ID G3TDR0_LOXAF Unreviewed; 1438 AA.
AC G3TDR0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Nuclear receptor binding SET domain protein 3 {ECO:0000313|Ensembl:ENSLAFP00000012330.4};
GN Name=NSD3 {ECO:0000313|Ensembl:ENSLAFP00000012330.4};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000012330.4, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000012330.4, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000012330.4,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000012330.4}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000012330.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_003412576.1; XM_003412528.2.
DR Ensembl; ENSLAFT00000014730.4; ENSLAFP00000012330.4; ENSLAFG00000014727.4.
DR GeneID; 100663420; -.
DR KEGG; lav:100663420; -.
DR CTD; 54904; -.
DR GeneTree; ENSGT00940000155355; -.
DR HOGENOM; CLU_004494_2_1_1; -.
DR OrthoDB; 950362at2759; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042054; F:histone methyltransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15649; PHD1_NSD3; 1.
DR CDD; cd15652; PHD2_NSD3; 1.
DR CDD; cd15658; PHD4_NSD3; 1.
DR CDD; cd15661; PHD5_NSD3; 1.
DR CDD; cd20163; PWWP_NSD3_rpt1; 1.
DR CDD; cd20166; PWWP_NSD3_rpt2; 1.
DR CDD; cd19212; SET_NSD3; 1.
DR Gene3D; 2.30.30.140; -; 2.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 4.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR041306; C5HCH.
DR InterPro; IPR047456; PHD2_NSD3.
DR InterPro; IPR047458; PHD4_NSD3.
DR InterPro; IPR047527; PHD5_NSD3.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR047451; PWWP_NSD3_rpt1.
DR InterPro; IPR047453; PWWP_NSD3_rpt2.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR047461; SET_NSD3.
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; PTHR22884:SF473; HISTONE-LYSINE N-METHYLTRANSFERASE NSD3; 1.
DR PANTHER; PTHR22884; SET DOMAIN PROTEINS; 1.
DR Pfam; PF17907; AWS; 1.
DR Pfam; PF17982; C5HCH; 1.
DR Pfam; PF00855; PWWP; 2.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00249; PHD; 5.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00293; PWWP; 2.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR SUPFAM; SSF82199; SET domain; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50812; PWWP; 2.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 270..333
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 701..748
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 961..1023
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 1094..1144
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 1146..1263
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1270..1286
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT DOMAIN 1322..1369
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 121..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1035..1062
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 124..142
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1438 AA; 161892 MW; 02E44309A28D66CC CRC64;
MDFSFSFMQG IMGNTIQQPP QLIDSANIRQ EDAFDNNSDI VEDGGQTQYE ATLQQGFQYQ
PTTEDLPPLT NGYPPSISMY ETQTKYQPYN QYPNGSANGF GAVRNFTPTD YYHTEIPNTR
PHEILEKPSP PQPPPPPSVP QTVIPKKTGS PEIKLKITKT IQNGRELFES SLCGDLLNEV
QASEHTKSKH ESRKEKRKKS NKHDSSRSEE RKSHKIPKLE PEEQNRPNER VDIVSEKPRE
DPVLKEETLV QPILSPVPTT EVSTGVKFQV GDLVWSKVGT YPWWPCMVSS DPQLEVHTKI
NTRGAREYHV QFFSNQPERA WVHEKRVREY KGHEQYEELL AEATKQASNH SEKQKIRKPR
PQRERAQWDI GIAHAEKALK MTREERIEQY TFIYIDKQPE EALSQAKKNV ASKAEVKKTR
RPRSVPNTQT EQTNTGEAAS SPSSTEIRRH SQRRHTSVEE EEPPPVKIAW KTAAARKSLP
ASITMHKGSL DLQKCNMSPV VKIEQVFALQ NATGDGKFID QFVYSTKGIG NKTEISVRGQ
DRLIISTPHQ RNEKATQNIS SPEATSGPTG SVEKKQQRRS IRTRSESEKS TEVVPKKKIK
KEQVETVPQA AVKTGLQKGA SEISDSCKPL KKRSRASTDV EMTSSAYRDT SDSDSRGLSD
LQVSFGKQVD SPSATADVDI SDVQSVDSSL SRSSFGMTKK DAVCQICEST GDSLIPCEGE
CCKHFHLECL GLASLPDGKF ICMECQTGQH PCFSCKVSGT DVKRCSVGTC GKFYHETCVR
KFPTAIFESK GFRCPQHCCS ACSMEKDIYK ASKGRMMRCL RCPVAYHSGD ACIAAGSIFV
SSYVLICSNH SKRSSNSSSA VNVGFCFVCA RGLIVQDHSD PMFSSYAYKS HYLLNESNRA
ELMKLPMIPS SSASKKKCEK GGRLLCCESC PASFHPECLG IGMPEGCWNC DDCKAGRKLH
YKQIVWVKLG NYRWWPAETC NPRSVPLNIQ GLKHDLGDFP VFFFGSHDYY WVHQGRVFPY
VEGDKSFAEG QTSINKTFKK ALEEAAKRFQ ELKAQRESKE ALEIEKNSRK PPPYKHIKAN
KVVGKVQIQV ADLSEIPRCN CKPADENPCG LESECLNRML QYECHPQVCP AGDRCQNQCF
TKRLYPDAEI IKTERRGWGL RTKRSIKKGE FVNEYVGELI DEEECRLRIK RAHENSVTNF
YMLTVTKDRI IDAGPKGNYS RFMNHSCNPN CETQKWTVNG DVRVGLFALC DIPAGMELTF
NYNLDCLGNG RTECHCGADN CSGFLGVRPK SACASTTEEK ARNAKLKQKR RKIKTEPKQM
HEDYCFQCGD GGELVMCDKK DCPKAYHLIC LNLTQPPYGK WECPWHQCDE CSSSAASFCE
FCPHSFCKDH EKGALVPSAL EGRLCCSEHD PISPVSPEYW SKIKCKLESQ DRGEEVKE
//
