ID   GEX3_CAEEL              Reviewed;        1141 AA.
AC   P55163; Q19880;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Membrane-associated protein gex-3;
DE   AltName: Full=Gut on exterior protein 3;
GN   Name=gex-3 {ECO:0000312|WormBase:F28D1.10};
GN   ORFNames=F28D1.10 {ECO:0000312|WormBase:F28D1.10};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH GEX-2, 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   INTERACTION WITH ACO-1.
RX   PubMed=11922622; DOI=10.1006/bbrc.2002.6717;
RA   Tsuboi D., Qadota H., Kasuya K., Amano M., Kaibuchi K.;
RT   "Isolation of the interacting molecules with GEX-3 by a novel functional
RT   screening.";
RL   Biochem. Biophys. Res. Commun. 292:697-701(2002).
RN   [4]
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   [5]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=33238150; DOI=10.1016/j.devcel.2020.10.020;
RA   Meng L., Yan D.;
RT   "NLR-1/CASPR Anchors F-Actin to Promote Gap Junction Formation.";
RL   Dev. Cell 55:574-587(2020).
CC   -!- FUNCTION: Rac effector required for tissue morphogenesis, cell
CC       migrations and egg laying (PubMed:11877381). May play a role in egg
CC       laying and in yolk protein clatherin-mediated endocytosis by oocytes
CC       during oogenesis (PubMed:19798448). Plays a role in the formation of
CC       gap junctions between EA and EP endodermal precursor cells in embryos
CC       (PubMed:33238150). {ECO:0000269|PubMed:11877381,
CC       ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:33238150}.
CC   -!- SUBUNIT: Interacts with aco-1, gei-13 and gex-2.
CC       {ECO:0000269|PubMed:11877381, ECO:0000269|PubMed:11922622}.
CC   -!- INTERACTION:
CC       P55163; O44518: gex-2; NbExp=4; IntAct=EBI-1570181, EBI-1570205;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11877381}.
CC       Note=Enriched at cell boundaries.
CC   -!- TISSUE SPECIFICITY: Expressed in neurons.
CC       {ECO:0000269|PubMed:33238150}.
CC   -!- DISRUPTION PHENOTYPE: Embryonic lethality with cells differentiating,
CC       but failing to become organized (PubMed:11877381). External hypodermal
CC       cells fail to spread over and enclose the embryo, but instead cluster
CC       on the dorsal side (PubMed:11877381). RNAi-mediated knockdown results
CC       in 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). RNAi-mediated knockdown
CC       results in abherrent inx-3-positive gap junction formation along the
CC       adjoining membranes of EA and EP endodermal precursor cells at the 16-
CC       24 cell stage of embryogenesis (PubMed:33238150).
CC       {ECO:0000269|PubMed:11877381, ECO:0000269|PubMed:19798448,
CC       ECO:0000269|PubMed:33238150}.
CC   -!- SIMILARITY: Belongs to the HEM-1/HEM-2 family. {ECO:0000305}.
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DR   EMBL; AB073210; BAB70473.1; -; mRNA.
DR   EMBL; BX284604; CAA94604.1; -; Genomic_DNA.
DR   EMBL; Z70682; CAA94604.1; JOINED; Genomic_DNA.
DR   PIR; T20611; T20611.
DR   RefSeq; NP_502368.1; NM_069967.5.
DR   AlphaFoldDB; P55163; -.
DR   SMR; P55163; -.
DR   BioGRID; 43284; 38.
DR   IntAct; P55163; 1.
DR   STRING; 6239.F28D1.10; -.
DR   EPD; P55163; -.
DR   PaxDb; P55163; -.
DR   PeptideAtlas; P55163; -.
DR   EnsemblMetazoa; F28D1.10.1; F28D1.10.1; WBGene00001580.
DR   GeneID; 178191; -.
DR   KEGG; cel:CELE_F28D1.10; -.
DR   UCSC; F28D1.10; c. elegans.
DR   CTD; 178191; -.
DR   WormBase; F28D1.10; CE05750; WBGene00001580; gex-3.
DR   eggNOG; KOG1917; Eukaryota.
DR   GeneTree; ENSGT00390000016619; -.
DR   HOGENOM; CLU_004450_0_0_1; -.
DR   InParanoid; P55163; -.
DR   OMA; VGMVMYN; -.
DR   OrthoDB; 138196at2759; -.
DR   PhylomeDB; P55163; -.
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:P55163; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00001580; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0030054; C:cell junction; IDA:WormBase.
DR   GO; GO:0031209; C:SCAR complex; IDA:WormBase.
DR   GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
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:0048668; P:collateral sprouting; IMP:UniProtKB.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0010172; P:embryonic body morphogenesis; IMP:UniProtKB.
DR   GO; GO:0048613; P:embryonic ectodermal digestive tract morphogenesis; IMP:UniProtKB.
DR   GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR   GO; GO:0018991; P:oviposition; IMP:UniProtKB.
DR   GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IMP:UniProtKB.
DR   GO; GO:1903598; P:positive regulation of gap junction assembly; IMP:UniProtKB.
DR   GO; GO:1901046; P:positive regulation of oviposition; IMP:UniProtKB.
DR   GO; GO:1902474; P:positive regulation of protein localization to synapse; IMP:UniProtKB.
DR   InterPro; IPR019137; Nck-associated_protein-1.
DR   PANTHER; PTHR12093; PTHR12093; 1.
DR   Pfam; PF09735; Nckap1; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Developmental protein; Reference proteome.
FT   CHAIN           1..1141
FT                   /note="Membrane-associated protein gex-3"
FT                   /id="PRO_0000216177"
SQ   SEQUENCE   1141 AA;  129919 MW;  FFCD8A74A5AED610 CRC64;
     MAYKDARQVK IAEKLVILND RAAGMMTRIY NIKKSSGDSK VKPQFLSDKK MEGAIKHIVR
     KFPVVDCRSN SSTFEYVQEK STEITKSLSL YYYTFADILD LKDHIMQVLT TMESCQCQLD
     VTLNYDLTTS YLNLVVHLVT MMILLSRIED RKAVLGLFNA AYDLQHGQSE ASFPRLGQMI
     LDYENPLKKL HEDLGPLNRL IYSALSSVTH TYQRRNKTAD SWRTSNVFSL TAAPAQILYA
     AQTETIACEY LSLDVIDRWI VFCGTVCHST LLNDDNIRHM WQLALQMNLC LRVFRDETFI
     VHQEIQAFLE SSKEKSKRLQ DVKDAFNHAS VTAVAVHADR RRFLRSSLRE LSLLLRDQPG
     LLGPKILYVW MALGAGRDEV IWLLRHQVEV PAISKKGSRM VEELVDRQLP ELLFYMLELR
     DLVTKYYAVI QRYYLQYVSS YDSIVVSEEI NQANGLTQEE AVLLTDFANE IGNINSDTDL
     RALRLDWFRF QAWTSAARSH FQLSRHKKLA IYMNTSVFHL KMIDLQDEML RETSDLSLYC
     FYPKLAEKHW LNCLQLPAQA RYVLSFARLA AHFTSALHDM CPEEKAFITE KALAQCNSVI
     EETCKQLSYI LEKVAEHEFG LAYQMTPSAV AVRVVAQVVQ QKGSGKAAAA AAAAARDYFI
     AGEESYRVDR QALTMPDKLQ TTLLEISAAL GAHRQIYVAD HTFAPRTYLA QSLETKFVEL
     LHGMFWEGQP HASNPKRPSE MLLALQAYMT VLQNLDTAIS VDISNTMQTT LLQQTQLVDS
     KNKDTIAALY TKWYLEVLLR RASSGHMVWS EHLRTMLSSG QEQLSFMPDH YSDPQELRAL
     VQIIGPYGVK LMTERLIWHV ASQIMEMSKI VATYKDALQI ARSNFDNAEK MKDVLNLLSV
     EPKDKKTPNA TCAADAILQR TIIIGQICLF RDALHDALRH IVESKLPFLQ ASFDMLYHNL
     DDVDKVKIGE MSAAMGVTGP VDMSLVNAVR AQNPNIHPQE HYVNSCLLMV AVAICIPRIG
     MSDLSSYKPS IQASLNNSHC VPMAINTIGS ALFHLHEQND IQSRMKEFLA LASSGILRTI
     HERDNSRQIS DDVLRSHTTL YIILEQMVRK NRWLSMDVLE TCFPYNLVRT AYQQCYEADA
     Q