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Database: UniProt
Entry: W5NPA5_LEPOC
LinkDB: W5NPA5_LEPOC
Original site: W5NPA5_LEPOC 
ID   W5NPA5_LEPOC            Unreviewed;       893 AA.
AC   W5NPA5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=RNA binding motif protein 12 {ECO:0000313|Ensembl:ENSLOCP00000022464.1};
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:ENSLOCP00000022464.1, 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:ENSLOCP00000022464.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AHAT01024303; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006639710.1; XM_006639647.2.
DR   RefSeq; XP_015220542.1; XM_015365056.1.
DR   AlphaFoldDB; W5NPA5; -.
DR   STRING; 7918.ENSLOCP00000022464; -.
DR   Ensembl; ENSLOCT00000022505.1; ENSLOCP00000022464.1; ENSLOCG00000018363.1.
DR   GeneID; 102692368; -.
DR   KEGG; loc:102692368; -.
DR   CTD; 10137; -.
DR   eggNOG; KOG4307; Eukaryota.
DR   GeneTree; ENSGT00940000160611; -.
DR   HOGENOM; CLU_004368_1_0_1; -.
DR   InParanoid; W5NPA5; -.
DR   OMA; QEFCVYL; -.
DR   OrthoDB; 5402241at2759; -.
DR   Proteomes; UP000018468; Linkage group LG18.
DR   Bgee; ENSLOCG00000018363; Expressed in embryo and 13 other cell types or tissues.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR   CDD; cd12512; RRM3_RBM12; 1.
DR   CDD; cd12749; RRM4_RBM12; 1.
DR   CDD; cd12751; RRM5_RBM12; 1.
DR   Gene3D; 3.30.70.330; -; 5.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR034855; RBM12_RRM3.
DR   InterPro; IPR034856; RBM12_RRM4.
DR   InterPro; IPR034854; RBM12_RRM5.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR13976:SF88; FI22004P1; 1.
DR   PANTHER; PTHR13976; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN-RELATED; 1.
DR   Pfam; PF00076; RRM_1; 4.
DR   SMART; SM00360; RRM; 4.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 4.
DR   PROSITE; PS50102; RRM; 4.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT   DOMAIN          308..383
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          440..517
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          555..632
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          817..893
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   REGION          94..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          389..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          531..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          718..816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..137
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..404
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..434
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        536..552
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        718..747
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   893 AA;  94633 MW;  8A0C2493F7019DCC CRC64;
     MAVVIRLQGL PIVAGTMDIR HFFSGLTIPD GGVHIVGGEH GEAFIVFATD EDARLGMMRT
     GGTIKGSKVS LLLSSKTEMQ NMIELSRRRF ETGNLEAPAG NGSRPGPPAS SGGSGRGSLP
     TTMQGFSSPT PSVVTTAAAS AHEPVGSKSI PTFSTASMST IPPSYSNNFS SPSLTMGSTM
     TTAISTLNSV PPPMPPLPTL PSLPPMPSIP PMPVPPPVST LPPVPPSTPI PPVPPVPPIT
     HMPPMSTMPP FNPGVPPPVG PVPSGLSGSG PPMSMGNPNH MFLGPMNPLG PLNPQAHLKP
     PVVNPDELYV HLQGLPFSAT EMDVRDFFHG LGVDSVRLLR DHLGRSSGRA LAKFFMPQDA
     FEALKRNAAM MGQRYVEISP ATERQWLASG GASSYSGGQG QSKHGSDHSD QDHHRRLRSS
     SESPSGRDRA RSRSPHKQEF CVYLKGLPYE AENKQIFEFF KNLDIVEDSI YIAYGPNGRA
     TGEGFVEFRN EMDYKAALGC HMQYMGSRFI QVHPITKKGM FEKIDVIRKR MQGTQQGDHK
     TGSFEGGGDK SSSRSCAHIS NIPYNVSKKD VQLFLEGIQL FEDSLKVLVD GNGQGLGQAV
     VQFRSEEEAL KAERLHRQKL NGRDAFVHLV TFEQMKEIER NPPPQVKRGQ KVQLPQAHSY
     PSVSGDEYAF LRGSSGSITN GPPFGTLYSA PGNGLGGPPP LPPVGVGGGL GDVPISVPPP
     VVPGHLPSPM LEPPGFRPGP SSTSGPPVFP GGPESMRGLP PFDNGPRKSS GPPSRGGAGG
     GGQGRAGGSQ SGYGPPSSEA LRGPPSLSGG PGSQRPTIVK IQNMPFTVTV DEILDFFYGY
     QVLPGSVCLQ FSDKGMPTGE AMVAFESQDE AMSAVLDLND RPIGSRKVKI TLG
//
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