U2AFM_MOUSE
ID U2AFM_MOUSE Reviewed; 462 AA.
AC Q62377;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2;
DE AltName: Full=CCCH type zinc finger, RNA-binding motif and serine/arginine rich protein 2;
DE AltName: Full=U2(RNU2) small nuclear RNA auxiliary factor 1-like 2;
DE AltName: Full=U2AF35-related protein;
DE Short=URP;
GN Name=Zrsr2; Synonyms=U2af1-rs2, U2af1l2, U2af1rs2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7558001; DOI=10.1006/geno.1995.1051;
RA Yamaoka T., Hatada I., Kitagawa K., Wang X., Mukai T.;
RT "Cloning and mapping of the U2af1-rs2 gene with a high transmission
RT distortion in interspecific backcross progeny.";
RL Genomics 27:337-340(1995).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Pre-mRNA-binding protein required for splicing of both
CC U2- and U12-type introns. Selectively interacts with the 3'-splice site
CC of U2- and U12-type pre-mRNAs and promotes different steps in U2 and
CC U12 intron splicing. Recruited to U12 pre-mRNAs in an ATP-dependent
CC manner and is required for assembly of the prespliceosome, a precursor
CC to other spliceosomal complexes. For U2-type introns, it is selectively
CC and specifically required for the second step of splicing (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the U11/U12 snRNPs that are part of the U12-type
CC spliceosome. Interacts (via RS domain) with SRSF1 and SRSF2. Interacts
CC with U2AF2/U2AF65 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Phosphorylated in the RS domain by SRPK1. {ECO:0000250}.
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DR EMBL; D45205; BAA08143.1; -; mRNA.
DR PIR; A57120; A57120.
DR AlphaFoldDB; Q62377; -.
DR SMR; Q62377; -.
DR STRING; 10090.ENSMUSP00000107908; -.
DR iPTMnet; Q62377; -.
DR PhosphoSitePlus; Q62377; -.
DR EPD; Q62377; -.
DR jPOST; Q62377; -.
DR MaxQB; Q62377; -.
DR PaxDb; Q62377; -.
DR PeptideAtlas; Q62377; -.
DR PRIDE; Q62377; -.
DR ProteomicsDB; 297691; -.
DR MGI; MGI:103287; Zrsr2.
DR eggNOG; KOG2202; Eukaryota.
DR InParanoid; Q62377; -.
DR Reactome; R-MMU-72165; mRNA Splicing - Minor Pathway.
DR ChiTaRS; Zrsr2; mouse.
DR PRO; PR:Q62377; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q62377; protein.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0005689; C:U12-type spliceosomal complex; ISS:UniProtKB.
DR GO; GO:0089701; C:U2AF complex; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030628; F:pre-mRNA 3'-splice site binding; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0000245; P:spliceosomal complex assembly; ISS:UniProtKB.
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; 1.
DR PRINTS; PR01848; U2AUXFACTOR.
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 1: Evidence at protein level;
KW Isopeptide bond; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Spliceosome; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..462
FT /note="U2 small nuclear ribonucleoprotein auxiliary factor
FT 35 kDa subunit-related protein 2"
FT /id="PRO_0000082002"
FT DOMAIN 202..308
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 170..198
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 310..337
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..427
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15696"
FT CROSSLNK 49
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15696"
SQ SEQUENCE 462 AA; 55358 MW; 0E980C029ACBA196 CRC64;
METAGATADA TAGPQKLSRK KYLALRKKER RKRRRQALAR LREAELAQKE EEEDPLAEEK
RLEEERLLEE ERQRLHEEWL LREEKAQEEF RAKKKKEEEA RKRKEELERK LKAEWEEQQR
KEREEEEQKR QEKREREEAV QKMLDQAENE LENGGTWQNP EPPMDIRVLE KDRANCPFYS
KTGACRFGDR CSRKHNFPTS SPTLLIKGMF TTFGMEQCRR DDYDPDSSLE FSEEEIYQQF
LDFYYDVLPE FKSVGKVIQF KVSCNLEPHL RGNVYVQYQS EEDCQAAFSV FNGRWYAGRQ
LQCEFCPVTR WKMAICGLFE VQQCPRGKHC NFLHVFRNPN NEYRDANRDL YPSPDWTSSS
FGKNSERRER ASHYDEYYGR SRRRRRSPSP DFYKRNGESD RKSSSRHRVK KSHRYGMKSR
ERRSSPSRRR KDHSPGPWEP EQEEPPQQES QSQPQPQPQS DP
