LSY12_CAEEL
ID LSY12_CAEEL Reviewed; 1585 AA.
AC K8ERR8; D7SFM3; G5EBH5; G5EGP0; G5EGU3; K8ES81; K8ESF3; K8F7U3; L8E6K3;
AC Q21789;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Histone acetyltransferase lsy-12 {ECO:0000303|PubMed:20923973};
DE EC=2.3.1.48 {ECO:0000255|PROSITE-ProRule:PRU01063};
GN Name=lsy-12 {ECO:0000312|WormBase:R07B5.9h};
GN Synonyms=mys-3 {ECO:0000312|WormBase:R07B5.9h};
GN ORFNames=R07B5.9 {ECO:0000312|WormBase:R07B5.9h};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF 1539-GLN--ARG-1585.
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: Probable histone acetyltransferase (Probable). Required to
CC initiate and then maintain lateralized gene expression in the ASE
CC sensory neurons (PubMed:20923973). Involved in determining cell fate in
CC the ASE neurons (PubMed:20923973). {ECO:0000269|PubMed:20923973,
CC ECO:0000305|PubMed:20923973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01063};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=h {ECO:0000312|WormBase:R07B5.9h};
CC IsoId=K8ERR8-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:R07B5.9a};
CC IsoId=K8ERR8-2; Sequence=VSP_061552, VSP_061560;
CC Name=b {ECO:0000312|WormBase:R07B5.9b};
CC IsoId=K8ERR8-3; Sequence=VSP_061553, VSP_061558, VSP_061559;
CC Name=c {ECO:0000312|WormBase:R07B5.9c};
CC IsoId=K8ERR8-4; Sequence=VSP_061555, VSP_061560;
CC Name=d {ECO:0000312|WormBase:R07B5.9d};
CC IsoId=K8ERR8-5; Sequence=VSP_061554, VSP_061555, VSP_061560;
CC Name=f {ECO:0000312|WormBase:R07B5.9f};
CC IsoId=K8ERR8-6; Sequence=VSP_061560;
CC Name=g {ECO:0000312|WormBase:R07B5.9g};
CC IsoId=K8ERR8-7; Sequence=VSP_061555;
CC Name=i {ECO:0000312|WormBase:R07B5.9i};
CC IsoId=K8ERR8-8; Sequence=VSP_061554, VSP_061555;
CC Name=j {ECO:0000312|WormBase:R07B5.9j};
CC IsoId=K8ERR8-9; Sequence=VSP_061553;
CC Name=k {ECO:0000312|WormBase:R07B5.9k};
CC IsoId=K8ERR8-10; Sequence=VSP_061553, VSP_061556, VSP_061557;
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
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DR EMBL; BX284605; CAA96668.3; -; Genomic_DNA.
DR EMBL; BX284605; CBM41216.2; -; Genomic_DNA.
DR EMBL; BX284605; CBM41217.2; -; Genomic_DNA.
DR EMBL; BX284605; CBM41218.2; -; Genomic_DNA.
DR EMBL; BX284605; CCA65604.1; -; Genomic_DNA.
DR EMBL; BX284605; CCO25615.1; -; Genomic_DNA.
DR EMBL; BX284605; CCO25616.1; -; Genomic_DNA.
DR EMBL; BX284605; CCO25617.1; -; Genomic_DNA.
DR EMBL; BX284605; CCO25618.1; -; Genomic_DNA.
DR EMBL; BX284605; CCQ25674.1; -; Genomic_DNA.
DR PIR; T24008; T24008.
DR RefSeq; NP_001256145.1; NM_001269216.1.
DR RefSeq; NP_001256146.1; NM_001269217.1.
DR RefSeq; NP_001256147.1; NM_001269218.1.
DR RefSeq; NP_001256148.1; NM_001269219.1.
DR RefSeq; NP_001256149.1; NM_001269220.1.
DR RefSeq; NP_001263847.1; NM_001276918.1.
DR RefSeq; NP_001263848.1; NM_001276919.1.
DR RefSeq; NP_001263849.1; NM_001276920.1.
DR RefSeq; NP_001263850.1; NM_001276921.1.
DR RefSeq; NP_001263851.1; NM_001276922.1.
DR SMR; K8ERR8; -.
DR STRING; 6239.R07B5.9h; -.
DR EPD; D7SFM3; -.
DR PaxDb; G5EBH5; -.
DR PeptideAtlas; D7SFM3; -.
DR EnsemblMetazoa; R07B5.9h.1; R07B5.9h.1; WBGene00045419.
DR GeneID; 3565873; -.
DR KEGG; cel:CELE_R07B5.9; -.
DR UCSC; R07B5.8b.1; c. elegans.
DR CTD; 3565873; -.
DR WormBase; R07B5.9a; CE45288; WBGene00045419; lsy-12.
DR WormBase; R07B5.9b; CE37036; WBGene00045419; lsy-12.
DR WormBase; R07B5.9c; CE45237; WBGene00045419; lsy-12.
DR WormBase; R07B5.9d; CE45219; WBGene00045419; lsy-12.
DR WormBase; R07B5.9f; CE46018; WBGene00045419; lsy-12.
DR WormBase; R07B5.9g; CE47894; WBGene00045419; lsy-12.
DR WormBase; R07B5.9h; CE47842; WBGene00045419; lsy-12.
DR WormBase; R07B5.9i; CE48008; WBGene00045419; lsy-12.
DR WormBase; R07B5.9j; CE48089; WBGene00045419; lsy-12.
DR WormBase; R07B5.9k; CE48104; WBGene00045419; lsy-12.
DR eggNOG; KOG2747; Eukaryota.
DR GeneTree; ENSGT00940000157744; -.
DR HOGENOM; CLU_003638_0_0_1; -.
DR InParanoid; K8ERR8; -.
DR OMA; PFFFYIV; -.
DR OrthoDB; 629545at2759; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00045419; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; K8ERR8; baseline and differential.
DR GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Metal-binding; Reference proteome;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1585
FT /note="Histone acetyltransferase lsy-12"
FT /id="PRO_0000456039"
FT DOMAIN 544..830
FT /note="MYST-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT ZN_FING 577..602
FT /note="C2HC MYST-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT ACT_SITE 720
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|PIRSR:PIRSR602717-51,
FT ECO:0000255|PROSITE-ProRule:PRU01063"
FT BINDING 685..689
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT BINDING 724
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT BINDING 815
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT MOD_RES 644
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT VAR_SEQ 1..359
FT /note="MGKKRKPSPERSSDEDEVSTPSPKDRTARPTAAARRENVALSQAVALSLEDA
FT SNFCSLAFSLERIKREPVDTDYDDPNQPGPSSVPVSARTDHVLPIRFKIKAEPQEYDSD
FT EYGKDHGAVQIANKEVPAISPIEEVSQKRRGRPRKTDAAQHLFFPHVSIKQEPDDGFIN
FT FHESRCVGIAQDPEMQHLHDVNESHSSEIAIFRETKKITERKKKKTEAEKLWDNMSLTE
FT KEVFQSHTRRRRTTRLPIIQNFEETEEGCIVEVPIPLIDLDNDAVESVTGPQHENVTVS
FT ENVLSTESTDQEVTETKRLHDSSRDFNPPRIQDTPSTVIRPEGDQKDPMSSTSSKRRNT
FT NNSRCASLLSNP -> MSSTSSKRRNTNNSRCASLLSNP (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_061552"
FT VAR_SEQ 1..336
FT /note="Missing (in isoform b, isoform j and isoform k)"
FT /evidence="ECO:0000305"
FT /id="VSP_061553"
FT VAR_SEQ 1..302
FT /note="MGKKRKPSPERSSDEDEVSTPSPKDRTARPTAAARRENVALSQAVALSLEDA
FT SNFCSLAFSLERIKREPVDTDYDDPNQPGPSSVPVSARTDHVLPIRFKIKAEPQEYDSD
FT EYGKDHGAVQIANKEVPAISPIEEVSQKRRGRPRKTDAAQHLFFPHVSIKQEPDDGFIN
FT FHESRCVGIAQDPEMQHLHDVNESHSSEIAIFRETKKITERKKKKTEAEKLWDNMSLTE
FT KEVFQSHTRRRRTTRLPIIQNFEETEEGCIVEVPIPLIDLDNDAVESVTGPQHENVTVS
FT ENVLSTESTDQEVT -> MFLSIETGYQHLQKLVFN (in isoform d and
FT isoform i)"
FT /evidence="ECO:0000305"
FT /id="VSP_061554"
FT VAR_SEQ 337..381
FT /note="Missing (in isoform c, isoform d, isoform g and
FT isoform i)"
FT /evidence="ECO:0000305"
FT /id="VSP_061555"
FT VAR_SEQ 828..850
FT /note="WVPRKMRPSMDGYHELSKEEIEQ -> FSVGSSKNATINGRLSRAFKRGD
FT (in isoform k)"
FT /evidence="ECO:0000305"
FT /id="VSP_061556"
FT VAR_SEQ 851..1585
FT /note="Missing (in isoform k)"
FT /evidence="ECO:0000305"
FT /id="VSP_061557"
FT VAR_SEQ 886..904
FT /note="ELRSRGHNRSVGRNLKHEV -> VRKRRFQFGMKHRKRNNTC (in
FT isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_061558"
FT VAR_SEQ 905..1585
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_061559"
FT VAR_SEQ 1405..1407
FT /note="Missing (in isoform a, isoform c, isoform d and
FT isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_061560"
FT MUTAGEN 1539..1585
FT /note="Missing: In ot154; Reduces expression of lim-6 in
FT the sensory ASEL neuron; exacerbated in a lin-49 mutant
FT background."
FT /evidence="ECO:0000269|PubMed:20923973"
SQ SEQUENCE 1585 AA; 178281 MW; FF9F2E8E39B24EDB CRC64;
MGKKRKPSPE RSSDEDEVST PSPKDRTARP TAAARRENVA LSQAVALSLE DASNFCSLAF
SLERIKREPV DTDYDDPNQP GPSSVPVSAR TDHVLPIRFK IKAEPQEYDS DEYGKDHGAV
QIANKEVPAI SPIEEVSQKR RGRPRKTDAA QHLFFPHVSI KQEPDDGFIN FHESRCVGIA
QDPEMQHLHD VNESHSSEIA IFRETKKITE RKKKKTEAEK LWDNMSLTEK EVFQSHTRRR
RTTRLPIIQN FEETEEGCIV EVPIPLIDLD NDAVESVTGP QHENVTVSEN VLSTESTDQE
VTETKRLHDS SRDFNPPRIQ DTPSTVIRPE GDQKDPMSST SSKRRNTNNS RCASLLSNPH
STPVTRLMRG ILDSENSDND EMLSNDQSEI AKRPRTPRPR YSPEAQRRTN SRLSALTIDT
NRSNDLNVDG SAPSSSSAAS CGLSTPDPDR TSQQRRKGNQ SAARSRKIKT PSPPLSQEDE
PMELDSDDDP VNELDNLPIV IDDPSYVLTK EHKEIFEQVK KSVSDRNEFS PAQISEIYRS
SKGEQARLPE RIHFGAFIMK TWYGSPFPAE FINVKKLFIC EFCFFYARSD EIMQNHAKKC
MLRAPPGLEI YRKGDISVFE VDGRLQKEYC QTLCLVSRMF LESKTVFYDT EPFFFYIVTI
NDDIGCHFAG YFSKEKYEPD VNNLSCIMTL PCYQEMGLGR FLIDISYALS RKEKWFGGPE
QPLSELGRKA YGGYWRTTIA SCLGRLKDEL EFGSGISIKM IADDTGVNCH DILEVVCSLG
WAKPVDPDEK NHYKLEWDVD WDMVSIILRE SEASKETKVQ YDPECLDWVP RKMRPSMDGY
HELSKEEIEQ DEQRRKSIQK TPVHVSMEKA TPTSTTSLPV GSVKKELRSR GHNRSVGRNL
KHEVNRKVKV PEWAAARDLT DEEITVEENK KQQKQNRKIF TRCADSVLDK SNIREETPED
DEPGPSTKPS GKRQRGNKCN NTESEPNPSG RKTSATSSGR GKYRNRRTDG TEEEEEDDDP
TDSEPLTTDD EKPFETSVNK EKNEKSRRGK KVSKKRRSVA GKKFPPNFGV RDRDEPKKAE
NSEDGEGLES KPGPSTEMIL VEKVEEEEAK VTVSDINMQA SESKIEGIEQ TSEVDIPKSD
EDHQSTEAYD RVEDEVPITD YNIPTPDSYH SSPPHSPTPS PQPQLMQAQQ NIYQDNDCHF
AENDSKPPHL VSEVDDPAAP QPTVTLQSGP SDAPPLSHNS VDGYSTGDDD APPNLSPQIG
KSENNEEEMP LIAPIVQHNG ITHHEESTAQ HYHDSMNAGP STSSHVTPQM SMINTTPQQP
PFSHPNSQQQ ATPGSGGVPS CGPAYTHHTP EQQSQQFMSP PMAGMPASVA SNHSIHNSNS
IEMVGGPASL QHTPQQYEMG HSMAQMSQES AIGGINTVPS IEQQNQLMLQ HHQFSSPPAA
PPPSQQQQVV QPPIPPAPTT ANGRRRSESA ATQRTKARQQ HQHQQQQPQQ PQQRIAAPGV
PQGVHPQMQF PMNAMNMMPA YPPFYPYTNY PNIWQPPYQN YPYNQVDYQQ PWLYNNGHIP
HQTNGTATNQ FHPGHMGYFP NNNGR
