ID W5N3F3_LEPOC Unreviewed; 1149 AA.
AC W5N3F3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=RNA binding motif protein 20 {ECO:0000313|Ensembl:ENSLOCP00000015162.1};
GN Name=RBM20 {ECO:0000313|Ensembl:ENSLOCP00000015162.1};
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:ENSLOCP00000015162.1, 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:ENSLOCP00000015162.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01017274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01017275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5N3F3; -.
DR Ensembl; ENSLOCT00000015191.1; ENSLOCP00000015162.1; ENSLOCG00000012315.1.
DR GeneTree; ENSGT01030000234642; -.
DR HOGENOM; CLU_007364_0_0_1; -.
DR Proteomes; UP000018468; Linkage group LG5.
DR Bgee; ENSLOCG00000012315; Expressed in larva and 4 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd12685; RRM_RBM20; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034790; RBM20_RRM.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR15592; MATRIN 3/NUCLEAR PROTEIN 220-RELATED; 1.
DR PANTHER; PTHR15592:SF11; RNA-BINDING PROTEIN 20; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00451; ZnF_U1; 2.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50171; ZF_MATRIN; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 451..526
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 1082..1113
FT /note="Matrin-type"
FT /evidence="ECO:0000259|PROSITE:PS50171"
FT REGION 210..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..857
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..881
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1149 AA; 127499 MW; 87DD461739FAD1E2 CRC64;
SQLSGGGQNP LLLTPASLQL AQLQAQLTLH RLKLAQTAVS SNTAAAATVL NQVLSKVAMS
QPFFNQLTSP MVSTPQSHAG GAHLGSGMLA SRFPSSGLPF PPQNTALGPL VGGDLGCGGA
LQNQNHTAIG LNPYTGGVSQ TPNQLTSEYG NKINLSAHTV YPSDTDRRSQ YSILSGGPNI
SDKGGNGFLP LSSAQSKMGN QSGFQRDFYG SSPQGPEGQQ GKQFCFAGEP NPSAFPPVNH
KEQWQQQGAM SKMEGAPTQG VTWATSSQPF HVRGELYNPE EPTTDSKYCS GAGPPFSGST
QGFVGYQQVQ PREQTLRGGP VPLQPHQLND FHAVTPVHMP HHCTICDKKV FNLKDWDQHV
KGELHLQNRA LFSECPAIGP AHFPKVPDVC LNSSTNTTMT FSSASNQAYT AYNSESLAAQ
EAKVFLKSNA RTFPCCGSKT EFPLRKSGPG RVVHICNIPE GSCTENDVIN LGLPFGKVTN
YILMRSTHQA FLEMAYVEAA QAMVQYYQEN PATINDEKLL IRMSKRYKEL QLKKPGKDVE
SIIQDIHSQR ERDGMQDVEC YPLERPRSRS PISRSLSPRS HSPSFTSCSS THSPLGTSRA
EWSNGLSERR ASWDWSPHVR REEEREEGFW RNEDEDRSDS WLQERRKPYL KLTDRASPRS
LEERGEPTRT TRERYPRSSP QNTSYSSYRC KEDDFYKREP RHKSDRPPRP PHQRHEAKLK
KRDPEEGYRP KYSHSEATED AIAAKSTEDR RQTSTDKGQS KRLHKKMATE KEEQVSDTQG
QQKYKDQSVS PNPKSEEMKG SDHERSKETQ PEESESGNET EGESWYPQAM EELVTVDEVG
EAEDCIIEPD LLELQEAEEA QAEEKAEKVS TTIDTRDTGE PAEEGGQSGS DTGHTAQDSR
VEVRPEEHTE HRSPCREISN TSPQDPTLTS DPECQISMEL HSELGDFPSR EFQAAFKEAC
SCTDSERREA DLPAAEERSL SPEDLDEGNN PLDVLSSCKK GERVTPIAKA ATEETGSEDE
QYVEAQKKDV AIKTQSQSPR HPEVEPKNVP SPPQWDQENI FGEHSIPLAC TGVEFVVPRS
GFYCKLCGLF YTSEETAKIT HCRSTVHYRN LQKYLSQLAE DSLRSSQKNT ASTEEAGIVP
QCKELNKPC
//
