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 27-MAR-2024, entry version 153.
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.F42A9.2.1; -.
DR iPTMnet; Q20318; -.
DR EPD; Q20318; -.
DR PaxDb; 6239-F42A9-2-2; -.
DR PeptideAtlas; 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 AGR; WB:WBGene00003034; -.
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; WHQKVLN; -.
DR OrthoDB; 2883181at2759; -.
DR PhylomeDB; Q20318; -.
DR PRO; PR:Q20318; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00003034; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR GO; GO:0001708; P:cell fate specification; IMP:UniProtKB.
DR GO; GO:0061968; P:maintenance of left/right asymmetry; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd04369; Bromodomain; 1.
DR CDD; cd15492; PHD_BRPF_JADE_like; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 PANTHER; PTHR13793:SF164; BROMODOMAIN-CONTAINING PROTEIN, 140KD, ISOFORM A; 1.
DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 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
//
