NLK_CAEEL
ID NLK_CAEEL Reviewed; 634 AA.
AC Q9U9Y8; O62395; Q69YW9; Q8WQB7; Q9U343; Q9UA07; Q9Y198;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Serine/threonine kinase NLK {ECO:0000250|UniProtKB:O54949};
DE EC=2.7.11.24 {ECO:0000250|UniProtKB:O54949};
DE AltName: Full=Loss of intestine protein 1;
DE AltName: Full=Nemo-like kinase {ECO:0000250|UniProtKB:O54949};
GN Name=lit-1 {ECO:0000303|PubMed:10380924, ECO:0000312|WormBase:W06F12.1a};
GN Synonyms=nlk {ECO:0000250|UniProtKB:O54949};
GN ORFNames=W06F12.1 {ECO:0000312|WormBase:W06F12.1a};
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:AAD37360.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND E), FUNCTION, IDENTIFICATION IN
RP THE BETA-CATENIN-LIT-1 COMPLEX, INTERACTION WITH WRM-1 AND POP-1,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LEU-357.
RX PubMed=10380924; DOI=10.1016/s0092-8674(00)80784-9;
RA Rocheleau C.E., Yasuda J., Shin T.H., Lin R., Sawa H., Okano H.,
RA Priess J.R., Davis R.J., Mello C.C.;
RT "WRM-1 activates the LIT-1 protein kinase to transduce anterior/posterior
RT polarity signals in C. elegans.";
RL Cell 97:717-726(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAD39815.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF CYS-541.
RX PubMed=10391246; DOI=10.1038/21666;
RA Meneghini M.D., Ishitani T., Carter J.C., Hisamoto N., Ninomiya-Tsuji J.,
RA Thorpe C.J., Hamill D.R., Matsumoto K., Bowerman B.;
RT "MAP kinase and Wnt pathways converge to downregulate an HMG-domain
RT repressor in Caenorhabditis elegans.";
RL Nature 399:793-797(1999).
RN [3] {ECO:0000312|EMBL:CAB05827.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAB05827.2};
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] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LEU-357 AND GLU-402.
RX PubMed=9384382; DOI=10.1038/36869;
RA Kaletta T., Schnabel H., Schnabel R.;
RT "Binary specification of the embryonic lineage in Caenorhabditis elegans.";
RL Nature 390:294-298(1997).
RN [5] {ECO:0000305}
RP MUTAGENESIS OF THR-400.
RX PubMed=10488343; DOI=10.1016/s1097-2765(00)80375-5;
RA Shin T.H., Yasuda J., Rocheleau C.E., Lin R., Soto M., Bei Y., Davis R.J.,
RA Mello C.C.;
RT "MOM-4, a MAP kinase kinase kinase-related protein, activates WRM-1/LIT-1
RT kinase to transduce anterior/posterior polarity signals in C. elegans.";
RL Mol. Cell 4:275-280(1999).
RN [6] {ECO:0000305}
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 [7] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE BETA-CATENIN-LIT-1 COMPLEX, INTERACTION
RP WITH WRM-1 AND POP-1, AND SUBCELLULAR LOCATION.
RX PubMed=15066285; DOI=10.1016/s0092-8674(04)00203-x;
RA Lo M.-C., Gay F., Odom R., Shi Y., Lin R.;
RT "Phosphorylation by the beta-catenin/MAPK complex promotes 14-3-3-mediated
RT nuclear export of TCF/POP-1 in signal-responsive cells in C. elegans.";
RL Cell 117:95-106(2004).
RN [8] {ECO:0000305}
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF CYS-541.
RX PubMed=15489294; DOI=10.1101/gad.1218504;
RA Shostak Y., Van Gilst M.R., Antebi A., Yamamoto K.R.;
RT "Identification of C. elegans DAF-12-binding sites, response elements, and
RT target genes.";
RL Genes Dev. 18:2529-2544(2004).
RN [9] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=16077003; DOI=10.1101/gad.1322805;
RA Takeshita H., Sawa H.;
RT "Asymmetric cortical and nuclear localizations of WRM-1/beta-catenin during
RT asymmetric cell division in C. elegans.";
RL Genes Dev. 19:1743-1748(2005).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19084000; DOI=10.1016/j.ydbio.2008.11.015;
RA Witze E.S., Field E.D., Hunt D.F., Rothman J.H.;
RT "C. elegans pur alpha, an activator of end-1, synergizes with the Wnt
RT pathway to specify endoderm.";
RL Dev. Biol. 327:12-23(2009).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21408209; DOI=10.1371/journal.pgen.1002010;
RA Nelson M.D., Zhou E., Kiontke K., Fradin H., Maldonado G., Martin D.,
RA Shah K., Fitch D.H.;
RT "A bow-tie genetic architecture for morphogenesis suggested by a genome-
RT wide RNAi screen in Caenorhabditis elegans.";
RL PLoS Genet. 7:E1002010-E1002010(2011).
CC -!- FUNCTION: Has a role in the Wnt signaling pathway controlling the
CC asymmetry of cell divisions during embryogenesis (PubMed:10380924).
CC Operates in the AB and EMS cell lineages influencing cell specification
CC (PubMed:10391246). Required for body wall muscle development, endoderm
CC development, pop-1 asymmetry and T-cell division asymmetry
CC (PubMed:10380924, PubMed:9384382). Component of the beta-catenin-lit-1
CC complex which promotes the phosphorylation, down-regulation and
CC subcellular relocation of pop-1 (PubMed:15066285, PubMed:10380924).
CC Regulates plp-1 nuclear localization in embryos (PubMed:19084000).
CC Plays a role in male tail tip morphogenesis (PubMed:21408209).
CC {ECO:0000269|PubMed:10380924, ECO:0000269|PubMed:10391246,
CC ECO:0000269|PubMed:15066285, ECO:0000269|PubMed:19084000,
CC ECO:0000269|PubMed:21408209, ECO:0000269|PubMed:9384382}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24;
CC Evidence={ECO:0000250|UniProtKB:O54949};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.24; Evidence={ECO:0000250|UniProtKB:O54949};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O54949};
CC -!- SUBUNIT: Component of the beta-catenin-lit-1 complex (also called the
CC lit-1/wrm-1 complex or the wrm-1/lit-1 kinase complex) at least
CC composed of lit-1 and wrm-1 (PubMed:10380924, PubMed:15066285).
CC Interacts with wrm-1 (via N-terminus); the interaction is direct and
CC activates lit-1 kinase activity which leads to the phosphorylation of
CC pop-1 (PubMed:10380924, PubMed:15066285). This promotes pop-1
CC interaction with par-5 and translocation of pop-1 from the nucleus to
CC the cytoplasm (PubMed:15066285). Interacts with pop-1 (when
CC phosphorylated on 'Ser-118' and 'Ser-127'); the interaction is
CC dependent on the beta-catenin-lit-1 complex (PubMed:10380924,
CC PubMed:15066285). {ECO:0000269|PubMed:10380924,
CC ECO:0000269|PubMed:15066285}.
CC -!- INTERACTION:
CC Q9U9Y8; Q9U1S2: brp-1; NbExp=3; IntAct=EBI-318513, EBI-313822;
CC Q9U9Y8; Q21636: CELE_R02D5.1; NbExp=6; IntAct=EBI-318513, EBI-329142;
CC Q9U9Y8; O76449: CELE_ZK1055.7; NbExp=3; IntAct=EBI-318513, EBI-313622;
CC Q9U9Y8; O45734: cpl-1; NbExp=2; IntAct=EBI-318513, EBI-315958;
CC Q9U9Y8; Q19749: dlat-1; NbExp=2; IntAct=EBI-318513, EBI-320763;
CC Q9U9Y8; Q18171: spe-44; NbExp=3; IntAct=EBI-318513, EBI-320157;
CC Q9U9Y8; Q10953: wrm-1; NbExp=8; IntAct=EBI-318513, EBI-2530558;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:15066285, ECO:0000269|PubMed:16077003}. Nucleus
CC {ECO:0000269|PubMed:15066285, ECO:0000269|PubMed:16077003,
CC ECO:0000269|PubMed:21408209}. Note=Located in the anterior cell cortex
CC before and during asymmetric cell division. After division, located
CC preferentially in the nucleus of the posterior daughter cell. Localizes
CC to the nucleus in hyp9 and hyp10 cells prior to male tail tip
CC morphogenesis (PubMed:21408209). {ECO:0000269|PubMed:15066285,
CC ECO:0000269|PubMed:16077003, ECO:0000269|PubMed:21408209}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=a {ECO:0000303|PubMed:10391246, ECO:0000312|WormBase:W06F12.1a};
CC IsoId=Q9U9Y8-1; Sequence=Displayed;
CC Name=b {ECO:0000303|PubMed:10380924, ECO:0000312|WormBase:W06F12.1b};
CC IsoId=Q9U9Y8-2; Sequence=VSP_052847, VSP_052850;
CC Name=c {ECO:0000312|WormBase:W06F12.1c};
CC IsoId=Q9U9Y8-3; Sequence=VSP_052845, VSP_052851;
CC Name=d {ECO:0000312|WormBase:W06F12.1c};
CC IsoId=Q9U9Y8-4; Sequence=VSP_052848, VSP_052849;
CC Name=e {ECO:0000303|PubMed:10380924, ECO:0000312|WormBase:W06F12.1e};
CC IsoId=Q9U9Y8-5; Sequence=VSP_052846;
CC -!- TISSUE SPECIFICITY: Expressed in the pharynx and seam and vulval cells.
CC {ECO:0000269|PubMed:15489294}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the pharynx and seam and vulval cells
CC in larvae (PubMed:15489294). Expressed in the male tail tip during the
CC L4 larval stage (PubMed:21408209). {ECO:0000269|PubMed:15489294,
CC ECO:0000269|PubMed:21408209}.
CC -!- DISRUPTION PHENOTYPE: Defects in body wall muscle, endoderm development
CC and pop-1 asymmetry (PubMed:10380924, PubMed:10391246, PubMed:9384382).
CC RNAi-mediated knockdown disrupts tail tip morphogenesis resulting in
CC retention of the pointed larval tail tip in adult males (also known as
CC the Lep phenotype) (PubMed:21408209). RNAi-mediated knockdown causes
CC the transcription factor plp-1 to localize at much lower levels in
CC nuclei and instead accumulate in the cytoplasm, during embryonic
CC development. {ECO:0000269|PubMed:10380924, ECO:0000269|PubMed:10391246,
CC ECO:0000269|PubMed:19084000, ECO:0000269|PubMed:21408209,
CC ECO:0000269|PubMed:9384382}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000255}.
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DR EMBL; AF143243; AAD37360.1; -; mRNA.
DR EMBL; AF143244; AAD37361.1; -; mRNA.
DR EMBL; AF145376; AAD39815.1; -; mRNA.
DR EMBL; BX284603; CAB05827.2; -; Genomic_DNA.
DR EMBL; BX284603; CAB60300.2; -; Genomic_DNA.
DR EMBL; BX284603; CAD18878.1; -; Genomic_DNA.
DR EMBL; BX284603; CAH10803.1; -; Genomic_DNA.
DR EMBL; BX284603; CAH10804.1; -; Genomic_DNA.
DR EMBL; Z92822; CAH10804.1; JOINED; Genomic_DNA.
DR PIR; T26240; T26240.
DR RefSeq; NP_001022805.1; NM_001027634.2. [Q9U9Y8-1]
DR RefSeq; NP_001022806.1; NM_001027635.2. [Q9U9Y8-2]
DR RefSeq; NP_001022807.1; NM_001027636.2. [Q9U9Y8-3]
DR RefSeq; NP_001022808.1; NM_001027637.3. [Q9U9Y8-4]
DR RefSeq; NP_001022809.1; NM_001027638.3.
DR AlphaFoldDB; Q9U9Y8; -.
DR SMR; Q9U9Y8; -.
DR BioGRID; 41974; 83.
DR ComplexPortal; CPX-1130; Beta-catenin-lit-1 complex.
DR DIP; DIP-25624N; -.
DR IntAct; Q9U9Y8; 42.
DR STRING; 6239.W06F12.1a; -.
DR EPD; Q9U9Y8; -.
DR PaxDb; Q9U9Y8; -.
DR PeptideAtlas; Q9U9Y8; -.
DR EnsemblMetazoa; W06F12.1a.1; W06F12.1a.1; WBGene00003048. [Q9U9Y8-1]
DR EnsemblMetazoa; W06F12.1b.1; W06F12.1b.1; WBGene00003048. [Q9U9Y8-2]
DR EnsemblMetazoa; W06F12.1c.1; W06F12.1c.1; WBGene00003048. [Q9U9Y8-3]
DR EnsemblMetazoa; W06F12.1d.1; W06F12.1d.1; WBGene00003048. [Q9U9Y8-4]
DR EnsemblMetazoa; W06F12.1d.2; W06F12.1d.2; WBGene00003048. [Q9U9Y8-4]
DR EnsemblMetazoa; W06F12.1d.3; W06F12.1d.3; WBGene00003048. [Q9U9Y8-4]
DR EnsemblMetazoa; W06F12.1e.1; W06F12.1e.1; WBGene00003048. [Q9U9Y8-5]
DR GeneID; 176808; -.
DR KEGG; cel:CELE_W06F12.1; -.
DR UCSC; W06F12.1d; c. elegans.
DR CTD; 176808; -.
DR WormBase; W06F12.1a; CE29476; WBGene00003048; lit-1. [Q9U9Y8-1]
DR WormBase; W06F12.1b; CE29477; WBGene00003048; lit-1. [Q9U9Y8-2]
DR WormBase; W06F12.1c; CE29478; WBGene00003048; lit-1. [Q9U9Y8-3]
DR WormBase; W06F12.1d; CE37160; WBGene00003048; lit-1. [Q9U9Y8-4]
DR WormBase; W06F12.1e; CE37161; WBGene00003048; lit-1. [Q9U9Y8-5]
DR eggNOG; KOG0664; Eukaryota.
DR GeneTree; ENSGT00940000168938; -.
DR InParanoid; Q9U9Y8; -.
DR OMA; DGARCHI; -.
DR OrthoDB; 741207at2759; -.
DR PhylomeDB; Q9U9Y8; -.
DR Reactome; R-CEL-4086398; Ca2+ pathway.
DR SignaLink; Q9U9Y8; -.
DR PRO; PR:Q9U9Y8; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003048; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005938; C:cell cortex; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:1902554; C:serine/threonine protein kinase complex; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008013; F:beta-catenin binding; IPI:WormBase.
DR GO; GO:0004707; F:MAP kinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:WormBase.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:WormBase.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IGI:WormBase.
DR GO; GO:0008356; P:asymmetric cell division; IMP:WormBase.
DR GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IMP:WormBase.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0007492; P:endoderm development; IMP:UniProtKB.
DR GO; GO:0001714; P:endodermal cell fate specification; IMP:WormBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0042694; P:muscle cell fate specification; IMP:WormBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:WormBase.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:WormBase.
DR GO; GO:0009949; P:polarity specification of anterior/posterior axis; IMP:ComplexPortal.
DR GO; GO:0010085; P:polarity specification of proximal/distal axis; IMP:WormBase.
DR GO; GO:0110039; P:positive regulation of nematode male tail tip morphogenesis; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:WormBase.
DR GO; GO:0016055; P:Wnt signaling pathway; IGI:WormBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01351; MAPK; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Developmental protein;
KW Kinase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Wnt signaling pathway.
FT CHAIN 1..634
FT /note="Serine/threonine kinase NLK"
FT /id="PRO_0000372802"
FT DOMAIN 240..531
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 366
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 246..254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 269
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..197
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_052845"
FT VAR_SEQ 1..180
FT /note="Missing (in isoform e)"
FT /evidence="ECO:0000303|PubMed:10380924"
FT /id="VSP_052846"
FT VAR_SEQ 1..172
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:10380924"
FT /id="VSP_052847"
FT VAR_SEQ 1..33
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_052848"
FT VAR_SEQ 34..51
FT /note="KDTEDEFCGCLFPDPEIP -> MGRNQEGQFNGAGNSESA (in isoform
FT d)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_052849"
FT VAR_SEQ 173..178
FT /note="HHQQLV -> MRDMIY (in isoform b)"
FT /evidence="ECO:0000303|PubMed:10380924"
FT /id="VSP_052850"
FT VAR_SEQ 198..216
FT /note="YEKNQQKQQQVQQIPTQPQ -> MILIAIIESFIEYLRKIVW (in
FT isoform c)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_052851"
FT MUTAGEN 357
FT /note="L->S: In t1512; intestine cells absent but have an
FT excess of pharyngeal cells, symmetrical localization of
FT pop-1 and symmetrical T-cell division."
FT /evidence="ECO:0000269|PubMed:10380924,
FT ECO:0000269|PubMed:9384382"
FT MUTAGEN 400
FT /note="T->A: No detectable kinase activity."
FT /evidence="ECO:0000269|PubMed:10488343"
FT MUTAGEN 402
FT /note="E->K: In t1534; reduced body-wall muscle."
FT /evidence="ECO:0000269|PubMed:9384382"
FT MUTAGEN 541
FT /note="C->Y: In or131; loss of pop-1 asymmetry and
FT protruding vulva phenotype and defects in gonadal migration
FT and development."
FT /evidence="ECO:0000269|PubMed:10391246,
FT ECO:0000269|PubMed:15489294"
SQ SEQUENCE 634 AA; 71777 MW; A9F2EA7E3E2CE7F5 CRC64;
MVSWGRGKDA YYLYISREQE EDDDDSLSFY SSQKDTEDEF CGCLFPDPEI PGSSSSSGCS
SSSTELYDLA AAHAALISRQ QQILSQAIPI IPEHQLAAVA AHHQHHQQLH PSVQYQLVAA
ATHHNHHQPQ AAQPHYSAVV PRSDVIQQPP HFALHHHLQN LVQQQQQQQA HHHHQQLVGE
MALVSHTHPA AVGSTTCYEK NQQKQQQVQQ IPTQPQVAHV SSNAILAAAQ PFYPPPVQDS
QPDRPIGYGA FGVVWSVTDP RSGKRVALKK MPNVFQNLAS CKRVFREIKM LSSFRHDNVL
SLLDILQPAN PSFFQELYVL TELMQSDLHK IIVSPQALTP DHVKVFVYQI LRGLKYLHTA
NILHRDIKPG NLLVNSNCIL KICDFGLART WDQRDRLNMT HEVVTQYYRA PELLMGARRY
TGAVDIWSVG CIFAELLQRK ILFQAAGPIE QLQMIIDLLG TPSQEAMKYA CEGAKNHVLR
AGLRAPDTQR LYKIASPDDK NHEAVDLLQK LLHFDPDKRI SVEEALQHRY LEEGRLRFHS
CMCSCCYTKP NMPSRLFAQD LDPRHESPFD PKWEKDMSRL SMFELREKMY QFVMDRPALY
GVALCINPQS AAYKNFASSS VAQASELPPS PQAW
