U2AF4_RAT
ID U2AF4_RAT Reviewed; 220 AA.
AC Q7TP17; Q7TP18;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Splicing factor U2AF 26 kDa subunit;
DE AltName: Full=Liver regeneration-related protein LRRG157/LRRG158;
DE AltName: Full=U2 auxiliary factor 26;
DE AltName: Full=U2 small nuclear RNA auxiliary factor 1-like protein 4;
DE Short=U2AF1-like 4 {ECO:0000250|UniProtKB:Q8BGJ9};
GN Name=U2af1l4; ORFNames=Cb2-806, Cb2-807;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Liver;
RA Xu C.S., Li W.Q., Li Y.C., Ma H., Wang L., Wang S.F., Han H.P., Wang G.P.,
RA Chai L.Q., Yuan J.Y., Yang K.J., Yan H.M., Chang C.F., Zhao L.F., Shi J.B.,
RA Rahman S., Wang Q.N., Zhang J.B.;
RT "Liver regeneration after PH.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA-binding protein that function as a pre-mRNA splicing
CC factor. Plays a critical role in both constitutive and enhancer-
CC dependent splicing by mediating protein-protein interactions and
CC protein-RNA interactions required for accurate 3'-splice site
CC selection. Acts by enhancing the binding of U2AF2 to weak pyrimidine
CC tracts. Also participates in the regulation of alternative pre-mRNA
CC splicing. Activates exon 5 skipping of PTPRC during T-cell activation;
CC an event reversed by GFI1. Binds to RNA at the AG dinucleotide at the
CC 3'-splice site. Shows a preference for AGC or AGA.
CC {ECO:0000250|UniProtKB:Q8BGJ9}.
CC -!- SUBUNIT: Interacts with GFI1, U2AF2 and C1QBP.
CC {ECO:0000250|UniProtKB:Q8BGJ9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8BGJ9}. Nucleus
CC speckle {ECO:0000250|UniProtKB:Q8BGJ9}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8BGJ9}. Note=Interaction with C1QBP is required
CC for the nuclear translocation. Displays active nucleo-cytoplasmic
CC shuttling. {ECO:0000250|UniProtKB:Q8BGJ9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TP17-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TP17-2; Sequence=VSP_029266;
CC -!- DOMAIN: The second zinc finger in necessary for interaction with GFI1
CC and for alternative pre-mRNA splicing events. {ECO:0000250}.
CC -!- DOMAIN: The region 162-220 is essential for the nuclear import of the
CC protein in spite of the absence of a nuclear localization signal (NLS).
CC This region is essential for the interaction with C1QBP, interaction
CC which is required for the nuclear translocation. This region may be
CC involved in the localization in nuclear dot-like structures and it also
CC confers the ability of nucleo-cytoplasmic shuttling.
CC {ECO:0000250|UniProtKB:Q8BGJ9}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
CC -!- CAUTION: Orthologs of U2AF1L4 do not appear to exist in lower
CC eukaryotes, Drosophila, C. elegans, plants, or vertebrates such as
CC Xenopus or zebrafish. Existence of circadian and light-inducible
CC alternative splicing of U2AF1L4 similar to the mouse in human and rat
CC is not yet proven. {ECO:0000305}.
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DR EMBL; AY325237; AAP92638.1; -; mRNA.
DR EMBL; AY325238; AAP92639.1; -; mRNA.
DR RefSeq; NP_001008775.1; NM_001008775.1. [Q7TP17-1]
DR RefSeq; XP_006228838.1; XM_006228776.3. [Q7TP17-1]
DR AlphaFoldDB; Q7TP17; -.
DR SMR; Q7TP17; -.
DR STRING; 10116.ENSRNOP00000041377; -.
DR PhosphoSitePlus; Q7TP17; -.
DR jPOST; Q7TP17; -.
DR Ensembl; ENSRNOT00000038154; ENSRNOP00000030286; ENSRNOG00000024497. [Q7TP17-1]
DR Ensembl; ENSRNOT00000116214; ENSRNOP00000095413; ENSRNOG00000024497. [Q7TP17-2]
DR GeneID; 361542; -.
DR KEGG; rno:361542; -.
DR UCSC; RGD:1305600; rat. [Q7TP17-1]
DR CTD; 199746; -.
DR RGD; 1305600; U2af1l4.
DR eggNOG; KOG2202; Eukaryota.
DR GeneTree; ENSGT00950000183152; -.
DR HOGENOM; CLU_059852_1_0_1; -.
DR InParanoid; Q7TP17; -.
DR OMA; DSAGHYP; -.
DR OrthoDB; 1340384at2759; -.
DR PhylomeDB; Q7TP17; -.
DR TreeFam; TF300143; -.
DR Reactome; R-RNO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-RNO-72187; mRNA 3'-end processing.
DR Reactome; R-RNO-73856; RNA Polymerase II Transcription Termination.
DR PRO; PR:Q7TP17; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000024497; Expressed in testis and 20 other tissues.
DR Genevisible; Q7TP17; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0089701; C:U2AF complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030628; F:pre-mRNA 3'-splice site binding; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR InterPro; IPR009145; U2AF_small.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR12620; PTHR12620; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00642; zf-CCCH; 2.
DR PRINTS; PR01848; U2AUXFACTOR.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00361; RRM_1; 1.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Cytoplasm; Metal-binding;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; Repeat;
KW RNA-binding; Spliceosome; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8WU68"
FT CHAIN 2..220
FT /note="Splicing factor U2AF 26 kDa subunit"
FT /id="PRO_0000309742"
FT DOMAIN 65..147
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 12..40
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 149..176
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 186..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8WU68"
FT VAR_SEQ 1..43
FT /note="MAEYLASIFGTEKDKVNCSFYFKIGACRHGDRCSRLHNKPTFS -> MVIQV
FT VRTITQKRKPTAERQTSRKKNQGLTALFTLRLGPAGTGTGAPDFTTNRLSARVGYTLHA
FT VPLSELRSLLNFV (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_029266"
SQ SEQUENCE 220 AA; 25836 MW; 90AC4B4126060169 CRC64;
MAEYLASIFG TEKDKVNCSF YFKIGACRHG DRCSRLHNKP TFSQTIVLLN LYRNPQNTAQ
TADGSHCHVS DVEVQEHYDN FFEEVFTELQ EKYGEIEEMN VCDNLGDHLV GNVYVKFRRE
EDAERAVAEL NNRWFNGQAV HAELSPVTDF RESCCRQYEM GECTRGGFCN FMHLRPISRN
LRRQLYGRGP RHRSPPRSHT GHRPRERNRR RSPDHRHGRF
