AFF2_MOUSE
ID AFF2_MOUSE Reviewed; 1272 AA.
AC O55112; B1ATW0;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=AF4/FMR2 family member 2 {ECO:0000312|MGI:MGI:1202294};
DE AltName: Full=Protein FMR-2;
DE Short=FMR2P;
DE AltName: Full=Protein Ox19;
GN Name=Aff2 {ECO:0000312|MGI:MGI:1202294}; Synonyms=Fmr2, Ox19;
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=9467002; DOI=10.1093/hmg/7.3.441;
RA Chakrabarti L., Bristulf J., Foss G.S., Davies K.E.;
RT "Expression of the murine homologue of FMR2 in mouse brain and during
RT development.";
RL Hum. Mol. Genet. 7:441-448(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19136466; DOI=10.1093/nar/gkn1058;
RA Bensaid M., Melko M., Bechara E.G., Davidovic L., Berretta A.,
RA Catania M.V., Gecz J., Lalli E., Bardoni B.;
RT "FRAXE-associated mental retardation protein (FMR2) is an RNA-binding
RT protein with high affinity for G-quartet RNA forming structure.";
RL Nucleic Acids Res. 37:1269-1279(2009).
CC -!- FUNCTION: RNA-binding protein. Might be involved in alternative
CC splicing regulation through an interaction with G-quartet RNA
CC structure. {ECO:0000269|PubMed:19136466}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:19136466}.
CC Note=When splicing or transcription are inhibited, accumulates in
CC large, rounded speckles and in the nucleolus. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the hippocampus, the piriform
CC cortex, Purkinje cells and the cingulate gyrus.
CC -!- DEVELOPMENTAL STAGE: Expressed before day 7 in the embryo and reached
CC its highest levels at 10.5-11.5 days. In the embryo at day 11,
CC expression is more specific in the roof of the hind brain and the
CC lateral ventricle of the brain.
CC -!- SIMILARITY: Belongs to the AF4 family. {ECO:0000305}.
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DR EMBL; AJ001549; CAA04821.1; -; mRNA.
DR EMBL; AL663113; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL672120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL808131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX294655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS30173.1; -.
DR PIR; T30248; T30248.
DR RefSeq; NP_032058.2; NM_008032.3.
DR AlphaFoldDB; O55112; -.
DR SMR; O55112; -.
DR BioGRID; 199717; 3.
DR STRING; 10090.ENSMUSP00000033532; -.
DR iPTMnet; O55112; -.
DR PhosphoSitePlus; O55112; -.
DR EPD; O55112; -.
DR PaxDb; O55112; -.
DR PRIDE; O55112; -.
DR ProteomicsDB; 285734; -.
DR Antibodypedia; 529; 162 antibodies from 23 providers.
DR DNASU; 14266; -.
DR Ensembl; ENSMUST00000033532; ENSMUSP00000033532; ENSMUSG00000031189.
DR GeneID; 14266; -.
DR KEGG; mmu:14266; -.
DR UCSC; uc009tjb.1; mouse.
DR CTD; 2334; -.
DR MGI; MGI:1202294; Aff2.
DR VEuPathDB; HostDB:ENSMUSG00000031189; -.
DR eggNOG; ENOG502QR32; Eukaryota.
DR GeneTree; ENSGT00950000182974; -.
DR HOGENOM; CLU_006484_0_0_1; -.
DR InParanoid; O55112; -.
DR OMA; THSSAPM; -.
DR OrthoDB; 558558at2759; -.
DR PhylomeDB; O55112; -.
DR TreeFam; TF326216; -.
DR BioGRID-ORCS; 14266; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Aff2; mouse.
DR PRO; PR:O55112; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; O55112; protein.
DR Bgee; ENSMUSG00000031189; Expressed in undifferentiated genital tubercle and 74 other tissues.
DR Genevisible; O55112; MM.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0002151; F:G-quadruplex RNA binding; IDA:UniProtKB.
DR GO; GO:0007611; P:learning or memory; IMP:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR GO; GO:0035063; P:nuclear speck organization; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
DR GO; GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR007797; AF4/FMR2.
DR InterPro; IPR043640; AF4/FMR2_CHD.
DR InterPro; IPR043639; AF4_int.
DR PANTHER; PTHR10528; PTHR10528; 1.
DR Pfam; PF18876; AF-4_C; 1.
DR Pfam; PF18875; AF4_int; 1.
PE 2: Evidence at transcript level;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT CHAIN 1..1272
FT /note="AF4/FMR2 family member 2"
FT /id="PRO_0000215913"
FT REGION 151..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..678
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..870
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51816"
FT MOD_RES 482
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51816"
FT CONFLICT 432
FT /note="P -> S (in Ref. 1; CAA04821)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="A -> S (in Ref. 1; CAA04821)"
FT /evidence="ECO:0000305"
FT CONFLICT 941
FT /note="V -> A (in Ref. 1; CAA04821)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1272 AA; 140181 MW; 1CE41F1AEFE9C2B4 CRC64;
MDLFDFFRDW DLEQQCHYEQ DRSALKKREW ERRNQEVQQE EDLFSSGFDL FGEPYKVAEY
TNKGDALANR VQNTLGSYDE MKDLLSNHSS QNHLVGIPKN SAPQTPISKS EASFYPEQKN
RMIPSHQETT HSSTPMPPPS VVILNSTLIH SNRKSKSEWP RDSHNTSPAQ ASQTSSQPNK
MQTSTQDPPQ TRLEDFFVYP AEQPQIGTVE KSNPSSKEEN NPNSGGEDTF KEIFQSNSPE
ESEFTVQAPG SPLVASSLLA PSSGLSVPTF PPGLYCKTSM GQQKPTAYVR PMDGQDQATD
ISPTLKPSIE FENSFGNLSF GSLLDGKPSA VSSKTKLPKF TILQTSEVSL TSDPSCVEEI
LRESQHLTPG FTLQKWSDPS SRASTKMLED DLKLSSDEDD LEPVKTLTTQ CTANELYQAV
EKAKPKNNPV NPLLATPQST PATQTNVGSG SSSESESSSE SDSDTESSTT DSESNEAPRV
ATPEPEPPST NKWQLDKWLN KVTSQNKSFI CGQNETPTET ISLPPPIIQP VEVQVKVKPN
PSQAVAVPKE RPLLSLIREK ARPRPTQKTP ETKALKHKLS TSVDTVSQRT IGKKQPKKVE
KNTSFEEFTW PKPNITNSTP KEKGSVELPD PPRSRNKATA HKPVPRKEPR PHVPLATEKK
KYRGPGKIVP KSREFIETDS STSDSNTDQE ETLQIKVLPP CITSKSKETS NASLTLSTLT
NGNSNNLSTS NEETAFSPPP AMQTELLSPL RDHENPKNLW VKIDLDLLSR VPGQNSVPVT
PAKTDYKETA SKPKRQTAAT AVEKPAPKGK RKHKPAETAE KIPEKKQRLE DNTTICLLPP
CISPAPPHKP PSTRENSSRR ANRKKEEKLF PPALSPLAED PPRRRNVSGN NGHFGQDKNI
SMAGQITSSK PKRSEGKFCA TFKGISINEG DAPKKAASAT VTVANMALAT ATATATVPAI
VTATVTATAT TTATATTTTT TTTISSITPT ITSGLMDSSH LEMTSWAALP LLSSSSANVR
RPKLTFDDSV HNADFYMQEA KKLKHKADAL FEKFGKAVNY ADAALSFTEC GNAMERDPLE
AKSPYTMYSE TVELLRYAMR LKNFASPLAS DGDKKLAVLC YRCLSLLYLR MFKLKKDHAM
KYSRSLMEYF KQNASKVTQI PSPWVGNGKN TPSPVSLNNV SPINSVGNCN NGPVTIPQRI
HHMAASHVNI TSNVLRGYEH WDMADKLTRD NKEFFGDLDT LMGPLTQHSS MTNLVRYVRQ
GLCWLRIDAH LL
