ID   EAT20_CAEBR             Reviewed;         811 AA.
AC   A8X481;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 3.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Abnormal pharyngeal pumping eat-20 {ECO:0000250|UniProtKB:Q9NL29};
DE   Flags: Precursor;
GN   Name=eat-20; ORFNames=CBG07717;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Regulates pharyngeal pumping during feeding.
CC       {ECO:0000250|UniProtKB:Q9NL29}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC       membrane protein {ECO:0000255}.
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DR   EMBL; HE601041; CAP27441.3; -; Genomic_DNA.
DR   RefSeq; XP_002645949.1; XM_002645903.1.
DR   AlphaFoldDB; A8X481; -.
DR   STRING; 6238.CBG07717; -.
DR   EnsemblMetazoa; CBG07717a.1; CBG07717a.1; WBGene00029679.
DR   GeneID; 8587948; -.
DR   KEGG; cbr:CBG_07717; -.
DR   CTD; 8587948; -.
DR   WormBase; CBG07717a; CBP01846; WBGene00029679; Cbr-eat-20.
DR   eggNOG; KOG1217; Eukaryota.
DR   HOGENOM; CLU_311306_0_0_1; -.
DR   InParanoid; A8X481; -.
DR   OMA; MPMSHIA; -.
DR   OrthoDB; 419576at2759; -.
DR   Proteomes; UP000008549; Chromosome X.
DR   GO; GO:0030424; C:axon; IEA:EnsemblMetazoa.
DR   GO; GO:0009986; C:cell surface; IEA:EnsemblMetazoa.
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   3: Inferred from homology;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..811
FT                   /note="Abnormal pharyngeal pumping eat-20"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000390713"
FT   TOPO_DOM        21..749
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        750..770
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        771..811
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          544..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          690..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..566
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..611
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..639
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..654
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..718
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        719..739
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"
SQ   SEQUENCE   811 AA;  87988 MW;  201256BC57F93FA1 CRC64;
     MTTFCRVLLI FGIYVAVSCA QSVEDDVFHF TNPSQGNAVW ILDESSLPWT GGYQFLRSIS
     GMPTTLLSIV DSSTGVTLGQ CVAPQDATGN FSKRWEKFSW ELTASGLDCQ FEQGAATRVE
     FDRSQNPRTF SIRIQSITGP ACLRDVVVQT EQATGCPPHL SRNSFTANAL NCSCPYLDAA
     NEDGETENED VDMLANSPQF PLFKVVDPSV LGSANPPTLP PSPCANHECH NNGTCLVSQE
     GAAMCLCRNG FTGDRCELDV CSAVPCQNGG VCRSNNGIAY CECPPAFSGL LCESAHTDES
     AAPICNPECS NGQCVLKDGQ PQCECRQGFT GANCNVLDVC LGDAACSMFG PSAKCVLDDN
     MDKMSSASLI NGTYDCLCPH PIHGQFVDCM QLHAPSATSV QPSEPAVVIN NVTPSFPVLE
     ISQVPTGAPK TFTATSTTSV ATQPAVPVVQ TLPTTQQVPS EPFVGFTVTR EPLRPFEATT
     TTTLPPPFQQ HIITAGEQPT WSSQQPQQPS EVPVPAQTMT TFIFPQTPET TTFPPTTGAT
     VHKFVSPNMP DENEEEEEDE TTDETEETFP TPSTMQVATD SSIRSEFFTS TFPTTTDMEE
     TDEEEDMTEE VTDSSTQPST TVFIQPSSTT FTTEAPTTTM EEEETTEQEE IESEEAISTT
     TQTSLPFWMT TIAIKMPDIV ASPTPMIIMP HPQPEEKMET STEGIESEEE RTTESNEEII
     PKNMEPTTPS DITHHHTSSG KQSSAVASWI IATIALIVLG SLLLATSLFV LRYIRQSRKL
     HGKYNPAREE HNLSAAYAMP MSHIAKEERL I