CYFIP_CAEEL
ID CYFIP_CAEEL Reviewed; 1262 AA.
AC O44518; Q95YG2;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 4.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Cytoplasmic FMR1-interacting protein homolog;
DE AltName: Full=Gut on exterior protein 2;
GN Name=gex-2 {ECO:0000312|WormBase:F56A11.1};
GN ORFNames=F56A11.1 {ECO:0000312|WormBase:F56A11.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAB70472.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH GEX-3, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=11877381; DOI=10.1101/gad.955702;
RA Soto M.C., Qadota H., Kasuya K., Inoue M., Tsuboi D., Mello C.C.,
RA Kaibuchi K.;
RT "The GEX-2 and GEX-3 proteins are required for tissue morphogenesis and
RT cell migrations in C. elegans.";
RL Genes Dev. 16:620-632(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 [3]
RP FUNCTION, 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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27123983; DOI=10.1371/journal.pgen.1006010;
RA D'Souza S.A., Rajendran L., Bagg R., Barbier L., van Pel D.M., Moshiri H.,
RA Roy P.J.;
RT "The MADD-3 LAMMER kinase interacts with a p38 MAP kinase pathway to
RT regulate the display of the EVA-1 guidance receptor in Caenorhabditis
RT elegans.";
RL PLoS Genet. 12:E1006010-E1006010(2016).
CC -!- FUNCTION: Required for initial steps of body morphogenesis
CC (PubMed:11877381). May play a role in egg laying and yolk protein
CC clatherin-mediated endocytosis by oocytes during oogenesis
CC (PubMed:19798448). Plays a role in the formation of muscle connections,
CC also called muscle arm extensions, between the body wall and the motor
CC axons in the dorsal and ventral cord (PubMed:27123983).
CC {ECO:0000269|PubMed:11877381, ECO:0000269|PubMed:19798448,
CC ECO:0000269|PubMed:27123983}.
CC -!- SUBUNIT: Interacts with gex-3. {ECO:0000269|PubMed:11877381}.
CC -!- INTERACTION:
CC O44518; P55163: gex-3; NbExp=4; IntAct=EBI-1570205, EBI-1570181;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11877381}.
CC Note=Enriched at cell boundaries. {ECO:0000269|PubMed:11877381}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal with cells differentiating, but
CC failing to become organized (PubMed:11877381). The external hypodermal
CC cells fail to spread over and enclose the embryo, but instead cluster
CC on the dorsal side (PubMed:11877381). In one study, animals are viable
CC and there is defective extension of body wall muscle connections or
CC arms towards the ventral nerve cord (PubMed:27123983). In this same
CC study, double knockout with madd-3 results in severe muscle arm
CC extension defects (PubMed:27123983). RNAi-mediated knockdown results in
CC reduced egg laying and in defective endocytosis by oocytes
CC characterized by an accumulation of aggregated yolk protein in the
CC pseudocoelomatic space (PubMed:19798448). {ECO:0000269|PubMed:11877381,
CC ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:27123983}.
CC -!- SIMILARITY: Belongs to the CYFIP family. {ECO:0000255}.
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DR EMBL; AB073209; BAB70472.1; -; mRNA.
DR EMBL; FO080624; CCD65256.1; -; Genomic_DNA.
DR PIR; T32647; T32647.
DR RefSeq; NP_499949.2; NM_067548.4.
DR AlphaFoldDB; O44518; -.
DR SMR; O44518; -.
DR BioGRID; 42046; 4.
DR IntAct; O44518; 1.
DR STRING; 6239.F56A11.1; -.
DR EPD; O44518; -.
DR PaxDb; O44518; -.
DR PeptideAtlas; O44518; -.
DR EnsemblMetazoa; F56A11.1.1; F56A11.1.1; WBGene00001579.
DR GeneID; 176885; -.
DR KEGG; cel:CELE_F56A11.1; -.
DR UCSC; F56A11.1; c. elegans.
DR CTD; 176885; -.
DR WormBase; F56A11.1; CE31351; WBGene00001579; gex-2.
DR eggNOG; KOG3534; Eukaryota.
DR GeneTree; ENSGT00500000044831; -.
DR HOGENOM; CLU_002688_2_1_1; -.
DR InParanoid; O44518; -.
DR OMA; MPKVCKL; -.
DR OrthoDB; 108507at2759; -.
DR PhylomeDB; O44518; -.
DR Reactome; R-CEL-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-CEL-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-9013149; RAC1 GTPase cycle.
DR PRO; PR:O44518; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001579; Expressed in embryo and 4 other tissues.
DR GO; GO:0030054; C:cell junction; IDA:WormBase.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0031209; C:SCAR complex; IDA:WormBase.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0010172; P:embryonic body morphogenesis; IMP:UniProtKB.
DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IMP:UniProtKB.
DR GO; GO:1901046; P:positive regulation of oviposition; IMP:UniProtKB.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR GO; GO:0006417; P:regulation of translation; IBA:GO_Central.
DR InterPro; IPR009828; CYRIA/CYRIB_Rac1-bd.
DR InterPro; IPR008081; Cytoplasmic_FMR1-int.
DR PANTHER; PTHR12195; PTHR12195; 1.
DR Pfam; PF07159; DUF1394; 1.
DR Pfam; PF05994; FragX_IP; 1.
DR PIRSF; PIRSF008153; FMR1_interacting; 1.
DR PRINTS; PR01698; CYTOFMRPINTP.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Reference proteome.
FT CHAIN 1..1262
FT /note="Cytoplasmic FMR1-interacting protein homolog"
FT /id="PRO_0000279713"
FT REGION 519..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1262 AA; 145013 MW; 34FBE7B43260A188 CRC64;
MNANVTVDDA ISNVNLLDTL AIPDDLPDIE ARALPLLYRS NFDTNFEDRS AFVTGIAKYS
EEATRHAQFN DMLSEGLQHA ANMYTWRCCS RAVPMAKSND QPNRTEINEM VVEVLKPEVS
KLGSFMRFTL TAIQRFCEEV RRLCHSEKRR DFVSEAYLLT LGRFINMFAV LDELKNMKAS
IKNDFSTFRR ASQFLTAMSD TQAVHDMQNL SMFLATQNKI KDDLKLQMKT IEGYEELLCD
VVNICAHMYE HQLYLSPNEK HMFVKVIAFS LFLMDGDAAN VAKLDQKKRL SISRLDKIFK
TLEVVPLYGD MQIQPFAFVR RSSHYEPSKW PLSDKESDRC HVNIVEKVQS IRSDHESYVT
QFAKINNEVA ICDRPGNDSE NREITSLALS GIQLLCQWSC AVVETISWKL LNPTNPKDNR
ECPENAEEYE RATRYNYSPA EKTALIQIIA MIKGLQSMLG KTESDMSNST RKCVYVELQA
FIHHTINEPL QKAVKHKKDL LASILQSVKD SISDAGNELN RMTDVKGKKK SSAPKGDSAN
SSSSDIRIPR RTAAPGSTQL YMARTQLESL ISDKLCGGKK ILRKELDSKT IEKISVFLRK
SAHWPALFRL SDSMTEAGEL SQLWFREFYL EMTMGQRIQF PIEMSMPWIL TDYILSCNEP
SLIESALYQL DLYNDAAQYS LFNFNKQFLY DEVEAEVNLC FDQFVYKLSE MVFTHYKQLA
SCMLLDKRFK AEILRSGTMI RSPSAARFES LLQQRHVQLL GRSVDLNRVV SQRVNMALLK
ALDAAIWKFE SEPLSSIVEL DMLIDTNRLC HTLLSDVLHS IAPFDDLFQE ANHAVNSPHG
RITLHVFWEL NYDFVPNFVY NGSTHRFVRA RHVFRKTPAR EKPPQVGQVY YWGSKSLMAA
FMNICNAYSQ CIGTQHLKAI TRLLHYQGIA VILDELLKMT NRLLNDKIRR HVRNVFNMMP
KVCKLPRSDY GSNALLQYYV HHLEAVGKYP ELKSEFCQDL RELGNMIVFC QQLEVALGQE
EAHDLFLAAA YTGTVPQPPA RNAQEQMKQL AKLEDKYSRI HLTEIIDKIS PDDGQAAIAK
DAELMTKERL CCGLNAFENF LVRIKQMLAA DDIWTGGYPT NGVFWIDECV EWYRVYSALQ
FFLCQPTRDD NEVYAEELFG DSLQWGGLTL ITLLGQHRRF EVLDFCYHLH RVNKADGKDE
VISGIRLAKM VERIRRFQLL NNQIFIILEN QLNENNDDPN ERVREFAPPV HPNYANHAAR
RQ
