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LIN61_CAEEL
ID   LIN61_CAEEL             Reviewed;         612 AA.
AC   B2D6M2; Q21769;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Protein lin-61;
DE   AltName: Full=Abnormal cell lineage protein 61;
GN   Name=lin-61; ORFNames=R06C7.7;
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 [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).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP   AND MUTAGENESIS OF PRO-253; PHE-368; GLY-371 AND SER-475.
RX   PubMed=17409073; DOI=10.1534/genetics.106.069633;
RA   Harrison M.M., Lu X., Horvitz H.R.;
RT   "LIN-61, one of two Caenorhabditis elegans malignant-brain-tumor-repeat-
RT   containing proteins, acts with the DRM and NuRD-like protein complexes in
RT   vulval development but not in certain other biological processes.";
RL   Genetics 176:255-271(2007).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH HISTONE H3,
RP   DISRUPTION PHENOTYPE, DOMAIN MBT, AND MUTAGENESIS OF ASP-549; PHE-573;
RP   TRP-576 AND PHE-580.
RC   STRAIN=Bristol N2;
RX   PubMed=21437264; DOI=10.1371/journal.pgen.1002017;
RA   Koester-Eiserfunke N., Fischle W.;
RT   "H3K9me2/3 binding of the MBT domain protein LIN-61 is essential for
RT   Caenorhabditis elegans vulva development.";
RL   PLoS Genet. 7:E1002017-E1002017(2011).
CC   -!- FUNCTION: Synthetic multivulva class B (synMuvB) protein required to
CC       repress the induction of vulval development by Ras signaling. Unlike
CC       other synMuv proteins it does not associate with the multiprotein DRM
CC       complex and the NuRD-like complex. Interaction with methylated histone
CC       H3 is essential for vulva development. It has a role in maintaining
CC       genome stability. {ECO:0000269|PubMed:17409073,
CC       ECO:0000269|PubMed:21437264}.
CC   -!- SUBUNIT: Interacts preferentially with histone H3 that is dimethylated
CC       or trimethylated at 'Lys-9'. {ECO:0000269|PubMed:21437264}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17409073}. Chromosome
CC       {ECO:0000269|PubMed:17409073}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=b;
CC         IsoId=B2D6M2-1; Sequence=Displayed;
CC       Name=a;
CC         IsoId=B2D6M2-2; Sequence=VSP_043612;
CC   -!- DEVELOPMENTAL STAGE: Expressed from the one-cell embryo to the adult
CC       (at protein level). {ECO:0000269|PubMed:17409073}.
CC   -!- DOMAIN: The MBT repeats specifically recognize and bind histone H3
CC       di- and tri-methylated at 'Lys-9' (H3K9me2/3).
CC       {ECO:0000269|PubMed:21437264}.
CC   -!- DISRUPTION PHENOTYPE: Multivulva phenotype in combination with loss of
CC       function of class A synMuv genes lin-8, lin-38, lin-56 and lin15A and
CC       with the class B synMuv gene hpl-2. Reduction of brood size and defects
CC       in the development of germ cells. Loss of function results in
CC       suppression of mat-3(ku233) mutant vulval phenotype.
CC       {ECO:0000269|PubMed:17409073, ECO:0000269|PubMed:21437264}.
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DR   EMBL; Z71266; CAA95838.3; -; Genomic_DNA.
DR   EMBL; Z71266; CAQ35053.1; -; Genomic_DNA.
DR   PIR; T23964; T23964.
DR   RefSeq; NP_001122501.1; NM_001129029.1. [B2D6M2-1]
DR   RefSeq; NP_492050.3; NM_059649.4. [B2D6M2-2]
DR   AlphaFoldDB; B2D6M2; -.
DR   SMR; B2D6M2; -.
DR   BioGRID; 37910; 3.
DR   STRING; 6239.R06C7.7b; -.
DR   EPD; B2D6M2; -.
DR   PaxDb; B2D6M2; -.
DR   PeptideAtlas; B2D6M2; -.
DR   PRIDE; B2D6M2; -.
DR   EnsemblMetazoa; R06C7.7a.1; R06C7.7a.1; WBGene00003041. [B2D6M2-2]
DR   EnsemblMetazoa; R06C7.7b.1; R06C7.7b.1; WBGene00003041. [B2D6M2-1]
DR   GeneID; 172467; -.
DR   KEGG; cel:CELE_R06C7.7; -.
DR   UCSC; R06C7.7a.1; c. elegans.
DR   CTD; 172467; -.
DR   WormBase; R06C7.7a; CE37542; WBGene00003041; lin-61. [B2D6M2-2]
DR   WormBase; R06C7.7b; CE31573; WBGene00003041; lin-61. [B2D6M2-1]
DR   eggNOG; KOG3766; Eukaryota.
DR   GeneTree; ENSGT00940000169237; -.
DR   InParanoid; B2D6M2; -.
DR   OMA; ISECFAT; -.
DR   OrthoDB; 1334498at2759; -.
DR   PhylomeDB; B2D6M2; -.
DR   PRO; PR:B2D6M2; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00003041; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0000785; C:chromatin; IDA:WormBase.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0040025; P:vulval development; IGI:WormBase.
DR   InterPro; IPR004092; Mbt.
DR   Pfam; PF02820; MBT; 3.
DR   SMART; SM00561; MBT; 3.
DR   PROSITE; PS51079; MBT; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromosome; Nucleus; Reference proteome; Repeat.
FT   CHAIN           1..612
FT                   /note="Protein lin-61"
FT                   /id="PRO_0000417369"
FT   REPEAT          143..249
FT                   /note="MBT 1"
FT   REPEAT          263..380
FT                   /note="MBT 2"
FT   REPEAT          381..501
FT                   /note="MBT 3"
FT   REPEAT          508..607
FT                   /note="MBT 4"
FT   VAR_SEQ         1..121
FT                   /note="Missing (in isoform a)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_043612"
FT   MUTAGEN         253
FT                   /note="P->S: In allele lin-61(n3624); does not affect
FT                   binding to histone H3 trimethylated at 'Lys-9'; multivulva
FT                   phenotype in combination with lin56(n2728)."
FT                   /evidence="ECO:0000269|PubMed:17409073"
FT   MUTAGEN         368
FT                   /note="F->S: In allele lin-61(n3736); reduces binding to
FT                   histone H3 trimethylated at 'Lys-9'; multivulva phenotype
FT                   in combination with lin56(n2728)."
FT                   /evidence="ECO:0000269|PubMed:17409073"
FT   MUTAGEN         371
FT                   /note="G->E: In allele lin-61(n3807); abolishes binding to
FT                   histone H3 trimethylated at 'Lys-9'; multivulva phenotype
FT                   in combination with lin56(n2728)."
FT                   /evidence="ECO:0000269|PubMed:17409073"
FT   MUTAGEN         475
FT                   /note="S->N: In allele lin-61(n3447); reduces binding to
FT                   histone H3 trimethylated at 'Lys-9'; multivulva phenotype
FT                   in combination with lin56(n2728)."
FT                   /evidence="ECO:0000269|PubMed:17409073"
FT   MUTAGEN         549
FT                   /note="D->A: Reduces binding to histone H3 trimethylated at
FT                   'Lys-9'; in isoform a."
FT                   /evidence="ECO:0000269|PubMed:21437264"
FT   MUTAGEN         573
FT                   /note="F->A: Abolishes binding to histone H3 trimethylated
FT                   at 'Lys-9'; when associated A-576 and A-580, in isoform a."
FT                   /evidence="ECO:0000269|PubMed:21437264"
FT   MUTAGEN         576
FT                   /note="W->A: Abolishes binding to histone H3 trimethylated
FT                   at 'Lys-9'; in isoform a."
FT                   /evidence="ECO:0000269|PubMed:21437264"
FT   MUTAGEN         580
FT                   /note="F->A: Abolishes binding to histone H3 trimethylated
FT                   at 'Lys-9'; in isoform a."
FT                   /evidence="ECO:0000269|PubMed:21437264"
SQ   SEQUENCE   612 AA;  70910 MW;  D0A1B0156C73C254 CRC64;
     MLKLVILCFA LFYNTVSSTR FLFGVEVKCD FDEVFQLTVS HWEDDGNTFW DRDEDITGRM
     TMFARKKIFF YQDGHHGFEF GKLEPYGWFL HNCTKNGNFR EYRHGLSSTS GSNGLEYIEY
     TMSEFLKIVR ANKKSDRKLD KTYLWESYLH QFEKGKTSFI PVEAFNRNLT VNFNECVKEG
     VIFETVVHDY DKNCDSIQVR WFARIEKVCG YRVLAQFIGA DTKFWLNILS DDMFGLANAA
     MSDPNMDKIV YAPPLAINEE YQNDMVNYVN NCIDGEIVGQ TSLSPKFDEG KALLSKHRFK
     VGQRLELLNY SNSTEIRVAR IQEICGRRMN VSITKKDFPE SLPDADDDRQ VFSSGSQYWI
     DEGSFFIFPV GFAAVNGYQL NAKKEYIEHT NKIAQAIKNG ENPRYDSDDV TFDQLAKDPI
     DPMIWRKVKV GQKFELIDPL AQQFNNLHVA SILKFCKTEG YLIVGMDGPD ALEDSFPIHI
     NNTFMFPVGY AEKYNLELVP PDEFKGTFRW DEYLEKESAE TLPLDLFKPM PSQERLDKFK
     VGLRLEAADM CENQFICPAT VKSVHGRLIN VNFDGWDEEF DELYDVDSHD ILPIGWCEAH
     SYVLQPPKKY NY
 
 
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