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   27-MAR-2024, entry version 131.
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; 10090-ENSMUSP00000033532; -.
DR   ProteomicsDB; 285734; -.
DR   Antibodypedia; 529; 181 antibodies from 23 providers.
DR   DNASU; 14266; -.
DR   Ensembl; ENSMUST00000033532.7; ENSMUSP00000033532.7; ENSMUSG00000031189.13.
DR   GeneID; 14266; -.
DR   KEGG; mmu:14266; -.
DR   UCSC; uc009tjb.1; mouse.
DR   AGR; MGI:1202294; -.
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; PKEKESM; -.
DR   OrthoDB; 4254515at2759; -.
DR   PhylomeDB; O55112; -.
DR   TreeFam; TF326216; -.
DR   BioGRID-ORCS; 14266; 2 hits in 81 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 76 other cell types or tissues.
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   Gene3D; 6.10.250.2670; -; 1.
DR   InterPro; IPR007797; AF4/FMR2.
DR   InterPro; IPR043640; AF4/FMR2_CHD.
DR   InterPro; IPR043639; AF4_int.
DR   PANTHER; PTHR10528; AF4/FMR2 FAMILY MEMBER; 1.
DR   PANTHER; PTHR10528:SF18; AF4_FMR2 FAMILY MEMBER 2; 1.
DR   Pfam; PF05110; AF-4; 2.
DR   Pfam; PF18875; AF4_int; 1.
DR   Pfam; PF18876; AFF4_CHD; 1.
DR   Genevisible; O55112; MM.
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
//