EAT20_CAEEL
ID EAT20_CAEEL Reviewed; 810 AA.
AC Q9NL29; Q9XXU1;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Abnormal pharyngeal pumping eat-20 {ECO:0000303|PubMed:10655217};
DE Flags: Precursor;
GN Name=eat-20; ORFNames=H30A04.1;
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:BAA92158.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:10655217};
RX PubMed=10655217; DOI=10.1093/genetics/154.2.635;
RA Shibata Y., Fujii T., Dent J.A., Fujisawa H., Takagi S.;
RT "EAT-20, a novel transmembrane protein with EGF motifs, is required for
RT efficient feeding in Caenorhabditis elegans.";
RL Genetics 154:635-646(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAC42315.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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).
CC -!- FUNCTION: Regulates pharyngeal pumping during feeding.
CC {ECO:0000269|PubMed:10655217}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000269|PubMed:9851916}; Synonyms=B
CC {ECO:0000269|PubMed:10655217};
CC IsoId=Q9NL29-1; Sequence=Displayed;
CC Name=a {ECO:0000269|PubMed:9851916}; Synonyms=A
CC {ECO:0000269|PubMed:10655217};
CC IsoId=Q9NL29-2; Sequence=VSP_053168;
CC -!- TISSUE SPECIFICITY: Highly expressed in the pharynx, circumpharyngeal
CC cells, pharyngeal-intestinal valve and a subset of neurons in larval
CC and embryonic stages. Also moderately expressed in the lining of the
CC intestine, coelomocytes, labial process bundles and some hypodermal
CC cells. In adults, it is predominantly expressed in the pharynx, the
CC pharyngeal-intenstinal valve, some circumpharyngeal cells, m3, m4 and
CC m6 pharyngeal muscles, and IL1, OLQ, BAG and ALN neurons. Weaker
CC expression is observed in labial process bundles, coelomocytes, the
CC ventral hypodermal ridge, the vulval hypodermis and the sensory rays of
CC the adult male tail. {ECO:0000269|PubMed:10655217}.
CC -!- DISRUPTION PHENOTYPE: Worms display a reduction in pharyngeal pumping
CC rates, body length and intestine size, as well as a prolonged egg
CC laying period and smaller brood size. {ECO:0000269|PubMed:10655217}.
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DR EMBL; AB032748; BAA92157.1; -; mRNA.
DR EMBL; AB032749; BAA92158.1; -; mRNA.
DR EMBL; AL008869; CAA15516.1; -; Genomic_DNA.
DR EMBL; AL008869; CAC42315.1; -; Genomic_DNA.
DR PIR; T23129; T23129.
DR RefSeq; NP_001024740.1; NM_001029569.2.
DR RefSeq; NP_001024741.1; NM_001029570.2. [Q9NL29-1]
DR AlphaFoldDB; Q9NL29; -.
DR BioGRID; 46535; 4.
DR IntAct; Q9NL29; 4.
DR STRING; 6239.H30A04.1b; -.
DR EPD; Q9NL29; -.
DR PaxDb; Q9NL29; -.
DR PeptideAtlas; Q9NL29; -.
DR EnsemblMetazoa; H30A04.1a.1; H30A04.1a.1; WBGene00001148. [Q9NL29-2]
DR EnsemblMetazoa; H30A04.1a.2; H30A04.1a.2; WBGene00001148. [Q9NL29-2]
DR EnsemblMetazoa; H30A04.1b.1; H30A04.1b.1; WBGene00001148. [Q9NL29-1]
DR GeneID; 181641; -.
DR KEGG; cel:CELE_H30A04.1; -.
DR UCSC; H30A04.1b.2; c. elegans.
DR CTD; 181641; -.
DR WormBase; H30A04.1a; CE18828; WBGene00001148; eat-20. [Q9NL29-2]
DR WormBase; H30A04.1b; CE27767; WBGene00001148; eat-20. [Q9NL29-1]
DR eggNOG; KOG1217; Eukaryota.
DR HOGENOM; CLU_311306_0_0_1; -.
DR InParanoid; Q9NL29; -.
DR OMA; MPMSHIA; -.
DR OrthoDB; 419576at2759; -.
DR PRO; PR:Q9NL29; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001148; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0009986; C:cell surface; IDA:WormBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR003645; Fol_N.
DR Pfam; PF00008; EGF; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00274; FOLN; 2.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 3.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; EGF-like domain; Glycoprotein;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..810
FT /note="Abnormal pharyngeal pumping eat-20"
FT /evidence="ECO:0000255"
FT /id="PRO_0000390492"
FT TOPO_DOM 21..748
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 749..769
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 770..810
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 220..257
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 258..293
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 301..335
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 522..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..557
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 224..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 229..245
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 247..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 261..272
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 266..281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 283..292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 305..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 309..323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 325..334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 711..712
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000303|PubMed:10655217"
FT /id="VSP_053168"
SQ SEQUENCE 810 AA; 87953 MW; 272B571605BF45C6 CRC64;
MTTFCRVLLI FGIYVAVCCA QSVEDDVFHF TNPSQGNAVW ILDESSLPWT GGYQFLRSIS
GMPTTLLSVV DSSTGVTLGQ CVAPQDATGN FSKRWERFSW ELTASGLDCT FEHGAAIRVE
FDRTQNPRTF SIRIQSITGP ACLRDVVVQT EQATGCPPHL SRNSFTANAL NCSCPFLDAA
NEDSEIENED VDMLANTPQF PLFKGIDPSV LGSANPPTLP PSPCANHECH NNGTCLVSQE
GAATCLCRNG FTGDRCELDV CSSVPCQNGG VCRSNNGIAY CECPPAFTGL LCESAHTDES
VAPICRPECS NGQCVFKDGQ AQCECRQGFT GANCNVLDVC LGDAACSMFG PLAKCVLDDN
MDKMSSLTLI NGTYDCLCPH PIHGQFVDCM QLHAPSATSV QPTEQVVINN VTPSFPVLEI
SKLPTGAPVT FTATSTTLMV TQPTVTVSPT HQVPSEPFVG FTVTRAPLRP LDIGSTTLPP
PFNQHIITAG EPTWSSQQPH QPSEVPTQTT FIFPQTPETT TFAPTTGTQQ PVHKFVSPSV
PDENEEEEEE ETTEETEETF PTPSTMQVAT NGQFTTETAF VTSTIPSTTT DMEETDEDED
MTEEVTDSST QPSTTVFVQP TTTFTTEAPT TTMEEEEEMT TDQVEDIESE EIATTTTQTS
LPFWMTTTNK QVVPDSPTPM VIMPHPQPDE KMETSTEGVV DEESDEERTT VPESNEEVVT
KNAEATTPSD ITHHHTSSGK QSSAAASWII AIIALIVLGL LLLATSLFIL RYIRQSRKLH
GKYNPAREEH NLSAAYAMPM SHIAKEERLI
