SET9_CAEEL
ID SET9_CAEEL Reviewed; 1623 AA.
AC O44498;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2013, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Histone-lysine N-methyltransferase set-9 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9U263};
GN Name=set-9 {ECO:0000312|WormBase:F15E6.1};
GN ORFNames=F15E6.1 {ECO:0000312|WormBase:F15E6.1};
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22212395; DOI=10.1111/j.1474-9726.2011.00785.x;
RA Ni Z., Ebata A., Alipanahiramandi E., Lee S.S.;
RT "Two SET domain containing genes link epigenetic changes and aging in
RT Caenorhabditis elegans.";
RL Aging Cell 11:315-325(2012).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DOMAIN.
RX PubMed=29714684; DOI=10.7554/elife.34970;
RA Wang W., Chaturbedi A., Wang M., An S., Santhi S., Lee S.S.;
RT "SET-9 and SET-26 are H3K4me3 readers and play critical roles in germline
RT development and longevity.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Histone methyltransferase (By similarity). Might play a role
CC in transcriptional regulation (PubMed:29714684). Together with set-26,
CC negatively regulates lifespan in a germline-independent, partially daf-
CC 16-dependent fashion (PubMed:22212395, PubMed:29714684). Together with
CC set-26, plays a role in germline development and maintenance and might
CC play a role in the restriction of the trimethylation mark on histone H3
CC 'Lys-4'(H3K4me3) to target genes specifically in the germline
CC (PubMed:29714684). {ECO:0000250|UniProtKB:Q9U263,
CC ECO:0000269|PubMed:22212395, ECO:0000269|PubMed:29714684}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC Evidence={ECO:0000250|UniProtKB:Q9U263};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22212395,
CC ECO:0000269|PubMed:29714684}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the germline (at protein
CC level). {ECO:0000269|PubMed:22212395, ECO:0000269|PubMed:29714684}.
CC -!- DOMAIN: The PHD-type domain binds histone H3 when trimethylated at
CC 'Lys-4' (H3K4me3) in combination with a nearby acetylation (K9ac, K14ac
CC and/or K18ac), but not H3K4me3 alone. {ECO:0000269|PubMed:29714684}.
CC -!- DISRUPTION PHENOTYPE: Simultaneous RNAi-mediated knockdown of set-9 and
CC set-26 results in extended lifespan. {ECO:0000269|PubMed:22212395}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000305}.
CC -!- CAUTION: Contrary to other SET-domain containing methyltransferases,
CC set-9 does not have the residues usually involved in cofactor binding:
CC instead of the highly conserved XGXG, Y and NH motifs, set-9 displays
CC AVEA (Ala-940-Ala-943), V (Val-959) and F (Phe-1055) and RR (Arg-1016-
CC Arg-1017) motifs. {ECO:0000303|PubMed:29714684}.
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DR EMBL; BX284604; CCD69511.2; -; Genomic_DNA.
DR PIR; T32633; T32633.
DR RefSeq; NP_500539.2; NM_068138.4.
DR AlphaFoldDB; O44498; -.
DR STRING; 6239.F15E6.1; -.
DR EPD; O44498; -.
DR PaxDb; O44498; -.
DR PeptideAtlas; O44498; -.
DR EnsemblMetazoa; F15E6.1.1; F15E6.1.1; WBGene00017482.
DR GeneID; 177196; -.
DR UCSC; F15E6.1; c. elegans.
DR CTD; 177196; -.
DR WormBase; F15E6.1; CE48653; WBGene00017482; set-9.
DR eggNOG; KOG1844; Eukaryota.
DR GeneTree; ENSGT00940000168747; -.
DR HOGENOM; CLU_243457_0_0_1; -.
DR InParanoid; O44498; -.
DR OrthoDB; 86638at2759; -.
DR PRO; PR:O44498; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00017482; Expressed in adult organism and 2 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
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; PF00628; PHD; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Metal-binding; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1623
FT /note="Histone-lysine N-methyltransferase set-9"
FT /id="PRO_0000438926"
FT DOMAIN 965..1056
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 786..834
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1356..1623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1093..1201
FT /evidence="ECO:0000255"
FT COILED 1364..1401
FT /evidence="ECO:0000255"
FT COMPBIAS 207..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..599
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1367..1433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1529..1548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1623 AA; 179056 MW; 1FAD2382F1F05459 CRC64;
MADGEHTLPA DEELFEQPPP QQQQPEIAEP IVMAQEPIQG VSEDPQASEA THEAPDNYPV
DHQMENQEFY HEPQIPEPQQ IPQIPVFQPA AYNPPNYVAP QQRANNFGEP AAADARPLTE
QEQLAAERPT EDTVWIDSDD DTDVEEAILR ANFWLPYSDH NYDPPDPADR IILPTEGPFP
CIAGLDEDCN IVKQWMPEDA VGPGSPGTQY RRNQQAGGGL PSTSVASQQQ QLPVRHNIQN
RPMVAAQPFS IGGNQVEYGG MDSRMQQRGV VRDGPQYRVM NDFGNGLPMR GLLPPRNSPA
ANAINRAREQ QQQMYHQAGA RGSLQQRAAP APADPTPGSY QHIVNAVPGG GANPMRRVPP
QARPGMIGGA ANNNRARPTH VTRPMDTQEF EHPVAPAAAP PHRVVDVAPH RMTPEQRQEL
QQMNRQRAAP QFPAAAAQRS AEVIVIQQRP GASSRAPRPS MAQEDLLRSP TRRLSERVPQ
EHQTPVLEPR RFQVKVTDTY STPIPKASDQ LPAQLTEEDP PEESAAAAAP EDVPDAAPED
PPKVILKPTP PHRMTQEEKN AHFARLTTDK EKPTSSTSIL PQDAAPPHVP PPPPPLVLRP
HHQDETLAMV QSVFESKPRQ PDTPKDKETI SKIADLLRFS ADEFTGQSGS SAAARQRTVS
GSAARAQTYQ MHHQQQQHHH QMPMDQRKRP SSGRYDALMG AMPLQQQPPP PPSQFQHTDS
IAHRPRGRPK GTRHPSVAVQ PQRSGGARTL PPRAQTVAMS ARNGANAKNS DSESEGIDEA
AEESWTMRCH CGMDHGDGDT IECEGCKTWQ HMACMGLTLK SNTSKYKCEM CLPRRLPVSK
AEAAREQERI LNRLRAAARK QKRKSEPVEQ KQKSSQPSTS RKSAPMALQQ PAEPRVAQLN
DYSKQASALL FGMEQTAGAD TLLAESRLHK KARRMFVEEA VEALVTTDLV QIRQVILEVN
GHVSMSSEVK RQPGGGNCIF MYDGLMKGTA GEDMGDGQEL VCIDTKRKGN DTKFTRRSCV
PNCVLKHVLG SNATLGIMIV ATKDITRNTE VTLPFDADWR ESEVELECAE HMKELQACPF
ESERRRFAAE RHRAMDHKKQ EAEEARRADE ERRRLEEEVR RERAAKTKQM DEAEKARLEA
EKAAEKEKKA KERKKMEASA AAAPESTNSI TAREERRIQQ AEEMFRRQEE EGKRKEARRR
SKSVTPGVLE AAGTAAREDA PEASIPVPAP SPPASRRSVS RTTQPSTSSF ATPTEPPAKN
KRMRSVVPPK SEPASSAKRV RATTVATPKA TTANDSRKRT ASATGKTPVA KRSKNVAPTS
FALALIEKEL REQARNSTVL EMILPDYIMN EERSGLLAGQ SPDFSEVRAQ IEEENRMKER
SRKREAKKKA VEKEKKEHRK EPKKTNEPGP APKSEKAVEK AVEKVEKKPK SPQKPPAKPT
AQNPPLKKTE EVDGIEREAS ESSSKESSVA PEEKKNPKKI TFAEYNSRRS QKREAGECST
PPAVTRRGFI PSTEGEDLVN VELSAIPLDD HPSSSNTAPT TTIAPSVGGA PKPTSVVVKS
PSTRSRTRGA ASESADDAPA EHSMSLQDRV FSMFGSTVDA PAPPPPPASA ETNSRRSRST
RWN
