LIN12_CAEEL
ID LIN12_CAEEL Reviewed; 1429 AA.
AC P14585;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Protein lin-12;
DE AltName: Full=Abnormal cell lineage protein 12;
DE AltName: Full=Notch-like protein lin-12 {ECO:0000303|PubMed:9389650};
DE Contains:
DE RecName: Full=lin-12/Notch intracellular domain {ECO:0000303|PubMed:16530045, ECO:0000303|PubMed:18036582};
DE Flags: Precursor;
GN Name=lin-12 {ECO:0000312|WormBase:R107.8};
GN ORFNames=R107.8 {ECO:0000312|WormBase:R107.8};
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], AND FUNCTION.
RC STRAIN=Bristol N2;
RX PubMed=3419531; DOI=10.1038/335547a0;
RA Yochem J., Weston K., Greenwald I.;
RT "The Caenorhabditis elegans lin-12 gene encodes a transmembrane protein
RT with overall similarity to Drosophila Notch.";
RL Nature 335:547-550(1988).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 173-712, AND FUNCTION.
RX PubMed=3000611; DOI=10.1016/0092-8674(85)90230-2;
RA Greenwald I.;
RT "lin-12, a nematode homeotic gene, is homologous to a set of mammalian
RT proteins that includes epidermal growth factor.";
RL Cell 43:583-590(1985).
RN [5]
RP FUNCTION.
RX PubMed=8343960; DOI=10.1016/0092-8674(93)90424-o;
RA Struhl G., Fitzgerald K., Greenwald I.;
RT "Intrinsic activity of the Lin-12 and Notch intracellular domains in
RT vivo.";
RL Cell 74:331-345(1993).
RN [6]
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 [7]
RP INTERACTION WITH SEL-10.
RX PubMed=9389650; DOI=10.1101/gad.11.23.3182;
RA Hubbard E.J.A., Wu G., Kitajewski J., Greenwald I.;
RT "sel-10, a negative regulator of lin-12 activity in Caenorhabditis elegans,
RT encodes a member of the CDC4 family of proteins.";
RL Genes Dev. 11:3182-3193(1997).
RN [8]
RP FUNCTION.
RX PubMed=10903169; DOI=10.1242/dev.127.16.3429;
RA Hermann G.J., Leung B., Priess J.R.;
RT "Left-right asymmetry in C. elegans intestine organogenesis involves a LIN-
RT 12/Notch signaling pathway.";
RL Development 127:3429-3440(2000).
RN [9]
RP FUNCTION.
RX PubMed=10830967; DOI=10.1038/35012645;
RA Petcherski A.G., Kimble J.;
RT "LAG-3 is a putative transcriptional activator in the C. elegans Notch
RT pathway.";
RL Nature 405:364-368(2000).
RN [10]
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 [11]
RP FUNCTION.
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 [12]
RP FUNCTION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF 400-TRP--PHE-1429.
RX PubMed=18036582; DOI=10.1016/j.ydbio.2007.10.027;
RA Foehr M.L., Liu J.;
RT "Dorsoventral patterning of the C. elegans postembryonic mesoderm requires
RT both LIN-12/Notch and TGFbeta signaling.";
RL Dev. Biol. 313:256-266(2008).
RN [13]
RP FUNCTION, INTERACTION WITH LAG-2; DSL-1 AND OSM-11, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18700817; DOI=10.1371/journal.pbio.0060196;
RA Komatsu H., Chao M.Y., Larkins-Ford J., Corkins M.E., Somers G.A.,
RA Tucey T., Dionne H.M., White J.Q., Wani K., Boxem M., Hart A.C.;
RT "OSM-11 facilitates LIN-12 Notch signaling during Caenorhabditis elegans
RT vulval development.";
RL PLoS Biol. 6:e196-e196(2008).
RN [14]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 400-TRP--PHE-1429.
RX PubMed=21549604; DOI=10.1016/j.cub.2011.04.010;
RA Singh K., Chao M.Y., Somers G.A., Komatsu H., Corkins M.E.,
RA Larkins-Ford J., Tucey T., Dionne H.M., Walsh M.B., Beaumont E.K.,
RA Hart D.P., Lockery S.R., Hart A.C.;
RT "C. elegans Notch signaling regulates adult chemosensory response and
RT larval molting quiescence.";
RL Curr. Biol. 21:825-834(2011).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27661254; DOI=10.7554/elife.17218;
RA McClatchey S.T., Wang Z., Linden L.M., Hastie E.L., Wang L., Shen W.,
RA Chen A., Chi Q., Sherwood D.R.;
RT "Boundary cells restrict dystroglycan trafficking to control basement
RT membrane sliding during tissue remodeling.";
RL Elife 5:0-0(2016).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=32053105; DOI=10.7554/elife.50986;
RA Haag A., Walser M., Henggeler A., Hajnal A.;
RT "The CHORD protein CHP-1 regulates EGF receptor trafficking and signaling
RT in C. elegans and in human cells.";
RL Elife 9:0-0(2020).
RN [17] {ECO:0007744|PDB:2FO1}
RP X-RAY CRYSTALLOGRAPHY (3.12 ANGSTROMS) OF 933-1297 IN COMPLEX WITH LAG-1;
RP LAG-3 AND DNA.
RX PubMed=16530045; DOI=10.1016/j.cell.2006.01.035;
RA Wilson J.J., Kovall R.A.;
RT "Crystal structure of the CSL-Notch-Mastermind ternary complex bound to
RT DNA.";
RL Cell 124:985-996(2006).
RN [18] {ECO:0007744|PDB:3BRD}
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 937-951 IN COMPLEX WITH LAG-1 AND
RP DNA, AND FUNCTION.
RX PubMed=18381292; DOI=10.1074/jbc.m709501200;
RA Friedmann D.R., Wilson J.J., Kovall R.A.;
RT "RAM-induced allostery facilitates assembly of a notch pathway active
RT transcription complex.";
RL J. Biol. Chem. 283:14781-14791(2008).
CC -!- FUNCTION: Essential signaling protein which has a major role in many
CC developmental processes; involved in cell fate decisions that require
CC cell-cell interactions (PubMed:3419531, PubMed:3000611). Probable
CC membrane-bound receptor for putative ligands lag-2, apx-1, dsl-1 and
CC osm-11 (PubMed:18036582, PubMed:18700817, PubMed:32053105,
CC PubMed:3419531). Upon ligand activation, and releasing from the cell
CC membrane, the lin-12/Notch intracellular domain (NICD) forms a
CC transcriptional activator complex with lag-1 and lag-3 and regulates
CC expression of various genes (PubMed:8343960, PubMed:7566091,
CC PubMed:16197940, PubMed:10830967, PubMed:16530045, PubMed:18381292).
CC Required for ventral cell fates in the postembryonic mesodermal lineage
CC (M lineage) and in uterine precursor cells (PubMed:3419531,
CC PubMed:18036582). Activity in cell fate decisions and tumorigenesis is
CC negatively regulated by sel-10 (PubMed:9389650). Best known for
CC involvement in cell-fate decisions during development, but also plays
CC roles in other events (PubMed:10903169, PubMed:18599512,
CC PubMed:21549604, PubMed:27661254). Regulates recovery from the dauer
CC larval state (PubMed:18599512). Modulates chemosensory avoidance of
CC octanol and quiescence during molting (PubMed:21549604). Promotes
CC basement membrane mobility during tissue remodeling (PubMed:27661254).
CC Involved in establishing left-right asymmetry during intestinal
CC organogenesis (PubMed:10903169). {ECO:0000269|PubMed:10830967,
CC ECO:0000269|PubMed:10903169, ECO:0000269|PubMed:16197940,
CC ECO:0000269|PubMed:16530045, ECO:0000269|PubMed:18036582,
CC ECO:0000269|PubMed:18381292, ECO:0000269|PubMed:18599512,
CC ECO:0000269|PubMed:18700817, ECO:0000269|PubMed:21549604,
CC ECO:0000269|PubMed:27661254, ECO:0000269|PubMed:3000611,
CC ECO:0000269|PubMed:32053105, ECO:0000269|PubMed:3419531,
CC ECO:0000269|PubMed:7566091, ECO:0000269|PubMed:8343960,
CC ECO:0000269|PubMed:9389650, ECO:0000303|PubMed:3419531}.
CC -!- SUBUNIT: May interact with dsl-1 (PubMed:18700817). May interact with
CC lag-2 (PubMed:18700817). May interact with osm-11 (PubMed:18700817).
CC Interacts with sel-10 (PubMed:9389650). {ECO:0000269|PubMed:18700817,
CC ECO:0000269|PubMed:9389650}.
CC -!- SUBUNIT: [lin-12/Notch intracellular domain]: When activated, the lin-
CC 12/Notch intracellular domain (NICD) can become a component of a
CC complex consisting of at least the NICD, lag-1 and sel-8/lag-3
CC (PubMed:16530045, PubMed:18381292). The NICD probably facilitates
CC ordered assembly of the ternary complex via allosteric interactions of
CC its RBP-j associated molecule (RAM) domain with lag-1 (PubMed:16530045,
CC PubMed:18381292). {ECO:0000269|PubMed:16530045,
CC ECO:0000269|PubMed:18381292}.
CC -!- INTERACTION:
CC P14585; Q93794: sel-10; NbExp=3; IntAct=EBI-326049, EBI-323098;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:32053105}; Single-pass type I membrane protein
CC {ECO:0000255}. Note=Localizes to the apical cell membrane of vulval
CC precursor cells. {ECO:0000269|PubMed:32053105}.
CC -!- SUBCELLULAR LOCATION: [lin-12/Notch intracellular domain]: Nucleus
CC {ECO:0000305|PubMed:16530045}. Note=Becomes localized to the nucleus
CC during signal transduction. {ECO:0000305|PubMed:16530045}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the postembryonic mesodermal lineage
CC (M lineage) at the 4-M to 8-M stages, at similar levels in both the
CC dorsal and the ventral sides (PubMed:18036582). At the 10-M stage and
CC later, expression becomes more restricted along the anterioposterior
CC axis and gradually lost in the anterior M lineage cells, but retained
CC in the posterior M lineage cells (PubMed:18036582).
CC {ECO:0000269|PubMed:18036582}.
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 in cells of the pi
CC uterine cell lineage results in impaired basement membrane mobility
CC (PubMed:27661254). Knockdown on a glp-1 mutant background impairs
CC octanol response when animals are shifted to the restrictive
CC temperature (PubMed:21549604). {ECO:0000269|PubMed:21549604,
CC ECO:0000269|PubMed:27661254}.
CC -!- SIMILARITY: Belongs to the NOTCH family. {ECO:0000305}.
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DR EMBL; M12069; AAA70191.1; -; Genomic_DNA.
DR EMBL; BX284603; CAA78474.1; -; Genomic_DNA.
DR PIR; S06434; S06434.
DR RefSeq; NP_499007.1; NM_066606.3.
DR PDB; 2FO1; X-ray; 3.12 A; E=933-1297.
DR PDB; 3BRD; X-ray; 2.21 A; D=937-951.
DR PDB; 3BRF; X-ray; 2.47 A; D=938-950.
DR PDBsum; 2FO1; -.
DR PDBsum; 3BRD; -.
DR PDBsum; 3BRF; -.
DR AlphaFoldDB; P14585; -.
DR SMR; P14585; -.
DR BioGRID; 41481; 28.
DR ComplexPortal; CPX-3152; CSL-Notch-Mastermind transcription factor complex.
DR DIP; DIP-25208N; -.
DR ELM; P14585; -.
DR IntAct; P14585; 5.
DR MINT; P14585; -.
DR STRING; 6239.R107.8; -.
DR iPTMnet; P14585; -.
DR PaxDb; P14585; -.
DR PRIDE; P14585; -.
DR EnsemblMetazoa; R107.8.1; R107.8.1; WBGene00003001.
DR GeneID; 176282; -.
DR KEGG; cel:CELE_R107.8; -.
DR UCSC; R107.8; c. elegans.
DR CTD; 176282; -.
DR WormBase; R107.8; CE00274; WBGene00003001; lin-12.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00980000198606; -.
DR HOGENOM; CLU_005264_0_0_1; -.
DR InParanoid; P14585; -.
DR OMA; TCIDSPL; -.
DR OrthoDB; 7525at2759; -.
DR PhylomeDB; P14585; -.
DR SignaLink; P14585; -.
DR EvolutionaryTrace; P14585; -.
DR PRO; PR:P14585; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003001; Expressed in embryo and 4 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IDA:WormBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; 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:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0005112; F:Notch binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:WormBase.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISS:WormBase.
DR GO; GO:0001708; P:cell fate specification; IMP:UniProtKB.
DR GO; GO:0048858; P:cell projection morphogenesis; IMP:UniProtKB.
DR GO; GO:0045168; P:cell-cell signaling involved in cell fate commitment; IMP:WormBase.
DR GO; GO:0043054; P:dauer exit; IGI:WormBase.
DR GO; GO:0002119; P:nematode larval development; IGI:WormBase.
DR GO; GO:0007219; P:Notch signaling pathway; ISS:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0048337; P:positive regulation of mesodermal cell fate specification; IGI:UniProtKB.
DR GO; GO:0110011; P:regulation of basement membrane organization; IMP:UniProtKB.
DR GO; GO:0042659; P:regulation of cell fate specification; IMP:UniProtKB.
DR GO; GO:0042661; P:regulation of mesodermal cell fate specification; IMP:UniProtKB.
DR GO; GO:0040028; P:regulation of vulval development; IMP:UniProtKB.
DR GO; GO:0030431; P:sleep; IMP:UniProtKB.
DR GO; GO:0040025; P:vulval development; IMP:WormBase.
DR Gene3D; 1.25.40.20; -; 1.
DR IDEAL; IID50027; -.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
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; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00008; EGF; 6.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF12661; hEGF; 3.
DR Pfam; PF06816; NOD; 1.
DR Pfam; PF07684; NODP; 1.
DR Pfam; PF00066; Notch; 3.
DR PRINTS; PR01452; LNOTCHREPEAT.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00181; EGF; 13.
DR SMART; SM00179; EGF_CA; 9.
DR SMART; SM00004; NL; 3.
DR SMART; SM01338; NOD; 1.
DR SMART; SM01339; NODP; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR SUPFAM; SSF90193; SSF90193; 3.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS00022; EGF_1; 12.
DR PROSITE; PS01186; EGF_2; 11.
DR PROSITE; PS50026; EGF_3; 13.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS50258; LNR; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; ANK repeat; Cell membrane; Developmental protein;
KW Differentiation; Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW Notch signaling pathway; Nucleus; Reference proteome; Repeat; Signal;
KW Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..1429
FT /note="Protein lin-12"
FT /id="PRO_0000007634"
FT CHAIN ?..1429
FT /note="lin-12/Notch intracellular domain"
FT /evidence="ECO:0000305|PubMed:16530045,
FT ECO:0000305|PubMed:18036582"
FT /id="PRO_0000453171"
FT TOPO_DOM 16..908
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 909..931
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 932..1429
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..61
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 114..150
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 152..190
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 201..246
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 250..285
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 287..323
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 323..363
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 365..402
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 404..441
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 449..492
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 503..541
FT /note="EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 543..579
FT /note="EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 582..619
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 638..674
FT /note="LNR 1"
FT REPEAT 678..709
FT /note="LNR 2"
FT REPEAT 716..754
FT /note="LNR 3"
FT REPEAT 1093..1122
FT /note="ANK 1"
FT REPEAT 1126..1158
FT /note="ANK 2"
FT REPEAT 1162..1194
FT /note="ANK 3"
FT REPEAT 1206..1236
FT /note="ANK 4"
FT REPEAT 1240..1269
FT /note="ANK 5"
FT REGION 933..952
FT /note="RAM domain"
FT /evidence="ECO:0000303|PubMed:16530045,
FT ECO:0000303|PubMed:18381292"
FT REGION 1308..1374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 623
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 751
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 754
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 900
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..35
FT /evidence="ECO:0000250"
FT DISULFID 29..49
FT /evidence="ECO:0000250"
FT DISULFID 51..60
FT /evidence="ECO:0000250"
FT DISULFID 118..129
FT /evidence="ECO:0000250"
FT DISULFID 123..138
FT /evidence="ECO:0000250"
FT DISULFID 140..149
FT /evidence="ECO:0000250"
FT DISULFID 156..169
FT /evidence="ECO:0000250"
FT DISULFID 163..178
FT /evidence="ECO:0000250"
FT DISULFID 180..189
FT /evidence="ECO:0000250"
FT DISULFID 205..227
FT /evidence="ECO:0000250"
FT DISULFID 221..234
FT /evidence="ECO:0000250"
FT DISULFID 236..245
FT /evidence="ECO:0000250"
FT DISULFID 254..264
FT /evidence="ECO:0000250"
FT DISULFID 259..273
FT /evidence="ECO:0000250"
FT DISULFID 275..284
FT /evidence="ECO:0000250"
FT DISULFID 291..302
FT /evidence="ECO:0000250"
FT DISULFID 296..311
FT /evidence="ECO:0000250"
FT DISULFID 313..322
FT /evidence="ECO:0000250"
FT DISULFID 327..339
FT /evidence="ECO:0000250"
FT DISULFID 334..351
FT /evidence="ECO:0000250"
FT DISULFID 353..362
FT /evidence="ECO:0000250"
FT DISULFID 369..381
FT /evidence="ECO:0000250"
FT DISULFID 375..390
FT /evidence="ECO:0000250"
FT DISULFID 392..401
FT /evidence="ECO:0000250"
FT DISULFID 408..419
FT /evidence="ECO:0000250"
FT DISULFID 413..429
FT /evidence="ECO:0000250"
FT DISULFID 431..440
FT /evidence="ECO:0000250"
FT DISULFID 462..475
FT /evidence="ECO:0000250"
FT DISULFID 469..480
FT /evidence="ECO:0000250"
FT DISULFID 482..491
FT /evidence="ECO:0000250"
FT DISULFID 507..518
FT /evidence="ECO:0000250"
FT DISULFID 512..529
FT /evidence="ECO:0000250"
FT DISULFID 531..540
FT /evidence="ECO:0000250"
FT DISULFID 547..558
FT /evidence="ECO:0000250"
FT DISULFID 552..567
FT /evidence="ECO:0000250"
FT DISULFID 569..578
FT /evidence="ECO:0000250"
FT DISULFID 586..597
FT /evidence="ECO:0000250"
FT DISULFID 591..607
FT /evidence="ECO:0000250"
FT DISULFID 609..618
FT /evidence="ECO:0000250"
FT DISULFID 638..661
FT /evidence="ECO:0000250"
FT DISULFID 643..656
FT /evidence="ECO:0000250"
FT DISULFID 652..668
FT /evidence="ECO:0000250"
FT DISULFID 678..702
FT /evidence="ECO:0000250"
FT DISULFID 684..697
FT /evidence="ECO:0000250"
FT DISULFID 693..709
FT /evidence="ECO:0000250"
FT DISULFID 716..742
FT /evidence="ECO:0000250"
FT DISULFID 724..737
FT /evidence="ECO:0000250"
FT DISULFID 733..749
FT /evidence="ECO:0000250"
FT MUTAGEN 400..1429
FT /note="Missing: In n941; Increased total quiescence versus
FT control animals. Affects cell fates of ventral, but not
FT dorsal, postembryonic mesodermal lineage (M lineage).
FT Similar, but enhanced phenotype seen when combined with
FT RNAi-mediated knockdown of lag-2. On a sma-9 mutant
FT background, reverses the dorsoventral polarity of the M
FT lineage. Normal octanol response, but dramatically impaired
FT when combined with RNAi-mediated knockdown of glp-1/Notch
FT receptor."
FT /evidence="ECO:0000269|PubMed:18036582,
FT ECO:0000269|PubMed:21549604"
FT STRAND 938..941
FT /evidence="ECO:0007829|PDB:3BRD"
FT HELIX 1025..1031
FT /evidence="ECO:0007829|PDB:2FO1"
FT STRAND 1032..1034
FT /evidence="ECO:0007829|PDB:2FO1"
FT TURN 1042..1047
FT /evidence="ECO:0007829|PDB:2FO1"
FT HELIX 1056..1061
FT /evidence="ECO:0007829|PDB:2FO1"
FT HELIX 1072..1082
FT /evidence="ECO:0007829|PDB:2FO1"
FT HELIX 1097..1104
FT /evidence="ECO:0007829|PDB:2FO1"
FT HELIX 1107..1115
FT /evidence="ECO:0007829|PDB:2FO1"
FT HELIX 1130..1136
FT /evidence="ECO:0007829|PDB:2FO1"
FT HELIX 1140..1146
FT /evidence="ECO:0007829|PDB:2FO1"
FT HELIX 1150..1154
FT /evidence="ECO:0007829|PDB:2FO1"
FT HELIX 1166..1172
FT /evidence="ECO:0007829|PDB:2FO1"
FT HELIX 1178..1188
FT /evidence="ECO:0007829|PDB:2FO1"
FT HELIX 1197..1199
FT /evidence="ECO:0007829|PDB:2FO1"
FT STRAND 1201..1204
FT /evidence="ECO:0007829|PDB:2FO1"
FT HELIX 1211..1215
FT /evidence="ECO:0007829|PDB:2FO1"
FT HELIX 1220..1229
FT /evidence="ECO:0007829|PDB:2FO1"
FT HELIX 1244..1251
FT /evidence="ECO:0007829|PDB:2FO1"
FT HELIX 1254..1262
FT /evidence="ECO:0007829|PDB:2FO1"
FT STRAND 1272..1274
FT /evidence="ECO:0007829|PDB:2FO1"
FT HELIX 1277..1283
FT /evidence="ECO:0007829|PDB:2FO1"
FT HELIX 1287..1294
FT /evidence="ECO:0007829|PDB:2FO1"
SQ SEQUENCE 1429 AA; 157116 MW; 255EDD7A62C025DB CRC64;
MRIPTICFLF LLISLSKSLH IGSCLGLICG RNGHCHAGPV NGTQTSYWCR CDEGFGGEYC
EQQCDVSKCG ADEKCVFDKD YRMETCVCKD CDINGNSLLK PSCPSGYGGD DCKTQGWCYP
SVCMNGGQCI GAGNRAKCAC PDGFKGERCE LDVNECEENK NACGNRSTCM NTLGTYICVC
PQGFLPPDCL KPGNTSTVEF KQPVCFLEIS ADHPDGRSMY CQNGGFCDKA SSKCQCPPGY
HGSTCELLEK EDSCASNPCS HGVCISFSGG FQCICDDGYS GSYCQEGKDN CVNNKCEAGS
KCINGVNSYF CDCPPERTGP YCEKMDCSAI PDICNHGTCI DSPLSEKAFE CQCEPGYEGI
LCEQDKNECL SENMCLNNGT CVNLPGSFRC DCARGFGGKW CDEPLNMCQD FHCENDGTCM
HTSDHSPVCQ CKNGFIGKRC EKECPIGFGG VRCDLRLEIG ICSRQGGKCF NGGKCLSGFC
VCPPDFTGNQ CEVNRKNGKS SLSENLCLSD PCMNNATCID VDAHIGYACI CKQGFEGDIC
ERHKDLCLEN PCSNGGVCHQ HRESFSCDCP PGFYGNGCEQ EKMFRCLKST CQNGGVCINE
EEKGRKCECS YGFSGARCEE KINLTGFTEK DSLLRSVCEK RKCSERANDG NCDADCNYAA
CKFDGGDCSG KREPFSKCRY GNMCADFFAN GVCNQACNNE ECLYDGMDCL PAVVRCPVKI
REHCASRFAN GICDPECNTN GCGFDGGDCD NETNATIITN IRITVQMDPK EFQVTGGQSL
MEISSALRVT VRIQRDEEGP LVFQWNGESE MDRVKMNERQ LTEQHVLSTS ISRKIKRSAT
NIGVVVYLEV QENCDTGKCL YKDAQSVVDS ISARLAKKGI DSFGIPISEA LVAEPRKSGN
NTGFLSWNAL LLIGAGCLIV MVVLMLGALP GNRTRKRRMI NASVWMPPME NEEKNRKNHQ
SITSSQHSLL EASYDGYIKR QRNELQHYSL YPNPQGYGNG NDFLGDFNHT NLQIPTEPEP
ESPIKLHTEA AGSYAITEPI TRESVNIIDP RHNRTVLHWI ASNSSAEKSE DLIVHEAKEC
IAAGADVNAM DCDENTPLML AVLARRRRLV AYLMKAGADP TIYNKSERSA LHQAAANRDF
GMMVYMLNST KLKGDIEELD RNGMTALMIV AHNEGRDQVA SAKLLVEKGA KVDYDGAARK
DSEKYKGRTA LHYAAQVSNM PIVKYLVGEK GSNKDKQDED GKTPIMLAAQ EGRIEVVMYL
IQQGASVEAV DATDHTARQL AQANNHHNIV DIFDRCRPER EYSMDLHIQH THQPQPSRKV
TRAPKKQTSR SKKESASNSR DSTHLTPPPS DGSTSTPSPQ HFMNTTHTTP TSLNYLSPEY
QTEAGSSEAF QPQCGAFGNG EMWYTRASTS YTQMQNEPMT RYSEPAHYF
