GLP1_CAEEL
ID GLP1_CAEEL Reviewed; 1295 AA.
AC P13508;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Protein glp-1;
DE Contains:
DE RecName: Full=glp-1/Notch intracellular domain {ECO:0000305|PubMed:9003776};
DE Flags: Precursor;
GN Name=glp-1 {ECO:0000312|WormBase:F02A9.6};
GN Synonyms=emb-33 {ECO:0000312|WormBase:F02A9.6};
GN ORFNames=F02A9.6 {ECO:0000312|WormBase:F02A9.6};
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 [GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=2758466; DOI=10.1016/0092-8674(89)90436-4;
RA Yochem J., Greenwald I.;
RT "glp-1 and lin-12, genes implicated in distinct cell-cell interactions in
RT C. elegans, encode similar transmembrane proteins.";
RL Cell 58:553-563(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [3]
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 [4]
RP DELETION OF 1174-1295.
RX PubMed=1881436; DOI=10.1038/352811a0;
RA Mango S.E., Maine E.M., Kimble J.;
RT "Carboxy-terminal truncation activates glp-1 protein to specify vulval
RT fates in Caenorhabditis elegans.";
RL Nature 352:811-815(1991).
RN [5]
RP CHARACTERIZATION OF FUNCTION OF THE ANKYRIN REPEATS.
RX PubMed=8350921; DOI=10.1038/364632a0;
RA Roehl H., Kimble J.;
RT "Control of cell fate in C. elegans by a GLP-1 peptide consisting primarily
RT of ankyrin repeats.";
RL Nature 364:632-635(1993).
RN [6]
RP FUNCTION.
RX PubMed=8156602; DOI=10.1016/0092-8674(94)90238-0;
RA Mello C.C., Draper B.W., Priess J.R.;
RT "The maternal genes apx-1 and glp-1 and establishment of dorsal-ventral
RT polarity in the early C. elegans embryo.";
RL Cell 77:95-106(1994).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=7607081; DOI=10.1242/dev.120.10.2913;
RA Henderson S.T., Gao D., Lambie E.J., Kimble J.;
RT "lag-2 may encode a signaling ligand for the GLP-1 and LIN-12 receptors of
RT C. elegans.";
RL Development 120:2913-2924(1994).
RN [8]
RP FUNCTION, AND PROTEOLYTIC PROCESSING.
RX PubMed=7566091; DOI=10.1038/377351a0;
RA Levitan D., Greenwald I.;
RT "Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis
RT elegans S182 Alzheimer's disease gene.";
RL Nature 377:351-354(1995).
RN [9]
RP FUNCTION, INTERACTION WITH LAG-1, AND SUBCELLULAR LOCATION.
RX PubMed=9003776; DOI=10.1002/j.1460-2075.1996.tb01092.x;
RA Roehl H., Bosenberg M., Blelloch R., Kimble J.;
RT "Roles of the RAM and ANK domains in signaling by the C. elegans GLP-1
RT receptor.";
RL EMBO J. 15:7002-7012(1996).
RN [10]
RP INTERACTION WITH SEL-10.
RX PubMed=9861048; DOI=10.1073/pnas.95.26.15787;
RA Wu G., Hubbard E.J.A., Kitajewski J.K., Greenwald I.;
RT "Evidence for functional and physical association between Caenorhabditis
RT elegans SEL-10, a Cdc4p-related protein, and SEL-12 presenilin.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:15787-15791(1998).
RN [11]
RP FUNCTION.
RX PubMed=10884418; DOI=10.1073/pnas.97.14.7877;
RA Doyle T.G., Wen C., Greenwald I.;
RT "SEL-8, a nuclear protein required for LIN-12 and GLP-1 signaling in
RT Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:7877-7881(2000).
RN [12]
RP FUNCTION, AND PROTEOLYTIC PROCESSING.
RX PubMed=16197940; DOI=10.1016/j.ydbio.2005.08.014;
RA Jarriault S., Greenwald I.;
RT "Evidence for functional redundancy between C. elegans ADAM proteins SUP-
RT 17/Kuzbanian and ADM-4/TACE.";
RL Dev. Biol. 287:1-10(2005).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF GLY-1043.
RX PubMed=16319922; DOI=10.1038/sj.emboj.7600901;
RA Lee M.H., Hook B., Lamont L.B., Wickens M., Kimble J.;
RT "LIP-1 phosphatase controls the extent of germline proliferation in
RT Caenorhabditis elegans.";
RL EMBO J. 25:88-96(2006).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP ARG-974.
RX PubMed=18599512; DOI=10.1242/dev.012435;
RA Ouellet J., Li S., Roy R.;
RT "Notch signalling is required for both dauer maintenance and recovery in C.
RT elegans.";
RL Development 135:2583-2592(2008).
RN [15]
RP REVIEW OF FUNCTION.
RX PubMed=19379690; DOI=10.1016/j.cell.2009.03.045;
RA Kopan R., Ilagan M.X.;
RT "The canonical Notch signaling pathway: unfolding the activation
RT mechanism.";
RL Cell 137:216-233(2009).
RN [16]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ALA-1034.
RX PubMed=19502484; DOI=10.1242/dev.034603;
RA Nadarajan S., Govindan J.A., McGovern M., Hubbard E.J., Greenstein D.;
RT "MSP and GLP-1/Notch signaling coordinately regulate actomyosin-dependent
RT cytoplasmic streaming and oocyte growth in C. elegans.";
RL Development 136:2223-2234(2009).
RN [17]
RP FUNCTION, AND MUTAGENESIS OF ARG-974.
RX PubMed=21906946; DOI=10.1016/j.cub.2011.07.042;
RA Lapierre L.R., Gelino S., Melendez A., Hansen M.;
RT "Autophagy and lipid metabolism coordinately modulate life span in
RT germline-less C. elegans.";
RL Curr. Biol. 21:1507-1514(2011).
RN [18]
RP MUTAGENESIS OF GLY-1043.
RX PubMed=22820175; DOI=10.1016/j.bbamcr.2012.07.006;
RA Cha D.S., Datla U.S., Hollis S.E., Kimble J., Lee M.H.;
RT "The Ras-ERK MAPK regulatory network controls dedifferentiation in
RT Caenorhabditis elegans germline.";
RL Biochim. Biophys. Acta 1823:1847-1855(2012).
RN [19]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-529 AND ARG-974.
RX PubMed=22278922; DOI=10.1242/dev.074047;
RA Korta D.Z., Tuck S., Hubbard E.J.;
RT "S6K links cell fate, cell cycle and nutrient response in C. elegans
RT germline stem/progenitor cells.";
RL Development 139:859-870(2012).
RN [20]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LEU-929.
RX PubMed=24332851; DOI=10.1016/j.celrep.2013.11.018;
RA Chen D., Li P.W., Goldstein B.A., Cai W., Thomas E.L., Chen F.,
RA Hubbard A.E., Melov S., Kapahi P.;
RT "Germline signaling mediates the synergistically prolonged longevity
RT produced by double mutations in daf-2 and rsks-1 in C. elegans.";
RL Cell Rep. 5:1600-1610(2013).
RN [21]
RP FUNCTION, AND MUTAGENESIS OF ARG-974.
RX PubMed=28853436; DOI=10.1038/ncomms16083;
RA Tiku V., Jain C., Raz Y., Nakamura S., Heestand B., Liu W., Spaeth M.,
RA Suchiman H.E.D., Mueller R.U., Slagboom P.E., Partridge L., Antebi A.;
RT "Small nucleoli are a cellular hallmark of longevity.";
RL Nat. Commun. 8:16083-16083(2016).
RN [22]
RP FUNCTION.
RX PubMed=32196486; DOI=10.1371/journal.pgen.1008650;
RA Chen J., Mohammad A., Pazdernik N., Huang H., Bowman B., Tycksen E.,
RA Schedl T.;
RT "GLP-1 Notch-LAG-1 CSL control of the germline stem cell fate is mediated
RT by transcriptional targets lst-1 and sygl-1.";
RL PLoS Genet. 16:e1008650-e1008650(2020).
CC -!- FUNCTION: Essential signaling protein which has a major role in
CC germline and embryonic development; involved in cell fate decisions
CC that require cell-cell interactions (PubMed:8156602, PubMed:16319922,
CC PubMed:19379690). Probable membrane-bound receptor for putative ligands
CC lag-2 and apx-1 (PubMed:8156602, PubMed:7607081). Upon ligand
CC activation, and releasing from the cell membrane, the glp-1/Notch
CC intracellular domain (NICD) probably forms a transcriptional activator
CC complex with lag-1 and lag-3 and regulates expression of various genes;
CC targets in the germline include lst-1 and sygl-1 (PubMed:9003776,
CC PubMed:10884418, PubMed:16319922, PubMed:32196486, PubMed:16197940,
CC PubMed:7566091, PubMed:19379690). Involved in the specification of the
CC cell fates of the blastomeres, ABa and ABp (PubMed:8156602). Proper
CC signaling by glp-1 induces ABa descendants to produce anterior
CC pharyngeal cells, and ABp descendants to adopt a different fate
CC (PubMed:8156602). Contributes to the establishment of the dorsal-
CC ventral axis in early embryos (PubMed:8156602). Required in postmitotic
CC neurons in order to maintain the developmentally arrested larval state
CC known as dauer, probably in response to lag-2 (PubMed:18599512).
CC Regulates germ cell mitotic proliferation probably by regulating MAP
CC kinase phosphatase lip-1 expression (PubMed:16319922, PubMed:22278922).
CC Required for oocyte growth control (PubMed:19502484). Plays a negative
CC role in lifespan (PubMed:21906946, PubMed:24332851, PubMed:28853436).
CC {ECO:0000269|PubMed:10884418, ECO:0000269|PubMed:16197940,
CC ECO:0000269|PubMed:16319922, ECO:0000269|PubMed:18599512,
CC ECO:0000269|PubMed:19502484, ECO:0000269|PubMed:21906946,
CC ECO:0000269|PubMed:22278922, ECO:0000269|PubMed:24332851,
CC ECO:0000269|PubMed:28853436, ECO:0000269|PubMed:32196486,
CC ECO:0000269|PubMed:7566091, ECO:0000269|PubMed:7607081,
CC ECO:0000269|PubMed:8156602, ECO:0000269|PubMed:9003776,
CC ECO:0000303|PubMed:19379690}.
CC -!- SUBUNIT: Interacts with sel-10. {ECO:0000269|PubMed:9861048}.
CC -!- SUBUNIT: [glp-1/Notch intracellular domain]: When activated, the glp-
CC 1/Notch intracellular domain (NICD) may become a component of a complex
CC consisting of at least the NICD, lag-1 and lag-3.
CC {ECO:0000269|PubMed:9003776, ECO:0000303|PubMed:19379690}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7607081};
CC Single-pass type I membrane protein {ECO:0000255}. Cell projection,
CC axon {ECO:0000269|PubMed:18599512}. Note=Localized to axons during
CC dauer larval stage. {ECO:0000269|PubMed:18599512}.
CC -!- SUBCELLULAR LOCATION: [glp-1/Notch intracellular domain]: Nucleus
CC {ECO:0000269|PubMed:9003776}. Note=The glp-1/Notch intracellular domain
CC (NICD) may become localized to the nucleus after ligand activation.
CC {ECO:0000269|PubMed:9003776}.
CC -!- TISSUE SPECIFICITY: Expressed in the distal mitotic region of the germ
CC line (PubMed:7607081). May be absent from the gonadal distal tip cell
CC (DTC) (PubMed:7607081). {ECO:0000269|PubMed:7607081}.
CC -!- DEVELOPMENTAL STAGE: Acts on ABp development during 4-cell and 12-cell
CC stages, and on ABa development during 12-cell and 28-cell stages
CC (PubMed:8156602). Expressed in various neurons, including AWC, during
CC the dauer larval stage (PubMed:18599512). {ECO:0000269|PubMed:18599512,
CC ECO:0000269|PubMed:8156602}.
CC -!- PTM: Upon binding its ligands, it is cleaved (S2 cleavage) in its
CC extracellular domain, close to the transmembrane domain (By
CC similarity). S2 cleavage is probably mediated by the metalloproteases
CC adm-4 and sup-17 (PubMed:16197940). It is then cleaved (S3 cleavage)
CC downstream of its transmembrane domain, releasing it from the cell
CC membrane; S3 cleavage requires a multiprotein gamma-secretase complex,
CC which may include presenilin sel-12 (PubMed:7566091).
CC {ECO:0000250|UniProtKB:P07207, ECO:0000269|PubMed:16197940,
CC ECO:0000269|PubMed:7566091}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes an increase in
CC lifespan and a moderate increase in aak-2 phosphorylation
CC (PubMed:24332851). RNAi-mediated knockdown in a rsks-1 mutant
CC background reduces the formation of proximal germ cell tumors
CC (PubMed:22278922). RNAi-mediated knockdown results in abnormally large
CC oocytes (PubMed:19502484). {ECO:0000269|PubMed:19502484,
CC ECO:0000269|PubMed:22278922, ECO:0000269|PubMed:24332851}.
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DR EMBL; M25580; AAA28058.1; -; Genomic_DNA.
DR EMBL; BX284603; CAA79620.1; -; Genomic_DNA.
DR EMBL; Z29116; CAA79620.1; JOINED; Genomic_DNA.
DR PIR; A32901; A32901.
DR RefSeq; NP_499014.1; NM_066613.4.
DR AlphaFoldDB; P13508; -.
DR SMR; P13508; -.
DR BioGRID; 41485; 94.
DR DIP; DIP-26562N; -.
DR ELM; P13508; -.
DR IntAct; P13508; 13.
DR MINT; P13508; -.
DR STRING; 6239.F02A9.6; -.
DR EPD; P13508; -.
DR PaxDb; P13508; -.
DR PRIDE; P13508; -.
DR EnsemblMetazoa; F02A9.6.1; F02A9.6.1; WBGene00001609.
DR GeneID; 176286; -.
DR KEGG; cel:CELE_F02A9.6; -.
DR UCSC; F02A9.6; c. elegans.
DR CTD; 176286; -.
DR WormBase; F02A9.6; CE00237; WBGene00001609; glp-1.
DR eggNOG; KOG1217; Eukaryota.
DR HOGENOM; CLU_005264_0_0_1; -.
DR InParanoid; P13508; -.
DR OMA; SKEPDAC; -.
DR OrthoDB; 7525at2759; -.
DR PhylomeDB; P13508; -.
DR SignaLink; P13508; -.
DR PRO; PR:P13508; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001609; Expressed in embryonic cell and 39 other tissues.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0012505; C:endomembrane system; IDA:WormBase.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:WormBase.
DR GO; GO:0044214; C:spanning component of plasma membrane; IDA:WormBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:WormBase.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:WormBase.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISS:WormBase.
DR GO; GO:0001708; P:cell fate specification; IGI:WormBase.
DR GO; GO:0007349; P:cellularization; IMP:UniProtKB.
DR GO; GO:0099636; P:cytoplasmic streaming; IMP:UniProtKB.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:WormBase.
DR GO; GO:0043055; P:maintenance of dauer; IGI:WormBase.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; IMP:UniProtKB.
DR GO; GO:0002119; P:nematode larval development; IGI:WormBase.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0001555; P:oocyte growth; IMP:UniProtKB.
DR GO; GO:0043282; P:pharyngeal muscle development; IMP:WormBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:1905938; P:positive regulation of germ cell proliferation; IMP:UniProtKB.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:WormBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:WormBase.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IGI:UniProtKB.
DR GO; GO:1905936; P:regulation of germ cell proliferation; IGI:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR035993; Notch-like_dom_sf.
DR InterPro; IPR000800; Notch_dom.
DR InterPro; IPR010660; Notch_NOD_dom.
DR InterPro; IPR011656; Notch_NODP_dom.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF06816; NOD; 1.
DR Pfam; PF07684; NODP; 1.
DR Pfam; PF00066; Notch; 3.
DR PRINTS; PR01452; LNOTCHREPEAT.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00181; EGF; 11.
DR SMART; SM00179; EGF_CA; 6.
DR SMART; SM00004; NL; 3.
DR SMART; SM01338; NOD; 1.
DR SMART; SM01339; NODP; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF90193; SSF90193; 3.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS00022; EGF_1; 10.
DR PROSITE; PS01186; EGF_2; 8.
DR PROSITE; PS50026; EGF_3; 10.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50258; LNR; 3.
PE 1: Evidence at protein level;
KW Activator; ANK repeat; Cell membrane; Cell projection;
KW Developmental protein; Differentiation; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Notch signaling pathway; Nucleus;
KW Reference proteome; Repeat; Signal; Transcription;
KW Transcription regulation; Transmembrane; Transmembrane helix.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..1295
FT /note="Protein glp-1"
FT /id="PRO_0000007594"
FT CHAIN ?..1295
FT /note="glp-1/Notch intracellular domain"
FT /evidence="ECO:0000305"
FT /id="PRO_0000453170"
FT TOPO_DOM 16..764
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 765..786
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 787..1295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..58
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 117..152
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 154..190
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 190..230
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 232..269
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 271..308
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 316..359
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 369..406
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 407..443
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 446..479
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 496..532
FT /note="LNR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525,
FT ECO:0000269|PubMed:8350921"
FT REPEAT 536..577
FT /note="LNR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525,
FT ECO:0000269|PubMed:8350921"
FT REPEAT 581..612
FT /note="LNR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525,
FT ECO:0000269|PubMed:8350921"
FT REPEAT 961..990
FT /note="ANK 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:8350921"
FT REPEAT 994..1023
FT /note="ANK 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:8350921"
FT REPEAT 1030..1062
FT /note="ANK 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:8350921"
FT REPEAT 1074..1103
FT /note="ANK 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:8350921"
FT REPEAT 1107..1136
FT /note="ANK 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:8350921"
FT REGION 1177..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 675
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 23..35
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 29..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 48..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 121..131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 126..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 142..151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 158..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 163..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 180..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 201..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 220..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 236..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 242..257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 259..268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 275..286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 280..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 298..307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 329..342
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 336..347
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 349..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 373..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 378..394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 396..405
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 411..422
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 416..431
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 433..442
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 450..461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 455..467
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 469..478
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 496..519
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT DISULFID 501..514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT DISULFID 510..526
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT DISULFID 536..560
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT DISULFID 542..555
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT DISULFID 551..567
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT DISULFID 582..595
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT DISULFID 591..607
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT MUTAGEN 529
FT /note="G->E: In ar202; formation of proximal germ cell-
FT derived tumors."
FT /evidence="ECO:0000269|PubMed:22278922"
FT MUTAGEN 929
FT /note="L->F: In 2144; moderate increase in aak-2
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:24332851"
FT MUTAGEN 974
FT /note="R->C: In 2141; reduces number of germline
FT progenitors at the semi-permissive temperature (20 degrees
FT Celsius). All germ cells differentiate at the restrictive
FT temperature (25 degrees Celsius). Defects in maintenance of
FT the developmentally arrested larval state known as dauer,
FT in response to pheromone; similar phenotype in absence of
FT pheromone, when on a daf-7 mutant background. Increases
FT longevity and reduces nucleoli size (20 degrees Celsius).
FT Increased longevity and reduced nucleoli size phenotypes
FT are suppressed in an ncl-1 mutant background (20 degrees
FT Celsius). Autophagy levels are increased due the up-
FT regulation of transcription factor pha-4 and its autophagy-
FT related target genes. Increases lipase activity. The
FT increase in autophagy and lipase activity is partially
FT suppressed in a lipl-4 RNAi-mediated background."
FT /evidence="ECO:0000269|PubMed:18599512,
FT ECO:0000269|PubMed:21906946, ECO:0000269|PubMed:22278922,
FT ECO:0000269|PubMed:28853436"
FT MUTAGEN 1034
FT /note="A->T: In tn777; abnormally large oocytes."
FT /evidence="ECO:0000269|PubMed:19502484"
FT MUTAGEN 1043
FT /note="G->E: In q224; at the restrictive temperature of 25
FT degrees Celsius, loss of interaction of lag-3 with lip-1
FT promoter. Loss of mpk-1 isoform b expression probably due
FT to a lack of germline."
FT /evidence="ECO:0000269|PubMed:16319922,
FT ECO:0000269|PubMed:22820175"
SQ SEQUENCE 1295 AA; 144079 MW; 422AAD0A2DEEF3B4 CRC64;
MRVLLILLAF FAPIASQLMG GECGREGACS VNGKCYNGKL IETYWCRCKK GFGGAFCERE
CDLDCKRGEK CIYDVYGENP TCICQDCEDE TPPTERTQKG CEEGYGGPDC KTPLFSGVNP
CDSDPCNNGL CYPFYGGFQC ICNNGYGGSY CEEGIDHCAQ NECAEGSTCV NSVYNYYCDC
PIGKSGRYCE RTECALMGNI CNHGRCIPNR DEDKNFRCVC DSGYEGEFCN KDKNECLIEE
TCVNNSTCFN LHGDFTCTCK PGYAGKYCEE AIDMCKDYVC QNDGYCAHDS NQMPICYCEQ
GFTGQRCEIE CPSGFGGIHC DLPLQRPHCS RSNGTCYNDG RCINGFCVCE PDYIGDRCEI
NRKDFKFPDI QSCKYNPCVN NATCIDLKNS GYSCHCPLGF YGLNCEQHLL CTPTTCANGG
TCEGVNGVIR CNCPNGFSGD YCEIKDRQLC SRHPCKNGGV CKNTGYCECQ YGYTGPTCEE
VLVIEKSKET VIRDLCEQRK CMDLASNGIC NPECNLEECN FDGGDCSGGQ RPFSKCQYPA
RCADQFANGV CNQECNNEEC LYDGLDCQSE LFRCPAHIRK HCIERRGDGV CNLECSFIGC
GFDGGDCNNG TEAIILSDIR IKVQIDPIEF QATGGETLMQ ISANLRATVR IQRDELGPLV
FRWDGEHEME RVEMNSSKLE DQFVLSHHVR RYRQAVVTGI VLYLEVEEIC KPEFCRFSTA
QSVVDLIAAG LVKSDGRMSL GLPITEAMVA VPKRNEIDEG WSRSQVILFA CIAFLAFGTV
VAGVIAKNGP ERSRKRKMVN ATVWMPPMES TNEKGRRNQS NHSSQCSLLD NSAYYHPNTK
RHCSDYSTGY NGEQYSQIYP QTLANGYPGD YNELNFDFQS ETFAPADLPA DEIPLHVQAA
GPDAITAPIT NESVNQVDSK YRRRVLHWLA ANVRGKPEDV ITTEAIRCLK AGADVNARDC
DENTALMLAV RAHRVRLSVV LLREGANPTI FNNSERSALH EAVVNKDLRI LRHLLTDKRL
LKEIDELDRN GMTALMLVAR ELGKHQVEMA ELLLSKGAKL DYDGAARKDS NKYKGRTALH
YAAMHDNEEM VIMLVRRSSN KDKQDEDGRT PIMLAAKEGC EKTVQYLALN DASLGIVDSM
DMTAAQVAEA SYHHELAAFL RQVANERHRN DIMRQQIVKS GHGAKSGRQT VKNIKRAGSR
KTPTSAASSR ETNHLTPPPS DGSFSSPSPH YYPTTTSTPN RMETSPEYMF NHEMAPPVNA
MWYTTPPPYQ DPNYRHVPPN TAFQNAEQMN GSFYC
