U2AF1_PIG
ID U2AF1_PIG Reviewed; 82 AA.
AC Q29350;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 106.
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;
DE Flags: Fragment;
GN Name=U2AF1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
RX PubMed=8672129; DOI=10.1007/s003359900153;
RA Winteroe A.K., Fredholm M., Davies W.;
RT "Evaluation and characterization of a porcine small intestine cDNA library:
RT analysis of 839 clones.";
RL Mamm. Genome 7:509-517(1996).
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 -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; F14757; CAA23231.1; -; mRNA.
DR AlphaFoldDB; Q29350; -.
DR SMR; Q29350; -.
DR STRING; 9823.ENSSSCP00000003119; -.
DR PaxDb; Q29350; -.
DR PeptideAtlas; Q29350; -.
DR PRIDE; Q29350; -.
DR eggNOG; KOG2202; Eukaryota.
DR HOGENOM; CLU_059852_1_0_1; -.
DR InParanoid; Q29350; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; Q29350; SS.
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:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR InterPro; IPR009145; U2AF_small.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR12620; PTHR12620; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR PRINTS; PR01848; U2AUXFACTOR.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Metal-binding; Methylation; mRNA processing; mRNA splicing;
KW Nucleus; Reference proteome; Repeat; RNA-binding; Spliceosome; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q01081"
FT CHAIN 2..>82
FT /note="Splicing factor U2AF 35 kDa subunit"
FT /id="PRO_0000081996"
FT DOMAIN 65..>82
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 12..40
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
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 NON_TER 82
SQ SEQUENCE 82 AA; 9416 MW; 96882458044823A8 CRC64;
MAEYLASIFG TEKDKVNCSF YFKIGACRHG DRCSRLHNKP TFSQTIVLLN LYRNPQNTAQ
TADGSHCHVS DVEVQEHYDN FF
