U2AFL_MOUSE
ID U2AFL_MOUSE Reviewed; 428 AA.
AC Q64707;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 1;
DE AltName: Full=CCCH type zinc finger, RNA-binding motif and serine/arginine rich protein 1;
DE AltName: Full=SP2;
DE AltName: Full=U2(RNU2) small nuclear RNA auxiliary factor 1-like 1;
GN Name=Zrsr1; Synonyms=Sp2, Sp2-7, U2af1-rs1, U2af1l1;
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=8284201; DOI=10.1093/nar/21.24.5577;
RA Hatada I., Sugama T., Mukai T.;
RT "A new imprinted gene cloned by a methylation-sensitive genome scanning
RT method.";
RL Nucleic Acids Res. 21:5577-5582(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=PWK; TISSUE=Liver;
RX PubMed=8136831; DOI=10.1038/ng0194-33;
RA Hayashizaki Y., Shibata H., Hirotsune S., Sugino H., Okazaki Y., Sasaki N.,
RA Hirose K., Imoto H., Okuizumi H., Muramatsu M., Komasubara H.,
RA Shiroishi T., Moriwaki K., Katsuki M., Hatano N., Sasaki H., Ueda T.,
RA Mise N., Takagi N., Plass C., Chapman V.M.;
RT "Identification of an imprinted U2af binding protein related sequence on
RT mouse chromosome 11 using the RLGS method.";
RL Nat. Genet. 6:33-40(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MATERNAL IMPRINTING.
RC TISSUE=Liver;
RX PubMed=7870588; DOI=10.1093/nar/23.1.36;
RA Hatada I., Kitagawa K., Yamaoka T., Wang X., Arai Y., Hashido K.,
RA Ohishi S., Masuda J., Ogata J., Mukai T.;
RT "Allele-specific methylation and expression of an imprinted U2af1-rs1 (SP2)
RT gene.";
RL Nucleic Acids Res. 23:36-41(1995).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=10679248; DOI=10.1006/bbrc.2000.2189;
RA Sunahara S., Nakamura K., Nakao K., Gondo Y., Nagata Y., Katsuki M.;
RT "The oocyte-specific methylated region of the U2afbp-rs/U2af1-rs1 gene is
RT dispensable for its imprinted methylation.";
RL Biochem. Biophys. Res. Commun. 268:590-595(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Spleen;
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).
RN [6]
RP FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND INTERACTION WITH
RP SF3B1 AND ZCRB1.
RX PubMed=29617656; DOI=10.1016/j.celrep.2018.03.028;
RA Horiuchi K., Perez-Cerezales S., Papasaikas P., Ramos-Ibeas P.,
RA Lopez-Cardona A.P., Laguna-Barraza R., Fonseca Balvis N., Pericuesta E.,
RA Fernandez-Gonzalez R., Planells B., Viera A., Suja J.A., Ross P.J.,
RA Alen F., Orio L., Rodriguez de Fonseca F., Pintado B., Valcarcel J.,
RA Gutierrez-Adan A.;
RT "Impaired spermatogenesis, muscle, and erythrocyte function in U12 intron
RT splicing-defective zrsr1 mutant mice.";
RL Cell Rep. 23:143-155(2018).
CC -!- FUNCTION: Plays a role in splicing of the U12-type introns
CC (PubMed:29617656). Implicated also in removal of U2 introns positioned
CC adjacent to a U12 intron (PubMed:29617656).
CC {ECO:0000269|PubMed:29617656}.
CC -!- SUBUNIT: Interacts with SF3B1 (PubMed:29617656). Interacts with ZCRB1
CC (PubMed:29617656). {ECO:0000269|PubMed:29617656}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Highest expression levels are detected in the
CC brain, and lower expression levels in other tissues like epididymis,
CC testis, bone marrow or muscle (PubMed:29617656). In testis, expressed
CC in both Sertoli and spermatogenic cell (PubMed:29617656).
CC {ECO:0000269|PubMed:29617656}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the 2-cell stage, and at the morula
CC and blastocyst stages. {ECO:0000269|PubMed:29617656}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, possibly because of the
CC compensating effects of one or more of the other 3 paralogs (U2AF1,
CC U2AF1L4, ZRSR2). {ECO:0000269|PubMed:10679248}.
CC -!- MISCELLANEOUS: Maternally imprinted. Active paternal allele is
CC unmethylated whereas the inactive maternal allele is highly methylated.
CC {ECO:0000269|PubMed:7870588}.
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DR EMBL; D17407; BAA04230.1; -; mRNA.
DR EMBL; S69507; AAB30301.1; -; mRNA.
DR EMBL; D26474; BAA05486.1; -; Genomic_DNA.
DR PIR; S41485; S41485.
DR RefSeq; NP_035793.1; NM_011663.3.
DR AlphaFoldDB; Q64707; -.
DR SMR; Q64707; -.
DR STRING; 10090.ENSMUSP00000062025; -.
DR iPTMnet; Q64707; -.
DR PhosphoSitePlus; Q64707; -.
DR PaxDb; Q64707; -.
DR PeptideAtlas; Q64707; -.
DR PRIDE; Q64707; -.
DR ProteomicsDB; 297690; -.
DR Antibodypedia; 8950; 110 antibodies from 22 providers.
DR DNASU; 22183; -.
DR Ensembl; ENSMUST00000049506; ENSMUSP00000062025; ENSMUSG00000044068.
DR GeneID; 22183; -.
DR KEGG; mmu:22183; -.
DR UCSC; uc007iem.2; mouse.
DR CTD; 22183; -.
DR MGI; MGI:98885; Zrsr1.
DR VEuPathDB; HostDB:ENSMUSG00000044068; -.
DR eggNOG; KOG2202; Eukaryota.
DR GeneTree; ENSGT00950000183152; -.
DR HOGENOM; CLU_029117_1_0_1; -.
DR InParanoid; Q64707; -.
DR OMA; EMQKCPK; -.
DR OrthoDB; 377499at2759; -.
DR PhylomeDB; Q64707; -.
DR TreeFam; TF324447; -.
DR BioGRID-ORCS; 22183; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Sp2; mouse.
DR PRO; PR:Q64707; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q64707; protein.
DR Bgee; ENSMUSG00000044068; Expressed in retinal neural layer and 251 other tissues.
DR ExpressionAtlas; Q64707; baseline and differential.
DR Genevisible; Q64707; MM.
DR GO; GO:0005681; C:spliceosomal complex; IMP:UniProtKB.
DR GO; GO:0005689; C:U12-type spliceosomal complex; IMP: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; ISO:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:UniProtKB.
DR GO; GO:0000245; P:spliceosomal complex assembly; ISO:MGI.
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 Metal-binding; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Spliceosome;
KW Zinc; Zinc-finger.
FT CHAIN 1..428
FT /note="U2 small nuclear ribonucleoprotein auxiliary factor
FT 35 kDa subunit-related protein 1"
FT /id="PRO_0000082000"
FT DOMAIN 189..295
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 157..185
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 297..324
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..34
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..406
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15696"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15696"
FT CONFLICT 351
FT /note="N -> S (in Ref. 2; AAB30301)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 428 AA; 51364 MW; 4542EE234B0759E6 CRC64;
MASRQTAIPE KLSRKQYKAA MKKEKRKKRR QKMARLRALE APPEEDDDVS ANEELAERLL
EIERQRLHEE WLLREEKAQE EFRIKKKKEE AARKQKEEQE RQIKAEWEEQ QKKQREEEEQ
KLQEKREREE AVQKMLDQAE NERIWQNPEP PKDLRLEKYR PSCPFYNKTG ACRFGNRCSR
KHDFPTSSPT LLVKSMFTTF GMEQCRRDDY DSDANLEYSE EETYQQFLDF YHDVLPEFKN
VGKVIQFKVS CNLEPHLRGN VYVQYQSEEE CQAALSLFNG RWYAGRQLQC EFCPVTRWKV
AICGLFEMQK CPKGKHCNFL HVFRNPNNEF REANRDIYMS PPAWTGSSGK NSDRRERKDH
HEEYYSKSRS YHSGSYHSSK RNRESERKSP HRWKKSHKQT TKSHERHSSR RGREEDSSPG
PQSQSHRT
