FUBP2_CHICK
ID FUBP2_CHICK Reviewed; 769 AA.
AC Q8UVD9;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Far upstream element-binding protein 2;
DE Short=FUSE-binding protein 2;
DE AltName: Full=KH type-splicing regulatory protein;
DE Short=KSRP;
DE AltName: Full=Zipcode-binding protein 2;
GN Name=KHSRP; Synonyms=FUBP2, ZPB2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000312|EMBL:AAL66365.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 104-119; 242-267; 679-685;
RP 705-711 AND 743-766, FUNCTION, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11781334; DOI=10.1083/jcb.200105133;
RA Gu W., Pan F., Zhang H., Bassell G.J., Singer R.H.;
RT "A predominantly nuclear protein affecting cytoplasmic localization of
RT beta-actin mRNA in fibroblasts and neurons.";
RL J. Cell Biol. 156:41-52(2002).
CC -!- FUNCTION: Part of a ternary complex that binds to the downstream
CC control sequence (DCS) of the pre-mRNA. Mediates exon inclusion in
CC transcripts that are subject to tissue-specific alternative splicing.
CC May interact with single-stranded DNA from the far-upstream element
CC (FUSE). May activate gene expression. Also involved in degradation of
CC inherently unstable mRNAs that contain AU-rich elements (AREs) in their
CC 3'-UTR, possibly by recruiting degradation machinery to ARE-containing
CC mRNAs. Binds to the dendritic targeting element and may play a role in
CC mRNA trafficking (By similarity). Binds to a 54-nucleotide localization
CC signal (the 'zipcode') found in the 3'-UTR of beta-actin mRNA and may
CC play a role in its localization. {ECO:0000250,
CC ECO:0000269|PubMed:11781334}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11781334}. Cytoplasm
CC {ECO:0000269|PubMed:11781334}. Note=Predominantly nuclear.
CC -!- DEVELOPMENTAL STAGE: The highest expression is found in 6-d embryos, is
CC reduced to 30% before hatching and remains stable thereafter.
CC {ECO:0000269|PubMed:11781334}.
CC -!- SIMILARITY: Belongs to the KHSRP family. {ECO:0000305}.
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DR EMBL; AF461020; AAL66365.1; -; mRNA.
DR RefSeq; NP_989608.1; NM_204277.1.
DR AlphaFoldDB; Q8UVD9; -.
DR SMR; Q8UVD9; -.
DR BioGRID; 675173; 1.
DR GeneID; 374140; -.
DR CTD; 8570; -.
DR VEuPathDB; HostDB:geneid_417184; -.
DR VEuPathDB; HostDB:geneid_424551; -.
DR InParanoid; Q8UVD9; -.
DR OrthoDB; 590738at2759; -.
DR PhylomeDB; Q8UVD9; -.
DR PRO; PR:Q8UVD9; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISS:UniProtKB.
DR GO; GO:0008298; P:intracellular mRNA localization; NAS:UniProtKB.
DR GO; GO:0010586; P:miRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 3.30.1370.10; -; 4.
DR InterPro; IPR015096; FUBP_C.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR Pfam; PF09005; DUF1897; 2.
DR Pfam; PF00013; KH_1; 4.
DR SMART; SM00322; KH; 4.
DR SUPFAM; SSF54791; SSF54791; 4.
DR PROSITE; PS50084; KH_TYPE_1; 4.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; mRNA transport; Nucleus;
KW Reference proteome; Repeat; RNA-binding; Transport.
FT CHAIN 1..769
FT /note="Far upstream element-binding protein 2"
FT /id="PRO_0000050139"
FT DOMAIN 208..272
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117,
FT ECO:0000305"
FT DOMAIN 296..362
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117,
FT ECO:0000305"
FT DOMAIN 385..449
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117,
FT ECO:0000305"
FT DOMAIN 486..553
FT /note="KH 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117,
FT ECO:0000305"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..177
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..604
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..672
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 769 AA; 80644 MW; 875A6C83529969EB CRC64;
MEISTPDFGF GTEDSSAQQS ANRAIPQPVP APAFPLKETA SDTGGTAPTF GTLQDNINEL
CLRYQTVCSE GRDGTGGGGP PGGGIRKDAF ADAVQRARQI AAKIGGDAAT TVNNSTPDFG
FGGQKRQLED GDQPESKKLA AQGDCEYGPR GGAPAAPPER SGPVGDPPGP PRAERGRRPP
PALTGGALPS AALPPQLGPM HPPPRSTTVT EEYRVPDGMV GLIIGRGGEQ INKIQQDSGC
KVQISPDSGG LPERSVSLTG SPEAVQKAKL MLDDIVSRGR GGPPGQFHDY ANGQNGTVQE
IMIPAGKAGL VIGKGGETIK QLQERAGVKM IFIQDGSQNT NVDKPLRIIG DPYKVQQACE
MVMDILRERD QGGFGDRNEY GSRIGGGIDV PVPRHSVGVV IGRSGEMIKK IQNDAGVRIQ
FKQDDGTGPE KIAHIMGPPE RCEHAARIIN DLLQSLRSGP PGPPGHGMPP GGRGRGRGQG
IWGPPGGEMT FSIPTHKCGL VIGRGGENVK AINQQRGAFV EISRQLPPNG DPNFKLFIIR
GSPQQIEHAK QPIEEKIEGP LCPVGPGPGP GGPPGPAGPM GPFNPGPFNQ GPPGGPPPHQ
YPPQGWGNTY PQWQPPAPHD PSKAAAAADP NAAWAGYYSH YYQQPPGPVP GQPPAPTAPP
VQGEPPQPPP TGQSDYTKAW EEYYKKIGQQ PQQPGAPPQQ DYTKAWEEYY KKQAAQVATG
GGPGAPPGPQ PDYSAAWAEY YRQQAAYYGQ TPGAAGPAPP PTQQGQQAQ
