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Database: UniProt
Entry: A0A3P8XLF5_ESOLU
LinkDB: A0A3P8XLF5_ESOLU
Original site: A0A3P8XLF5_ESOLU 
ID   A0A3P8XLF5_ESOLU        Unreviewed;       401 AA.
AC   A0A3P8XLF5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 2.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Splicing factor 45 {ECO:0000256|PIRNR:PIRNR031066};
DE   AltName: Full=RNA-binding motif protein 17 {ECO:0000256|PIRNR:PIRNR031066};
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:ENSELUP00000005387.2, ECO:0000313|Proteomes:UP000265140};
RN   [1] {ECO:0000313|Ensembl:ENSELUP00000005387.2, 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:ENSELUP00000005387.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Splice factor that binds to the single-stranded 3'AG at the
CC       exon/intron border and promotes its utilization in the second catalytic
CC       step. Involved in the regulation of alternative splicing and the
CC       utilization of cryptic splice sites. {ECO:0000256|PIRNR:PIRNR031066}.
CC   -!- SUBUNIT: Associates with the spliceosome.
CC       {ECO:0000256|PIRNR:PIRNR031066}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR031066}.
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DR   AlphaFoldDB; A0A3P8XLF5; -.
DR   Ensembl; ENSELUT00000010758.2; ENSELUP00000005387.2; ENSELUG00000006440.2.
DR   GeneTree; ENSGT00790000123099; -.
DR   Proteomes; UP000265140; LG23.
DR   Bgee; ENSELUG00000006440; Expressed in testis and 14 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR000467; G_patch_dom.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR040052; RBM17.
DR   InterPro; IPR003954; RRM_dom_euk.
DR   PANTHER; PTHR13288:SF8; SPLICING FACTOR 45; 1.
DR   PANTHER; PTHR13288; SPLICING FACTOR 45 SPF45; 1.
DR   Pfam; PF01585; G-patch; 1.
DR   PIRSF; PIRSF031066; Splicing_factor_SPF45; 2.
DR   SMART; SM00443; G_patch; 1.
DR   SMART; SM00361; RRM_1; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   mRNA processing {ECO:0000256|PIRNR:PIRNR031066};
KW   mRNA splicing {ECO:0000256|PIRNR:PIRNR031066};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR031066};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW   RNA-binding {ECO:0000256|PIRNR:PIRNR031066};
KW   Spliceosome {ECO:0000256|PIRNR:PIRNR031066};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        139..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        172..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          246..286
FT                   /note="G-patch"
FT                   /evidence="ECO:0000259|PROSITE:PS50174"
FT   REGION          202..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..303
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   401 AA;  45201 MW;  6456AA3CD6604B78 CRC64;
     MSLYDDMGVG SATSDTKTEG WSKNFKLLQS QLKVKKAALT QAKSQRMKQG TVLAPVIDLK
     RGGSSDDRQI IDTPPHIAAG LKDTIPSGFS SGEVLIPLAD EYDPMFPNDY ERVVKRHREE
     RQRQREQERL KEMDDREKYG LLMLLEHSGF CCFVHTLHFS NPSENCKESG HGLWFIGVFT
     LVTWAVTWIT SLVNSMSEMR SSYPYEDEGR PPRGSKAAIP PPMYEDSERP RSPPGGPTNS
     FLANMGGTVA HKIMQKYGFR EGQGLGKHEQ GLSTALSVEK TSKRGGKIII GDSTEKTDPS
     KKSEPNPLTE ILKCPTKVVL LRVSAGERWM KIWRERPRKS VKYRVCVTDD EAVRIFLEFE
     RVESAIKAVV DLNGRFFGGR VVKACFYNLD KFRVLDLGEQ M
//
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