ID W5MPG2_LEPOC Unreviewed; 871 AA.
AC W5MPG2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Interleukin enhancer binding factor 3 {ECO:0000313|Ensembl:ENSLOCP00000010271.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000010271.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000010271.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AHAT01007581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01007582; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01007583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MPG2; -.
DR Ensembl; ENSLOCT00000010284.1; ENSLOCP00000010271.1; ENSLOCG00000008430.1.
DR GeneTree; ENSGT00940000156719; -.
DR HOGENOM; CLU_015490_0_0_1; -.
DR Proteomes; UP000018468; Linkage group LG6.
DR Bgee; ENSLOCG00000008430; Expressed in camera-type eye and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR CDD; cd19910; DSRM_ILF3_rpt1; 1.
DR CDD; cd19912; DSRM_ILF3_rpt2; 1.
DR Gene3D; 1.10.1410.40; -; 1.
DR Gene3D; 3.30.160.20; -; 2.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR033099; DSRM1_ILF3.
DR InterPro; IPR006561; DZF_dom.
DR InterPro; IPR049402; DZF_dom_C.
DR InterPro; IPR049401; DZF_dom_N.
DR InterPro; IPR043519; NT_sf.
DR PANTHER; PTHR45762:SF4; INTERLEUKIN ENHANCER-BINDING FACTOR 3; 1.
DR PANTHER; PTHR45762; ZINC FINGER RNA-BINDING PROTEIN; 1.
DR Pfam; PF00035; dsrm; 2.
DR Pfam; PF20965; DZF_C; 1.
DR Pfam; PF07528; DZF_N; 1.
DR SMART; SM00358; DSRM; 2.
DR SMART; SM00572; DZF; 1.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 2.
DR PROSITE; PS50137; DS_RBD; 2.
DR PROSITE; PS51703; DZF; 1.
PE 4: Predicted;
KW Antiviral defense {ECO:0000256|ARBA:ARBA00023118};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00266}; Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 11..383
FT /note="DZF"
FT /evidence="ECO:0000259|PROSITE:PS51703"
FT DOMAIN 407..476
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 539..605
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 69..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 871 AA; 92695 MW; DE58B855E663C5F9 CRC64;
MPPPFRQRPM RIFVNDDRHV MAKHSAVYPT QEELEGVQNM VSHTERALKA VSDWLDEQEK
VVVVVKQEPD APAEGAAEEE KESEQKPTEQ ATRTLRGVMR VGLVAKGLLL KGDLDLELVL
LCKDKPTITL LKKVAENLAV QFASITEEKY EIIQSIREAA IVIKSTKEPV LTLTIHLTSP
VVREEAEKQA AGETLSVNDP PDVLDRQKCL TALASLRHAK WFQARANGLK SCVIVIRILR
DLCSRVPTWA PLRGWPLELL CEKAIGTGNR PMGAGEALRR VLECLASGIL MPDGPGISDP
CEKETTDAIS HLDRQQREDI TQSAQHALRL AAFGQLHKVL GMDPLPSKMP RKPKTDAPID
YTVQIPPSTT YAPPAKRPIE EEEGGDDKNP NKKKKKLQKK SPDEKAEPPQ AMNALMRLNQ
LKPGLQYKLI SQTGPVHVPV FTMAVEVDGK TFEASGPSKR TAKLHVAVKV LQDMGLPTGV
EVKTTADSTK GEEVPNDVEM KPPAAPAVAT DSSTPAAPNS ETADSTENSR QQGPILTKHG
KNPVMELNEK RRGLKYELIS ETGGSHDKRF VMEVEIDGLK FQGTGSNKKV AKAYAALAAL
ERLFPEGSTT ESAKKKKPPP MHSPVFGMMG GAPADPAVNP RGRGRGGRGR GRGRGFNNAG
GYNQGGYGTY GYGSNANSGY NNYYNNNGGG SGAGGPGAGG AGMGSGTNAG AGGGGGGGGG
GGGGNYGSYY QNDGIFPSQP QNPKPPGKKP PHHPGGGGGG GPAGGYQPPP QGQVSYNQYN
QGYNQGGPGK KSYSHNQSGG GGAGYSNYST AYPSQVTGGG GSQDYSYEGY NSQSNYSTQG
GGGQSYGGNQ TSYQNQGGYG RGDHTMSYQY R
//
