TOCA1_CAEEL
ID TOCA1_CAEEL Reviewed; 592 AA.
AC Q19253; Q8MQ82;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Transducer of Cdc42-dependent actin assembly protein 1 homolog {ECO:0000305};
GN Name=toca-1 {ECO:0000312|WormBase:F09E10.8a};
GN ORFNames=F09E10.8 {ECO:0000312|WormBase:F09E10.8a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH WSP-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=19798448; DOI=10.1371/journal.pgen.1000675;
RA Giuliani C., Troglio F., Bai Z., Patel F.B., Zucconi A., Malabarba M.G.,
RA Disanza A., Stradal T.B., Cassata G., Confalonieri S., Hardin J.D.,
RA Soto M.C., Grant B.D., Scita G.;
RT "Requirements for F-BAR proteins TOCA-1 and TOCA-2 in actin dynamics and
RT membrane trafficking during Caenorhabditis elegans oocyte growth and
RT embryonic epidermal morphogenesis.";
RL PLoS Genet. 5:E1000675-E1000675(2009).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP ALA-100.
RX PubMed=23150597; DOI=10.1534/genetics.112.146589;
RA Chang Y.T., Dranow D., Kuhn J., Meyerzon M., Ngo M., Ratner D.,
RA Warltier K., Starr D.A.;
RT "toca-1 is in a novel pathway that functions in parallel with a SUN-KASH
RT nuclear envelope bridge to move nuclei in Caenorhabditis elegans.";
RL Genetics 193:187-200(2013).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26578656; DOI=10.1093/jmcb/mjv062;
RA Ouellette M.H., Martin E., Lacoste-Caron G., Hamiche K., Jenna S.;
RT "Spatial control of active CDC-42 during collective migration of hypodermal
RT cells in Caenorhabditis elegans.";
RL J. Mol. Cell Biol. 8:313-327(2016).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CDC-42 AND WVE-1, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=25775511; DOI=10.1073/pnas.1418651112;
RA Bai Z., Grant B.D.;
RT "A TOCA/CDC-42/PAR/WAVE functional module required for retrograde endocytic
RT recycling.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E1443-E1452(2015).
CC -!- FUNCTION: Plays a role in protein trafficking, actin organization and
CC embryonic morphogenesis (PubMed:19798448). Potentially acts as cdc-42
CC effector (PubMed:25775511). May play a role in hypodermal P-cell
CC nuclear positioning (PubMed:23150597). Together with toca-2, is
CC required for protein trafficking regulating yolk protein clathrin-
CC mediated endocytosis by oocytes during oogenesis and retrograde
CC recycling and the sorting of recycling endosome cargo proteins such as
CC mig-14 (PubMed:19798448, PubMed:25775511). Also, together with toca-2,
CC controls the distribution of actin at cell junctions (PubMed:19798448,
CC PubMed:26578656). {ECO:0000269|PubMed:19798448,
CC ECO:0000269|PubMed:23150597, ECO:0000269|PubMed:25775511,
CC ECO:0000269|PubMed:26578656}.
CC -!- SUBUNIT: Interacts (via SH3 domain) with wsp-1 (PubMed:19798448).
CC Interacts with cdc-42 and (via SH3 domain) with wve-1
CC (PubMed:25775511). {ECO:0000269|PubMed:19798448,
CC ECO:0000269|PubMed:25775511}.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:19798448,
CC ECO:0000269|PubMed:23150597}. Apical cell membrane
CC {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}; Peripheral
CC membrane protein {ECO:0000269|PubMed:19798448,
CC ECO:0000269|PubMed:25775511}; Cytoplasmic side
CC {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}. Basolateral
CC cell membrane {ECO:0000269|PubMed:19798448,
CC ECO:0000269|PubMed:25775511}; Peripheral membrane protein
CC {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}; Cytoplasmic
CC side {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}.
CC Cytoplasmic vesicle {ECO:0000269|PubMed:19798448}. Cytoplasm
CC {ECO:0000269|PubMed:23150597, ECO:0000269|PubMed:25775511}. Cytoplasm,
CC perinuclear region {ECO:0000269|PubMed:23150597}. Recycling endosome
CC {ECO:0000269|PubMed:25775511}. Note=Co-localizes with ajm-1 at cell
CC junctions (PubMed:19798448). Co-localizes with toca-2, rme-1, cdc-42
CC and wve-1 on recycling endosomes (PubMed:25775511).
CC {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:F09E10.8a};
CC IsoId=Q19253-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F09E10.8b};
CC IsoId=Q19253-2; Sequence=VSP_058522;
CC -!- TISSUE SPECIFICITY: Expressed in the germline and specifically in the
CC gonads. {ECO:0000269|PubMed:19798448}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed in developing embryos.
CC {ECO:0000269|PubMed:19798448}.
CC -!- DISRUPTION PHENOTYPE: Defective endocytosis by occytes characterized by
CC either reduced or non-detectable yolk protein in the oocytes and by an
CC accumulation of aggregated yolk in the pseudocoelomatic space
CC (PubMed:19798448). This is more pronounced in the double knockout with
CC toca-2 where nearly 100% of animals display this phenotype
CC (PubMed:19798448). Double knockout mutants with toca-2 also produce 20%
CC fewer eggs compared to wild-type animals and there is some embryonic
CC lethality whereby the dying embryos display defective morphogenesis
CC including failed epidermal enclosure with extruding gut cells and
CC increased width of the intestinal lumen (PubMed:19798448). This perhaps
CC results from failed intercalation and migration of hypodermal cells and
CC irregular protein trafficking as indicated by an accumulation of the
CC cell junction protein ajm-1 and diffuse localization of actin at cell
CC junctions (PubMed:19798448, PubMed:26578656). These double mutants also
CC demonstrate defective endosomal sorting of recycling cargo proteins
CC such as mig-14 (PubMed:25775511). Double knockown with unc-84 results
CC in defective hypodermal P-cell nuclear positioning with nuclei failing
CC to migrate during larval development and a reduced number of GABA
CC neurons (PubMed:23150597). {ECO:0000269|PubMed:19798448,
CC ECO:0000269|PubMed:23150597, ECO:0000269|PubMed:25775511,
CC ECO:0000269|PubMed:26578656}.
CC -!- SIMILARITY: Belongs to the FNBP1 family. {ECO:0000305}.
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DR EMBL; BX284606; CCD68288.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD68289.1; -; Genomic_DNA.
DR PIR; T15992; T15992.
DR RefSeq; NP_741722.1; NM_171630.6.
DR RefSeq; NP_741723.1; NM_171940.4. [Q19253-1]
DR AlphaFoldDB; Q19253; -.
DR SMR; Q19253; -.
DR IntAct; Q19253; 29.
DR STRING; 6239.F09E10.8a; -.
DR EPD; Q19253; -.
DR PaxDb; Q19253; -.
DR PeptideAtlas; Q19253; -.
DR EnsemblMetazoa; F09E10.8.1; F09E10.8.1; WBGene00017298. [Q19253-1]
DR GeneID; 180492; -.
DR KEGG; cel:CELE_F09E10.8; -.
DR UCSC; F09E10.8a; c. elegans.
DR CTD; 180492; -.
DR WormBase; F09E10.8a; CE27939; WBGene00017298; toca-1. [Q19253-1]
DR WormBase; F09E10.8b; CE30940; WBGene00017298; toca-1. [Q19253-2]
DR eggNOG; KOG3565; Eukaryota.
DR GeneTree; ENSGT00950000183047; -.
DR InParanoid; Q19253; -.
DR OMA; SEGTMAM; -.
DR OrthoDB; 348563at2759; -.
DR PhylomeDB; Q19253; -.
DR Reactome; R-CEL-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q19253; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00017298; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0097708; C:intracellular vesicle; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048613; P:embryonic ectodermal digestive tract morphogenesis; IMP:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:1904703; P:negative regulation of protein localization to adherens junction; IGI:UniProtKB.
DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IMP:UniProtKB.
DR GO; GO:1901046; P:positive regulation of oviposition; IGI:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IGI:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036028; SH3-like_dom_sf.
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; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS51860; REM_1; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Endocytosis; Endosome; Membrane; Reference proteome;
KW SH3 domain.
FT CHAIN 1..592
FT /note="Transducer of Cdc42-dependent actin assembly protein
FT 1 homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437443"
FT DOMAIN 3..267
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 359..436
FT /note="REM-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 527..589
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 343..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 363..441
FT /evidence="ECO:0000255"
FT COMPBIAS 447..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 249..311
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058522"
FT MUTAGEN 100
FT /note="A->V: In yc20; enhances the hypodermal P-cell
FT nuclear migration defect in unc-84 mutants."
FT /evidence="ECO:0000269|PubMed:23150597"
SQ SEQUENCE 592 AA; 65077 MW; 92DB676762F789F0 CRC64;
MNDSCSWDQL WDQQGTLNEY TGKGIDLLER IMAYSKERAS IELEYSSKLK ALSKKTAMKM
KSESELWNSV SYVKGFHDVI AGIVPVATQH ELIAENLKSA VIPFTTQKIA EYRVAKKQLE
SDNSNLGKQL RMVIDEMAKS HKEYVKCYKE TEAAMLKYAK AEKNMDISRL ELEKTKNNYQ
QKCGMLEESK QTYAVMTTKA NEEQSAHYDR KLPQLLDNYK KLHTNRILDT VEILSKCVEA
ESCVNQIIAS CHNDMRRDIG LIDPSRDANL VVENMKSGHP VPQPFVFEDL GHPQDRSSFM
GGGASGPAGS MDGMDATMKK GGTLMSKNGK GVARKQSMHQ KFFGGGTADK KTDSGDYGTL
PPQQRARKIA GKISDLEKEK DRATQSREGV SKMQAAYREN PKLGNPSDCD AQLAQYGHEI
DALSNQIQKF KILLDDVNAQ LGAGGLSATS VGGSDTPPSI RSVSSASSGV TSRVNTINDA
HRTNGGVGGG RRESFSGSNG GSDTDPTING NGHGRDELYE ECSNPNPVLG EAIAQFAFDG
AQDGTIRMEA NEKLWLIEKD EGDGWTRVRK ENNSADGFVP SSYLKVTWFG KV
