Q2HWF0 (FBP1L_RAT) 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

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [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 › Rattus

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. 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. Cytoplasm › cytoskeleton By similarity. Cytoplasm › cell 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.

Ontologies

Keywords
Biological process	Autophagy Differentiation Endocytosis Neurogenesis
Cellular component	Cell membrane Cytoplasm Cytoplasmic vesicle Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing
Domain	Coiled coil SH3 domain
Ligand	Lipid-binding
Molecular function	Developmental protein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	autophagy Inferred from electronic annotation. Source: UniProtKB-KW cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW endocytosis Inferred from electronic annotation. Source: UniProtKB-KW nervous system development 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 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 605	605	Formin-binding protein 1-like		PRO_0000261436
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 By similarity
Natural variations
	Alternative sequence	331 – 388	58	Missing in isoform 3.		VSP_021714
	Alternative sequence	605	1	S → AVTYI in isoform 2 and isoform 3.		VSP_021715
Experimental info
	Mutagenesis	51 – 52	2	KK → QQ: Impairs membrane tubulation and suppression of neurite elongation. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 28, 2006. Version 2. Checksum: 6DF6AA35D562FAF7	FASTA	605	69,974
	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
	Isoform 2 (Long) (L) [UniParc]. Checksum: C862B6CFC596AA35	FASTA	609	70,435
	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 NSKGAVTYI
	Isoform 3 (Short) (S) [UniParc]. Checksum: 6B93588F7274B088	FASTA	551	63,947
	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 GPALEDFSHL PPEQRRKKLQ QRIDELNRGL 370 380 390 400 410 420 QKESDQKEAL NKMKDVYEKN PQMGDPGSLQ PKLAETMNNI DRLRMEIHKN EAWLSEVEGK 430 440 450 460 470 480 TGVRGDRRHS SDINHLVTQG RESPEGSYTD DANQEVRGPP QQHGHHSEFD DEFEDDDPLP 490 500 510 520 530 540 AIGHCKAIYP FDGHNEGTLA MKEGEVLYII EEDKGDGWTR ARRQNGEEGY VPTTYIDVTL 550 EKNSKGAVTY I

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00369169. IPI00778394. IPI00808698.
RefSeq	NP_001034698.1. NM_001039609.1.
UniGene	Rn.213503.
3D structure databases
ProteinModelPortal	Q2HWF0.
SMR	Q2HWF0. Positions 1-287, 542-597.
ModBase	Search...
PTM databases
PhosphoSite	Q2HWF0.
Proteomic databases
PaxDb	Q2HWF0.
PRIDE	Q2HWF0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	310839.
KEGG	rno:310839.
UCSC	RGD:1305386. rat.
Organism-specific databases
CTD	54874.
RGD	1305386. Fnbp1l.
Phylogenomic databases
eggNOG	NOG323796.
HOGENOM	HOG000231767.
HOVERGEN	HBG002489.
OrthoDB	EOG4SN1NK.
Gene expression databases
Genevestigator	Q2HWF0.
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
NextBio	662725.

Entry information

Entry name

FBP1L_RAT

Accession

Primary (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 1, 2013
This is version 57 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program