ID A0A3P9AEM5_ESOLU Unreviewed; 635 AA.
AC A0A3P9AEM5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=RNA-binding protein EWS-like {ECO:0000313|Ensembl:ENSELUP00000039513.1};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000039513.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000039513.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000039513.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RRM TET family.
CC {ECO:0000256|ARBA:ARBA00008448}.
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DR RefSeq; XP_010875810.1; XM_010877508.3.
DR AlphaFoldDB; A0A3P9AEM5; -.
DR Ensembl; ENSELUT00000030909.2; ENSELUP00000039513.1; ENSELUG00000025423.1.
DR GeneID; 105014859; -.
DR KEGG; els:105014859; -.
DR GeneTree; ENSGT00940000154191; -.
DR InParanoid; A0A3P9AEM5; -.
DR OMA; MDDMGGR; -.
DR OrthoDB; 162112at2759; -.
DR Proteomes; UP000265140; LG14.
DR Bgee; ENSELUG00000025423; Expressed in ovary and 14 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0021954; P:central nervous system neuron development; IEA:Ensembl.
DR GO; GO:0051256; P:mitotic spindle midzone assembly; IEA:Ensembl.
DR GO; GO:1903041; P:regulation of chondrocyte hypertrophy; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IEA:Ensembl.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034870; TET_fam.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR23238; RNA BINDING PROTEIN; 1.
DR PANTHER; PTHR23238:SF3; RNA-BINDING PROTEIN EWS; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00322}.
FT DOMAIN 342..428
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 494..525
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT REGION 34..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 635 AA; 64712 MW; 48B7996848696081 CRC64;
MASAADYSAY GQAGGQQGYG SYVAQPAQAA YGQNTQPAYG QQQGYGSYSQ PADSTYAQGS
SSSSGYSQQS YGSSYSQQPP AATGYGATTA AAPAAPQGYS QPAQGYGAGG YDAAPAAAAA
STTTTTSQGS YGTQSGYAAQ ASYPGYGQQP AAGAPPSYST SSQPPPSYEQ NSYSQTPQQG
AYSQPPQSGG YQSQPGGYSQ QGSGYQAPLP QTQAPPSSYA PPSGGSYGQP PSSQYGQQGG
PGGSYGSQGS YRQDHSNGGG YSGPEPGGYG GHGEGRGMGG ESRGRGRGGF DRGGMMRGGG
GMRGGMGRGG MGIAGDRGGF IKPGGPASDM GRPEEQDDSE NSTIYITGLT ENATLPEVAD
FFKHSGIIRI NKRTGLPAIN IYTDKDSGKP KGDCTLSYDE PPCAKAAVEW FDGKDFQGKK
LKVSMARRKP MMGMMRGGMP MRGDRGGMMN RGGPGMMGRG GPMGRGGDRG GFMPRGGPRG
MGRGGPSGGN MQQRAGDWEC PNAGCGNQNF AWRMECNQCK APKPEGFGPP PFPPPGGDRG
RGGPGMRGRG GMDRGGPGGP GGPLGFRGGR GGDRGGGFRG RGGMERGGFG GRGRGGPGGP
PMDDMGGRGR RGMGPPGKMM EMKGDHRQDR RDRPY
//