U2AF1_BOVIN
ID U2AF1_BOVIN Reviewed; 237 AA.
AC A1A4K8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Splicing factor U2AF 35 kDa subunit;
DE AltName: Full=U2 auxiliary factor 35 kDa subunit;
DE AltName: Full=U2 snRNP auxiliary factor small subunit;
GN Name=U2AF1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: 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. Recruits U2 snRNP to the branch point. Directly mediates
CC interactions between U2AF2 and proteins bound to the enhancers and thus
CC may function as a bridge between U2AF2 and the enhancer complex to
CC recruit it to the adjacent intron (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Identified in the spliceosome C complex. Heterodimer with
CC U2AF2. Interacts with ZRANB2. Interacts (via RS domain) with PHF5A (via
CC N-terminus) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle
CC {ECO:0000250}.
CC -!- DOMAIN: The C-terminal SR-rich domain is required for interactions with
CC SR proteins and the splicing regulators TRA and TRA2, and the N-
CC terminal domain is required for formation of the U2AF1/U2AF2
CC heterodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; BC126638; AAI26639.1; -; mRNA.
DR RefSeq; NP_001073737.1; NM_001080268.2.
DR AlphaFoldDB; A1A4K8; -.
DR SMR; A1A4K8; -.
DR STRING; 9913.ENSBTAP00000015465; -.
DR PaxDb; A1A4K8; -.
DR PRIDE; A1A4K8; -.
DR Ensembl; ENSBTAT00000015465; ENSBTAP00000015465; ENSBTAG00000011645.
DR GeneID; 512680; -.
DR KEGG; bta:512680; -.
DR CTD; 7307; -.
DR VEuPathDB; HostDB:ENSBTAG00000011645; -.
DR eggNOG; KOG2202; Eukaryota.
DR GeneTree; ENSGT00950000183152; -.
DR HOGENOM; CLU_059852_1_0_1; -.
DR InParanoid; A1A4K8; -.
DR OMA; NDGEDRW; -.
DR OrthoDB; 1340384at2759; -.
DR TreeFam; TF300143; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000011645; Expressed in omental fat pad and 108 other tissues.
DR ExpressionAtlas; A1A4K8; baseline and differential.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
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:0050733; F:RS domain binding; IEA:Ensembl.
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; Metal-binding; Methylation; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Spliceosome; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q01081"
FT CHAIN 2..237
FT /note="Splicing factor U2AF 35 kDa subunit"
FT /id="PRO_0000285836"
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 185..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..205
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q01081"
FT MOD_RES 39
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01081"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01081"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01081"
FT MOD_RES 165
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01081"
SQ SEQUENCE 237 AA; 27701 MW; D3705CFC4A4D36A3 CRC64;
MAEYLASIFG TEKDKVNCSF YFKIGACRHG DRCSRLHNKP TFSQTIALLN IYRNPQNSSQ
SADGLRCAVS DVEMQEHYDE FFEEVFTEME EKYGEVEEMN VCDNLGDHLV GNVYVKFRRE
EDAEKAVIDL NNRWFNGQPI HAELSPVTDF REACCRQYEM GECTRGGFCN FMHLKPISRE
LRRELYGRRR KKHRSRSRSR ERRSRSRDRG RGGGGGGGGG RERDRRRSRD RERSGRF
