Full text data of FNBP1L
FNBP1L
(C1orf39, TOCA1)
[Confidence: low (only semi-automatic identification from reviews)]
Formin-binding protein 1-like (Transducer of Cdc42-dependent actin assembly protein 1; Toca-1)
Formin-binding protein 1-like (Transducer of Cdc42-dependent actin assembly protein 1; Toca-1)
UniProt
Q5T0N5
ID FBP1L_HUMAN Reviewed; 605 AA.
AC Q5T0N5; Q5T0N6; Q6B097; Q6P653; Q6R4Q4; Q9NXG1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 28-NOV-2006, sequence version 2.
DT 22-JAN-2014, entry version 92.
DE RecName: Full=Formin-binding protein 1-like;
DE AltName: Full=Transducer of Cdc42-dependent actin assembly protein 1;
DE Short=Toca-1;
GN Name=FNBP1L; Synonyms=C1orf39, TOCA1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH
RP CDC42 AND WASL, AND MUTAGENESIS OF 441-MET--ASP-443 AND TRP-576.
RC TISSUE=Fetal brain;
RX PubMed=15260990; DOI=10.1016/j.cell.2004.06.027;
RA Ho H.-Y.H., Rohatgi R., Lebensohn A.M., Ma L., Li J., Gygi S.P.,
RA Kirschner M.W.;
RT "Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-
RT WASP-WIP complex.";
RL Cell 118:203-216(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 134-605 (ISOFORM 4), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 208-605 (ISOFORM 3).
RC TISSUE=Lung, and Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 200-605 (ISOFORM 3).
RC TISSUE=Hepatoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP FUNCTION, AND INTERACTION WITH DNM1 AND WASL.
RX PubMed=16326391; DOI=10.1016/j.devcel.2005.11.005;
RA Itoh T., Erdmann K.S., Roux A., Habermann B., Werner H.,
RA De Camilli P.;
RT "Dynamin and the actin cytoskeleton cooperatively regulate plasma
RT membrane invagination by BAR and F-BAR proteins.";
RL Dev. Cell 9:791-804(2005).
RN [6]
RP INTERACTION WITH DAAM1; DIAPH1 AND DIAPH2.
RX PubMed=16630611; DOI=10.1016/j.yexcr.2006.03.013;
RA Aspenstroem P., Richnau N., Johansson A.-S.;
RT "The diaphanous-related formin DAAM1 collaborates with the Rho GTPases
RT RhoA and Cdc42, CIP4 and Src in regulating cell morphogenesis and
RT actin dynamics.";
RL Exp. Cell Res. 312:2180-2194(2006).
RN [7]
RP INTERACTION WITH DNM2 AND WASL.
RX PubMed=16418535; DOI=10.1083/jcb.200508091;
RA Tsujita K., Suetsugu S., Sasaki N., Furutani M., Oikawa T.,
RA Takenawa T.;
RT "Coordination between the actin cytoskeleton and membrane deformation
RT by a novel membrane tubulation domain of PCH proteins is involved in
RT endocytosis.";
RL J. Cell Biol. 172:269-279(2006).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=16757518; DOI=10.1242/jcs.03005;
RA Kovacs E.M., Makar R.S., Gertler F.B.;
RT "Tuba stimulates intracellular N-WASP-dependent actin assembly.";
RL J. Cell Sci. 119:2715-2726(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-488 AND
RP SER-501, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP FUNCTION IN AUTOPHAGY, AND INTERACTION WITH ATG3.
RX PubMed=19342671; DOI=10.4049/jimmunol.0803050;
RA Huett A., Ng A., Cao Z., Kuballa P., Komatsu M., Daly M.J.,
RA Podolsky D.K., Xavier R.J.;
RT "A novel hybrid yeast-human network analysis reveals an essential role
RT for FNBP1L in antibacterial autophagy.";
RL J. Immunol. 182:4917-4930(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-488 AND
RP SER-501, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-488 AND
RP SER-501, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Required to coordinate membrane tubulation with
CC reorganization of the actin cytoskeleton during endocytosis. May
CC bind to lipids such as phosphatidylinositol 4,5-bisphosphate and
CC phosphatidylserine and promote membrane invagination and the
CC formation of tubules. Also promotes CDC42-induced actin
CC polymerization by activating the WASL/N-WASP-WASPIP/WIP complex,
CC the predominant form of WASL/N-WASP in cells. Actin polymerization
CC may promote the fission of membrane tubules to form endocytic
CC vesicles. Essential for autophagy of intracellular bacterial
CC pathogens.
CC -!- SUBUNIT: Homodimerizes, the dimers can polymerize end-to-end to
CC form filamentous structures (By similarity). Interacts with GTP-
CC bound CDC42. Interacts with DAAM1, DIAPH1, DIAPH2, DNM1, DNM2 and
CC WASL/N-WASP. Interacts with ATG3.
CC -!- INTERACTION:
CC Q9Y4D1:DAAM1; NbExp=2; IntAct=EBI-714058, EBI-2817289;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton (By
CC similarity). Cytoplasm, cell cortex (By similarity). Cytoplasmic
CC vesicle (By similarity). Cell membrane; Peripheral membrane
CC protein; Cytoplasmic side (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q5T0N5-1; Sequence=Displayed;
CC Note=Gene prediction based on EST data;
CC Name=2;
CC IsoId=Q5T0N5-2; Sequence=VSP_021710;
CC Note=Gene prediction based on EST data;
CC Name=3;
CC IsoId=Q5T0N5-3; Sequence=VSP_021709;
CC Name=4;
CC IsoId=Q5T0N5-4; Sequence=VSP_021709, VSP_021711;
CC Note=Gene prediction based on EST data;
CC Name=5;
CC IsoId=Q5T0N5-5; Sequence=VSP_021710, VSP_021711;
CC Note=Gene prediction based on EST data. No experimental
CC confirmation available;
CC -!- DOMAIN: The F-BAR domain binds the phospholipid membrane with its
CC concave surface. The end-to-end polymerization of dimers of these
CC domains provides a curved surface that fits best membranes with
CC around 600 A diameter, and may drive tubulation (By similarity).
CC -!- SIMILARITY: Belongs to the FNBP1 family.
CC -!- SIMILARITY: Contains 1 FCH domain.
CC -!- SIMILARITY: Contains 1 REM (Hr1) repeat.
CC -!- SIMILARITY: Contains 1 SH3 domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91051.1; Type=Erroneous initiation;
CC Sequence=CAI18954.1; Type=Erroneous gene model prediction;
CC Sequence=CAI18981.1; Type=Erroneous gene model prediction;
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DR EMBL; AY514449; AAR98814.1; -; mRNA.
DR EMBL; AL109613; CAI18952.1; -; Genomic_DNA.
DR EMBL; AC095034; CAI18952.1; JOINED; Genomic_DNA.
DR EMBL; AL512651; CAI18952.1; JOINED; Genomic_DNA.
DR EMBL; AL109613; CAI18953.1; -; Genomic_DNA.
DR EMBL; AC095034; CAI18953.1; JOINED; Genomic_DNA.
DR EMBL; AL512651; CAI18953.1; JOINED; Genomic_DNA.
DR EMBL; AL109613; CAI18954.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC095034; CAI18954.1; JOINED; Genomic_DNA.
DR EMBL; AL512651; CAI18954.1; JOINED; Genomic_DNA.
DR EMBL; AL512651; CAI18979.1; -; Genomic_DNA.
DR EMBL; AC095034; CAI18979.1; JOINED; Genomic_DNA.
DR EMBL; AL109613; CAI18979.1; JOINED; Genomic_DNA.
DR EMBL; AL512651; CAI18980.1; -; Genomic_DNA.
DR EMBL; AC095034; CAI18980.1; JOINED; Genomic_DNA.
DR EMBL; AL109613; CAI18980.1; JOINED; Genomic_DNA.
DR EMBL; AL512651; CAI18981.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC095034; CAI18981.1; JOINED; Genomic_DNA.
DR EMBL; AL109613; CAI18981.1; JOINED; Genomic_DNA.
DR EMBL; BC062477; AAH62477.1; -; mRNA.
DR EMBL; BC074891; AAH74891.1; -; mRNA.
DR EMBL; BC074892; AAH74892.1; -; mRNA.
DR EMBL; AK000282; BAA91051.1; ALT_INIT; mRNA.
DR RefSeq; NP_001020119.1; NM_001024948.2.
DR RefSeq; NP_001157945.1; NM_001164473.2.
DR RefSeq; NP_060207.2; NM_017737.4.
DR UniGene; Hs.134060; -.
DR ProteinModelPortal; Q5T0N5; -.
DR SMR; Q5T0N5; 10-287, 393-484, 542-597.
DR IntAct; Q5T0N5; 6.
DR MINT; MINT-1424364; -.
DR STRING; 9606.ENSP00000271234; -.
DR PhosphoSite; Q5T0N5; -.
DR DMDM; 118572313; -.
DR PaxDb; Q5T0N5; -.
DR PRIDE; Q5T0N5; -.
DR Ensembl; ENST00000260506; ENSP00000260506; ENSG00000137942.
DR Ensembl; ENST00000370253; ENSP00000359275; ENSG00000137942.
DR Ensembl; ENST00000370256; ENSP00000359278; ENSG00000137942.
DR GeneID; 54874; -.
DR KEGG; hsa:54874; -.
DR CTD; 54874; -.
DR GeneCards; GC01P093913; -.
DR HGNC; HGNC:20851; FNBP1L.
DR MIM; 608848; gene.
DR neXtProt; NX_Q5T0N5; -.
DR PharmGKB; PA128394675; -.
DR eggNOG; NOG323796; -.
DR HOGENOM; HOG000231767; -.
DR HOVERGEN; HBG002489; -.
DR OrthoDB; EOG780RQK; -.
DR GeneWiki; FNBP1L; -.
DR GenomeRNAi; 54874; -.
DR NextBio; 57799; -.
DR PRO; PR:Q5T0N5; -.
DR ArrayExpress; Q5T0N5; -.
DR Bgee; Q5T0N5; -.
DR CleanEx; HS_FNBP1L; -.
DR Genevestigator; Q5T0N5; -.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:BHF-UCL.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0072583; P:clathrin-mediated endocytosis; IDA:BHF-UCL.
DR GO; GO:0006900; P:membrane budding; IDA:BHF-UCL.
DR GO; GO:0010324; P:membrane invagination; IDA:BHF-UCL.
DR GO; GO:0097320; P:membrane tubulation; IDA:BHF-UCL.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IDA:BHF-UCL.
DR GO; GO:0030050; P:vesicle transport along actin filament; IDA:BHF-UCL.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50133; FCH; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Cell membrane; Coiled coil;
KW Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Endocytosis; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1 605 Formin-binding protein 1-like.
FT /FTId=PRO_0000261434.
FT DOMAIN 1 65 FCH.
FT REPEAT 409 484 REM.
FT DOMAIN 538 599 SH3.
FT REGION 1 287 F-BAR domain (By similarity).
FT REGION 245 535 Interaction with CDC42.
FT REGION 522 605 Interaction with DNM1.
FT REGION 541 605 Interaction with DAAM1, DIAPH1 and
FT DIAPH2.
FT REGION 541 597 Interaction with DNM2 and WASL.
FT COILED 66 258 By similarity.
FT COILED 392 484 By similarity.
FT SITE 165 165 Mediates end-to-end attachment of dimers
FT (By similarity).
FT MOD_RES 295 295 Phosphoserine.
FT MOD_RES 488 488 Phosphoserine.
FT MOD_RES 501 501 Phosphoserine.
FT VAR_SEQ 331 388 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_021709.
FT VAR_SEQ 384 388 Missing (in isoform 2 and isoform 5).
FT /FTId=VSP_021710.
FT VAR_SEQ 605 605 S -> AVTYI (in isoform 4 and isoform 5).
FT /FTId=VSP_021711.
FT MUTAGEN 441 443 MGD->IST: Impairs interaction with CDC42
FT and reduces CDC42-induced actin assembly.
FT MUTAGEN 576 576 W->K: Impairs interaction with WASL and
FT reduces CDC42-induced actin assembly.
SQ SEQUENCE 605 AA; 69977 MW; 9C8576E8FAA3B626 CRC64;
MSWGTELWDQ FDSLDKHTQW GIDFLERYAK FVKERIEIEQ NYAKQLRNLV KKYCPKRSSK
DEEPRFTSCV AFFNILNELN DYAGQREVVA EEMAHRVYGE LMRYAHDLKT ERKMHLQEGR
KAQQYLDMCW KQMDNSKKKF ERECREAEKA QQSYERLDND TNATKADVEK AKQQLNLRTH
MADENKNEYA AQLQNFNGEQ HKHFYVVIPQ IYKQLQEMDE RRTIKLSECY RGFADSERKV
IPIISKCLEG MILAAKSVDE RRDSQMVVDS FKSGFEPPGD FPFEDYSQHI YRTISDGTIS
ASKQESGKMD AKTTVGKAKG KLWLFGKKPK PQSPPLTPTS LFTSSTPNGS QFLTFSIEPV
HYCMNEIKTG KPRIPSFRSL KRGVSLIMGP ALEDFSHLPP EQRRKKLQQR IDELNRELQK
ESDQKDALNK MKDVYEKNPQ MGDPGSLQPK LAETMNNIDR LRMEIHKNEA WLSEVEGKTG
GRGDRRHSSD INHLVTQGRE SPEGSYTDDA NQEVRGPPQQ HGHHNEFDDE FEDDDPLPAI
GHCKAIYPFD GHNEGTLAMK EGEVLYIIEE DKGDGWTRAR RQNGEEGYVP TSYIDVTLEK
NSKGS
//
ID FBP1L_HUMAN Reviewed; 605 AA.
AC Q5T0N5; Q5T0N6; Q6B097; Q6P653; Q6R4Q4; Q9NXG1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 28-NOV-2006, sequence version 2.
DT 22-JAN-2014, entry version 92.
DE RecName: Full=Formin-binding protein 1-like;
DE AltName: Full=Transducer of Cdc42-dependent actin assembly protein 1;
DE Short=Toca-1;
GN Name=FNBP1L; Synonyms=C1orf39, TOCA1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH
RP CDC42 AND WASL, AND MUTAGENESIS OF 441-MET--ASP-443 AND TRP-576.
RC TISSUE=Fetal brain;
RX PubMed=15260990; DOI=10.1016/j.cell.2004.06.027;
RA Ho H.-Y.H., Rohatgi R., Lebensohn A.M., Ma L., Li J., Gygi S.P.,
RA Kirschner M.W.;
RT "Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-
RT WASP-WIP complex.";
RL Cell 118:203-216(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 134-605 (ISOFORM 4), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 208-605 (ISOFORM 3).
RC TISSUE=Lung, and Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 200-605 (ISOFORM 3).
RC TISSUE=Hepatoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP FUNCTION, AND INTERACTION WITH DNM1 AND WASL.
RX PubMed=16326391; DOI=10.1016/j.devcel.2005.11.005;
RA Itoh T., Erdmann K.S., Roux A., Habermann B., Werner H.,
RA De Camilli P.;
RT "Dynamin and the actin cytoskeleton cooperatively regulate plasma
RT membrane invagination by BAR and F-BAR proteins.";
RL Dev. Cell 9:791-804(2005).
RN [6]
RP INTERACTION WITH DAAM1; DIAPH1 AND DIAPH2.
RX PubMed=16630611; DOI=10.1016/j.yexcr.2006.03.013;
RA Aspenstroem P., Richnau N., Johansson A.-S.;
RT "The diaphanous-related formin DAAM1 collaborates with the Rho GTPases
RT RhoA and Cdc42, CIP4 and Src in regulating cell morphogenesis and
RT actin dynamics.";
RL Exp. Cell Res. 312:2180-2194(2006).
RN [7]
RP INTERACTION WITH DNM2 AND WASL.
RX PubMed=16418535; DOI=10.1083/jcb.200508091;
RA Tsujita K., Suetsugu S., Sasaki N., Furutani M., Oikawa T.,
RA Takenawa T.;
RT "Coordination between the actin cytoskeleton and membrane deformation
RT by a novel membrane tubulation domain of PCH proteins is involved in
RT endocytosis.";
RL J. Cell Biol. 172:269-279(2006).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=16757518; DOI=10.1242/jcs.03005;
RA Kovacs E.M., Makar R.S., Gertler F.B.;
RT "Tuba stimulates intracellular N-WASP-dependent actin assembly.";
RL J. Cell Sci. 119:2715-2726(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-488 AND
RP SER-501, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP FUNCTION IN AUTOPHAGY, AND INTERACTION WITH ATG3.
RX PubMed=19342671; DOI=10.4049/jimmunol.0803050;
RA Huett A., Ng A., Cao Z., Kuballa P., Komatsu M., Daly M.J.,
RA Podolsky D.K., Xavier R.J.;
RT "A novel hybrid yeast-human network analysis reveals an essential role
RT for FNBP1L in antibacterial autophagy.";
RL J. Immunol. 182:4917-4930(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-488 AND
RP SER-501, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-488 AND
RP SER-501, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Required to coordinate membrane tubulation with
CC reorganization of the actin cytoskeleton during endocytosis. May
CC bind to lipids such as phosphatidylinositol 4,5-bisphosphate and
CC phosphatidylserine and promote membrane invagination and the
CC formation of tubules. Also promotes CDC42-induced actin
CC polymerization by activating the WASL/N-WASP-WASPIP/WIP complex,
CC the predominant form of WASL/N-WASP in cells. Actin polymerization
CC may promote the fission of membrane tubules to form endocytic
CC vesicles. Essential for autophagy of intracellular bacterial
CC pathogens.
CC -!- SUBUNIT: Homodimerizes, the dimers can polymerize end-to-end to
CC form filamentous structures (By similarity). Interacts with GTP-
CC bound CDC42. Interacts with DAAM1, DIAPH1, DIAPH2, DNM1, DNM2 and
CC WASL/N-WASP. Interacts with ATG3.
CC -!- INTERACTION:
CC Q9Y4D1:DAAM1; NbExp=2; IntAct=EBI-714058, EBI-2817289;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton (By
CC similarity). Cytoplasm, cell cortex (By similarity). Cytoplasmic
CC vesicle (By similarity). Cell membrane; Peripheral membrane
CC protein; Cytoplasmic side (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q5T0N5-1; Sequence=Displayed;
CC Note=Gene prediction based on EST data;
CC Name=2;
CC IsoId=Q5T0N5-2; Sequence=VSP_021710;
CC Note=Gene prediction based on EST data;
CC Name=3;
CC IsoId=Q5T0N5-3; Sequence=VSP_021709;
CC Name=4;
CC IsoId=Q5T0N5-4; Sequence=VSP_021709, VSP_021711;
CC Note=Gene prediction based on EST data;
CC Name=5;
CC IsoId=Q5T0N5-5; Sequence=VSP_021710, VSP_021711;
CC Note=Gene prediction based on EST data. No experimental
CC confirmation available;
CC -!- DOMAIN: The F-BAR domain binds the phospholipid membrane with its
CC concave surface. The end-to-end polymerization of dimers of these
CC domains provides a curved surface that fits best membranes with
CC around 600 A diameter, and may drive tubulation (By similarity).
CC -!- SIMILARITY: Belongs to the FNBP1 family.
CC -!- SIMILARITY: Contains 1 FCH domain.
CC -!- SIMILARITY: Contains 1 REM (Hr1) repeat.
CC -!- SIMILARITY: Contains 1 SH3 domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91051.1; Type=Erroneous initiation;
CC Sequence=CAI18954.1; Type=Erroneous gene model prediction;
CC Sequence=CAI18981.1; Type=Erroneous gene model prediction;
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DR EMBL; AY514449; AAR98814.1; -; mRNA.
DR EMBL; AL109613; CAI18952.1; -; Genomic_DNA.
DR EMBL; AC095034; CAI18952.1; JOINED; Genomic_DNA.
DR EMBL; AL512651; CAI18952.1; JOINED; Genomic_DNA.
DR EMBL; AL109613; CAI18953.1; -; Genomic_DNA.
DR EMBL; AC095034; CAI18953.1; JOINED; Genomic_DNA.
DR EMBL; AL512651; CAI18953.1; JOINED; Genomic_DNA.
DR EMBL; AL109613; CAI18954.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC095034; CAI18954.1; JOINED; Genomic_DNA.
DR EMBL; AL512651; CAI18954.1; JOINED; Genomic_DNA.
DR EMBL; AL512651; CAI18979.1; -; Genomic_DNA.
DR EMBL; AC095034; CAI18979.1; JOINED; Genomic_DNA.
DR EMBL; AL109613; CAI18979.1; JOINED; Genomic_DNA.
DR EMBL; AL512651; CAI18980.1; -; Genomic_DNA.
DR EMBL; AC095034; CAI18980.1; JOINED; Genomic_DNA.
DR EMBL; AL109613; CAI18980.1; JOINED; Genomic_DNA.
DR EMBL; AL512651; CAI18981.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC095034; CAI18981.1; JOINED; Genomic_DNA.
DR EMBL; AL109613; CAI18981.1; JOINED; Genomic_DNA.
DR EMBL; BC062477; AAH62477.1; -; mRNA.
DR EMBL; BC074891; AAH74891.1; -; mRNA.
DR EMBL; BC074892; AAH74892.1; -; mRNA.
DR EMBL; AK000282; BAA91051.1; ALT_INIT; mRNA.
DR RefSeq; NP_001020119.1; NM_001024948.2.
DR RefSeq; NP_001157945.1; NM_001164473.2.
DR RefSeq; NP_060207.2; NM_017737.4.
DR UniGene; Hs.134060; -.
DR ProteinModelPortal; Q5T0N5; -.
DR SMR; Q5T0N5; 10-287, 393-484, 542-597.
DR IntAct; Q5T0N5; 6.
DR MINT; MINT-1424364; -.
DR STRING; 9606.ENSP00000271234; -.
DR PhosphoSite; Q5T0N5; -.
DR DMDM; 118572313; -.
DR PaxDb; Q5T0N5; -.
DR PRIDE; Q5T0N5; -.
DR Ensembl; ENST00000260506; ENSP00000260506; ENSG00000137942.
DR Ensembl; ENST00000370253; ENSP00000359275; ENSG00000137942.
DR Ensembl; ENST00000370256; ENSP00000359278; ENSG00000137942.
DR GeneID; 54874; -.
DR KEGG; hsa:54874; -.
DR CTD; 54874; -.
DR GeneCards; GC01P093913; -.
DR HGNC; HGNC:20851; FNBP1L.
DR MIM; 608848; gene.
DR neXtProt; NX_Q5T0N5; -.
DR PharmGKB; PA128394675; -.
DR eggNOG; NOG323796; -.
DR HOGENOM; HOG000231767; -.
DR HOVERGEN; HBG002489; -.
DR OrthoDB; EOG780RQK; -.
DR GeneWiki; FNBP1L; -.
DR GenomeRNAi; 54874; -.
DR NextBio; 57799; -.
DR PRO; PR:Q5T0N5; -.
DR ArrayExpress; Q5T0N5; -.
DR Bgee; Q5T0N5; -.
DR CleanEx; HS_FNBP1L; -.
DR Genevestigator; Q5T0N5; -.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:BHF-UCL.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0072583; P:clathrin-mediated endocytosis; IDA:BHF-UCL.
DR GO; GO:0006900; P:membrane budding; IDA:BHF-UCL.
DR GO; GO:0010324; P:membrane invagination; IDA:BHF-UCL.
DR GO; GO:0097320; P:membrane tubulation; IDA:BHF-UCL.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IDA:BHF-UCL.
DR GO; GO:0030050; P:vesicle transport along actin filament; IDA:BHF-UCL.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50133; FCH; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Cell membrane; Coiled coil;
KW Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Endocytosis; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1 605 Formin-binding protein 1-like.
FT /FTId=PRO_0000261434.
FT DOMAIN 1 65 FCH.
FT REPEAT 409 484 REM.
FT DOMAIN 538 599 SH3.
FT REGION 1 287 F-BAR domain (By similarity).
FT REGION 245 535 Interaction with CDC42.
FT REGION 522 605 Interaction with DNM1.
FT REGION 541 605 Interaction with DAAM1, DIAPH1 and
FT DIAPH2.
FT REGION 541 597 Interaction with DNM2 and WASL.
FT COILED 66 258 By similarity.
FT COILED 392 484 By similarity.
FT SITE 165 165 Mediates end-to-end attachment of dimers
FT (By similarity).
FT MOD_RES 295 295 Phosphoserine.
FT MOD_RES 488 488 Phosphoserine.
FT MOD_RES 501 501 Phosphoserine.
FT VAR_SEQ 331 388 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_021709.
FT VAR_SEQ 384 388 Missing (in isoform 2 and isoform 5).
FT /FTId=VSP_021710.
FT VAR_SEQ 605 605 S -> AVTYI (in isoform 4 and isoform 5).
FT /FTId=VSP_021711.
FT MUTAGEN 441 443 MGD->IST: Impairs interaction with CDC42
FT and reduces CDC42-induced actin assembly.
FT MUTAGEN 576 576 W->K: Impairs interaction with WASL and
FT reduces CDC42-induced actin assembly.
SQ SEQUENCE 605 AA; 69977 MW; 9C8576E8FAA3B626 CRC64;
MSWGTELWDQ FDSLDKHTQW GIDFLERYAK FVKERIEIEQ NYAKQLRNLV KKYCPKRSSK
DEEPRFTSCV AFFNILNELN DYAGQREVVA EEMAHRVYGE LMRYAHDLKT ERKMHLQEGR
KAQQYLDMCW KQMDNSKKKF ERECREAEKA QQSYERLDND TNATKADVEK AKQQLNLRTH
MADENKNEYA AQLQNFNGEQ HKHFYVVIPQ IYKQLQEMDE RRTIKLSECY RGFADSERKV
IPIISKCLEG MILAAKSVDE RRDSQMVVDS FKSGFEPPGD FPFEDYSQHI YRTISDGTIS
ASKQESGKMD AKTTVGKAKG KLWLFGKKPK PQSPPLTPTS LFTSSTPNGS QFLTFSIEPV
HYCMNEIKTG KPRIPSFRSL KRGVSLIMGP ALEDFSHLPP EQRRKKLQQR IDELNRELQK
ESDQKDALNK MKDVYEKNPQ MGDPGSLQPK LAETMNNIDR LRMEIHKNEA WLSEVEGKTG
GRGDRRHSSD INHLVTQGRE SPEGSYTDDA NQEVRGPPQQ HGHHNEFDDE FEDDDPLPAI
GHCKAIYPFD GHNEGTLAMK EGEVLYIIEE DKGDGWTRAR RQNGEEGYVP TSYIDVTLEK
NSKGS
//
MIM
608848
*RECORD*
*FIELD* NO
608848
*FIELD* TI
*608848 TRANSDUCER OF CDC42-DEPENDENT ACTIN ASSEMBLY 1
;;TOCA1;;
CHROMOSOME 1 OPEN READING FRAME 39; C1ORF39
read more*FIELD* TX
CLONING
An important signaling pathway to the actin cytoskeleton links the Rho
family GTPase CDC42 (116952) to the actin-nucleating Arp2/3 complex (see
604221) through N-WASP (605056). However, these components are not
sufficient to mediate CDC42-induced actin polymerization in a
physiologic context. Ho et al. (2004) biochemically purified bovine
Toca1 as an essential component of the Cdc42 pathway. By sequence
analysis and PCR of fetal brain cDNA, they cloned human TOCA1. The
deduced 547-amino acid TOCA1 protein belongs to the evolutionarily
conserved PCH protein family, which includes CIP4 (604504) and FBP17
(606191). Like other members of this family, TOCA1 contains an
N-terminal FCH domain, 2 coiled-coil regions, one of which forms an HR1
domain, and a C-terminal SH3 domain.
GENE FUNCTION
Ho et al. (2004) showed that TOCA1 binds both N-WASP and CDC42. They
found that TOCA1 promotes CDC42-induced actin nucleation by activating
the N-WASP-WIP (602357) complex, the predominant form of N-WASP in
cells. They concluded that the cooperative actions of 2 distinct CDC42
effectors, the N-WASP-WIP complex and TOCA1, are required for
CDC42-induced actin assembly.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the TOCA1
gene to chromosome 1 (TMAP WI-20617).
*FIELD* RF
1. Ho, H.-Y. H.; Rohatgi, R.; Lebensohn, A. M.; Ma, L.; Li, J.; Gygi,
S. P.; Kirschner, M. W.: Toca-1 mediates Cdc42-dependent actin nucleation
by activating the N-WASP-WIP complex. Cell 118: 203-216, 2004.
*FIELD* CD
Stylianos E. Antonarakis: 8/17/2004
*FIELD* ED
mgross: 08/17/2004
*RECORD*
*FIELD* NO
608848
*FIELD* TI
*608848 TRANSDUCER OF CDC42-DEPENDENT ACTIN ASSEMBLY 1
;;TOCA1;;
CHROMOSOME 1 OPEN READING FRAME 39; C1ORF39
read more*FIELD* TX
CLONING
An important signaling pathway to the actin cytoskeleton links the Rho
family GTPase CDC42 (116952) to the actin-nucleating Arp2/3 complex (see
604221) through N-WASP (605056). However, these components are not
sufficient to mediate CDC42-induced actin polymerization in a
physiologic context. Ho et al. (2004) biochemically purified bovine
Toca1 as an essential component of the Cdc42 pathway. By sequence
analysis and PCR of fetal brain cDNA, they cloned human TOCA1. The
deduced 547-amino acid TOCA1 protein belongs to the evolutionarily
conserved PCH protein family, which includes CIP4 (604504) and FBP17
(606191). Like other members of this family, TOCA1 contains an
N-terminal FCH domain, 2 coiled-coil regions, one of which forms an HR1
domain, and a C-terminal SH3 domain.
GENE FUNCTION
Ho et al. (2004) showed that TOCA1 binds both N-WASP and CDC42. They
found that TOCA1 promotes CDC42-induced actin nucleation by activating
the N-WASP-WIP (602357) complex, the predominant form of N-WASP in
cells. They concluded that the cooperative actions of 2 distinct CDC42
effectors, the N-WASP-WIP complex and TOCA1, are required for
CDC42-induced actin assembly.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the TOCA1
gene to chromosome 1 (TMAP WI-20617).
*FIELD* RF
1. Ho, H.-Y. H.; Rohatgi, R.; Lebensohn, A. M.; Ma, L.; Li, J.; Gygi,
S. P.; Kirschner, M. W.: Toca-1 mediates Cdc42-dependent actin nucleation
by activating the N-WASP-WIP complex. Cell 118: 203-216, 2004.
*FIELD* CD
Stylianos E. Antonarakis: 8/17/2004
*FIELD* ED
mgross: 08/17/2004