ID   LIN49_CAEEL             Reviewed;        1042 AA.
AC   Q20318;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Protein lin-49;
DE   AltName: Full=Abnormal cell lineage protein 49;
GN   Name=lin-49; ORFNames=F42A9.2;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS
RP   OF CYS-325 AND CYS-330.
RC   STRAIN=Bristol N2;
RX   PubMed=10648230; DOI=10.1242/dev.127.4.713;
RA   Chamberlin H.M., Thomas J.H.;
RT   "The bromodomain protein LIN-49 and trithorax-related protein LIN-59 affect
RT   development and gene expression in Caenorhabditis elegans.";
RL   Development 127:713-723(2000).
RN   [2]
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   [3]
RP   FUNCTION.
RX   PubMed=20923973; DOI=10.1534/genetics.110.123661;
RA   O'Meara M.M., Zhang F., Hobert O.;
RT   "Maintenance of neuronal laterality in Caenorhabditis elegans through MYST
RT   histone acetyltransferase complex components LSY-12, LSY-13 and LIN-49.";
RL   Genetics 186:1497-1502(2010).
CC   -!- FUNCTION: Required to initiate and then maintain lateralized gene
CC       expression in the ASE sensory neurons (PubMed:20923973). Involved in
CC       determining cell fate in the ASE neurons (PubMed:20923973). Essential
CC       protein required to maintain expression of homeotic genes egl-5 and
CC       mab-5 (PubMed:10648230). May play an analogous role to the trithorax
CC       Group (trxG) proteins (PubMed:10648230). TrxG proteins form
CC       multiprotein complexes that are required to maintain the
CC       transcriptionally active state of homeotic genes throughout development
CC       (PubMed:10648230). May act via a modification of chromatin
CC       (PubMed:10648230). {ECO:0000269|PubMed:10648230,
CC       ECO:0000269|PubMed:20923973}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Widely expressed throughout embryonic development
CC       and into adulthood. {ECO:0000269|PubMed:10648230}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from mid-blastula.
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DR   EMBL; AF163018; AAD49323.1; -; mRNA.
DR   EMBL; FO080904; CCD67656.1; -; Genomic_DNA.
DR   PIR; T29307; T29307.
DR   RefSeq; NP_501475.1; NM_069074.5.
DR   AlphaFoldDB; Q20318; -.
DR   SMR; Q20318; -.
DR   STRING; 6239.F42A9.2.2; -.
DR   iPTMnet; Q20318; -.
DR   EPD; Q20318; -.
DR   PaxDb; Q20318; -.
DR   PeptideAtlas; Q20318; -.
DR   PRIDE; Q20318; -.
DR   EnsemblMetazoa; F42A9.2.1; F42A9.2.1; WBGene00003034.
DR   GeneID; 177666; -.
DR   KEGG; cel:CELE_F42A9.2; -.
DR   UCSC; F42A9.2; c. elegans.
DR   CTD; 177666; -.
DR   WormBase; F42A9.2; CE07224; WBGene00003034; lin-49.
DR   eggNOG; KOG0955; Eukaryota.
DR   GeneTree; ENSGT00940000169333; -.
DR   HOGENOM; CLU_306587_0_0_1; -.
DR   InParanoid; Q20318; -.
DR   OMA; WVDETHF; -.
DR   OrthoDB; 566217at2759; -.
DR   PhylomeDB; Q20318; -.
DR   PRO; PR:Q20318; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00003034; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0018205; P:peptidyl-lysine modification; IEA:UniProt.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.20.920.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 2.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF00439; Bromodomain; 1.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00249; PHD; 2.
DR   SUPFAM; SSF47370; SSF47370; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   1: Evidence at protein level;
KW   Activator; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..1042
FT                   /note="Protein lin-49"
FT                   /id="PRO_0000211205"
FT   DOMAIN          523..593
FT                   /note="Bromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   ZN_FING         195..245
FT                   /note="PHD-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   ZN_FING         249..282
FT                   /note="C2HC pre-PHD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT   ZN_FING         306..366
FT                   /note="PHD-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT   REGION          647..864
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..685
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        695..717
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        718..737
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        746..864
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         325
FT                   /note="C->S: In SA470; reduced activity."
FT                   /evidence="ECO:0000269|PubMed:10648230"
FT   MUTAGEN         330
FT                   /note="C->Y: In SY238; reduced activity."
FT                   /evidence="ECO:0000269|PubMed:10648230"
SQ   SEQUENCE   1042 AA;  117643 MW;  8ED000257E202B84 CRC64;
     MGRGRGVAIQ ETIEECRDTI SDRIQYNLGL NESKVVLMDI VTGPNQNVSL QERTKRWMAV
     SVDARMTKFK KNFYPTNQKN SKNISKDLDP PIQRVDAHIV TPVAGKCGMP LQKFPEFKHD
     HEKIKIERDA KYVDYSVDEF DMSWMSIMNA KRTKLGLEIF SVAIYEHWVD RLEKMCIWKP
     KEFHKLKDEN GEELDDVCNI CLDGDTSNCN QIVYCDRCNL SVHQDCYGIP FIPEGCLECR
     RCGISPAGRV NCVLCPSTTG AFKQVDQKRW VHVLCVIWVD ETHFGNTIFM ENVQNVEKAL
     HDRRALSCLL CKNRQNARMG ACIQCSETKC TASFHVTCAR DSGLVMRINE TEDGQVNRFV
     WCPKHAPPLT DADREMRQLM LRNARRENER KGPMISMPTL MKSMISTICV ERPFSDYSEI
     IYFWYEKRLN RLGAPLLKNF TQGASKSRRL LPKSTICGQL KNVETCEMKK QVNAVKESLA
     SGLEIFDMIV RREERKKDML NSYIRMFERG FKPTELLCQE VIEALKTIDA GKVFAEPVEL
     VGYTDIIENP ICLKDMSEKA ASGKYSTVAA LSADVQLMLS NCATFNKGNR VYIKYGNTYR
     KDSTPILEIA EKEEVERLAL KTDEKFMTQL LNGVMVEYNG WAQSRNEVAK EIPPPTPSRG
     RGTGRRRQNP FLDVQELDTD DSKDSSALSE IPGSSKKSSR KRGIQDTKME EDEEIKPSTS
     GTNAVASVPL LSSSRESKNK SKSSDADVSS PKSSWLGSPS TSQNLRRRVQ GFSGNESSPK
     VHKKLSTDNP SNSNLRQTTL TNFFGTNPKT QQQVTFADMT ATPSGSGNKN VSQRSLFDTP
     STSKASSFTS LSSTRPSTRS TSIIPTINKK NAFRMSSASI QSPLPTTKKI GVRAMATDDE
     EEDIVIQPPP KEMTTQELEA EKLKSAENEA MSKFAHNQLV IVDGRAAKVI ESRLAHLASD
     IHHEQRQSMM KKRREVLSEI PQAAVIYVEF FQKSNTLENF QWVTPDKVEL LDLNNIGQRS
     PKIPGLKAAK EWHQKVLNGE DV