8K012.
OrthoDB	EOG4SN1NK.
Gene expression databases
CleanEx	MM_FNBP1L.
Genevestigator	Q8K012.
GermOnline	ENSMUSG00000039735. Mus musculus.
Family and domain databases
InterPro	IPR001060. FCH_dom. IPR001452. SH3_domain. [Graphical view]
Pfam	PF00611. FCH. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
SMART	SM00055. FCH. 1 hit. SM00326. SH3. 1 hit. [Graphical view]
SUPFAM	SSF50044. SH3. 1 hit.
PROSITE	PS50133. FCH. 1 hit. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	FNBP1L. mouse.
NextBio	374318.
SOURCE	Search...

Entry information

Entry name

FBP1L_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program