PHAX_BOVIN
ID PHAX_BOVIN Reviewed; 394 AA.
AC Q3MHI4;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Phosphorylated adapter RNA export protein;
DE AltName: Full=RNA U small nuclear RNA export adapter protein;
GN Name=PHAX; Synonyms=RNUXA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-43.
RA Adelson D., Gill C.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: A phosphoprotein adapter involved in the XPO1-mediated U
CC snRNA export from the nucleus. Bridge components required for U snRNA
CC export, the cap binding complex (CBC)-bound snRNA on the one hand and
CC the GTPase Ran in its active GTP-bound form together with the export
CC receptor XPO1 on the other. Its phosphorylation in the nucleus is
CC required for U snRNA export complex assembly and export, while its
CC dephosphorylation in the cytoplasm causes export complex disassembly.
CC It is recycled back to the nucleus via the importin alpha/beta
CC heterodimeric import receptor. The directionality of nuclear export is
CC thought to be conferred by an asymmetric distribution of the GTP- and
CC GDP-bound forms of Ran between the cytoplasm and nucleus. Its
CC compartmentalized phosphorylation cycle may also contribute to the
CC directionality of export. Binds strongly to m7G-capped U1 and U5 small
CC nuclear RNAs (snRNAs) in a sequence-unspecific manner and
CC phosphorylation-independent manner. Also plays a role in the biogenesis
CC of U3 small nucleolar RNA (snoRNA). Involved in the U3 snoRNA transport
CC from nucleoplasm to Cajal bodies. Binds strongly to m7G-capped U3, U8
CC and U13 precursor snoRNAs and weakly to trimethylated (TMG)-capped U3,
CC U8 and U13 snoRNAs. Binds also to telomerase RNA (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Found in a U snRNA export complex with PHAX/RNUXA,
CC NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA. Part of a
CC precomplex with PHAX/RNUXA, NCBP1/CBP80, NCBP2/CBP20 and m7G-capped
CC RNA. Interacts with NCBP1/CBP80. Found in a complex with snoRNA,
CC Interacts with NCBP2/CBP20 (By similarity).
CC {ECO:0000250|UniProtKB:Q9H814, ECO:0000250|UniProtKB:Q9JJT9}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9H814}. Nucleus, Cajal body
CC {ECO:0000250|UniProtKB:Q9H814}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9H814}. Note=Located in the nucleoplasm and
CC Cajal bodies. Shuttles between the nucleus and the cytoplasm. Shuttles
CC between the nucleoplasm and Cajal bodies.
CC {ECO:0000250|UniProtKB:Q9H814}.
CC -!- PTM: Phosphorylated in the nucleus. Dephosphorylated in the cytoplasm.
CC -!- SIMILARITY: Belongs to the PHAX family. {ECO:0000305}.
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DR EMBL; BC105227; AAI05228.1; -; mRNA.
DR EMBL; CB171153; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001160034.1; NM_001166562.1.
DR AlphaFoldDB; Q3MHI4; -.
DR SMR; Q3MHI4; -.
DR STRING; 9913.ENSBTAP00000035479; -.
DR PaxDb; Q3MHI4; -.
DR PRIDE; Q3MHI4; -.
DR Ensembl; ENSBTAT00000035608; ENSBTAP00000035479; ENSBTAG00000009647.
DR GeneID; 507478; -.
DR KEGG; bta:507478; -.
DR CTD; 51808; -.
DR VEuPathDB; HostDB:ENSBTAG00000009647; -.
DR VGNC; VGNC:32807; PHAX.
DR eggNOG; KOG3948; Eukaryota.
DR GeneTree; ENSGT00390000011084; -.
DR HOGENOM; CLU_058840_1_0_1; -.
DR InParanoid; Q3MHI4; -.
DR OMA; EEGCIKK; -.
DR OrthoDB; 1223195at2759; -.
DR TreeFam; TF321050; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000009647; Expressed in occipital lobe and 104 other tissues.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:Ensembl.
DR GO; GO:0140262; F:mRNA cap binding complex binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0043489; P:RNA stabilization; IEA:Ensembl.
DR GO; GO:0006408; P:snRNA export from nucleus; IBA:GO_Central.
DR Gene3D; 1.10.10.1440; -; 1.
DR InterPro; IPR039047; PHAX.
DR InterPro; IPR019385; PHAX_RNA-binding_domain.
DR InterPro; IPR038092; PHAX_RNA-binding_sf.
DR PANTHER; PTHR13135; PTHR13135; 1.
DR Pfam; PF10258; RNA_GG_bind; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; RNA-binding; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H814"
FT CHAIN 2..394
FT /note="Phosphorylated adapter RNA export protein"
FT /id="PRO_0000239774"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..329
FT /note="Necessary for interaction with CBP80"
FT /evidence="ECO:0000250"
FT REGION 178..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..328
FT /note="Sufficient for poly U RNA-binding"
FT /evidence="ECO:0000250"
FT REGION 279..287
FT /note="Necessary for poly U RNA-binding and snRNA export"
FT /evidence="ECO:0000250"
FT REGION 365..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 81..84
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 130..139
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT MOTIF 198..201
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 61..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H814"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H814"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H814"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63068"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63068"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63068"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63068"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63068"
FT MOD_RES 296
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H814"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H814"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H814"
FT CONFLICT 1
FT /note="M -> W (in Ref. 1; AAI05228)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 394 AA; 44578 MW; 98217571B875DC61 CRC64;
MAQEAGDMDD GQVSDSDSDM TVAPSDRPLP VPKALGGDCG LRPFQSTATA CAPASHYRTV
KSVDSSEESF SDSDDDSSVW KRKRQKCFNT PPKPEPFQFD QSSQKPPIAG RKKVNNIWSA
VLQEQNQDAV ATELGILGME GTIDRSRQSE TYNYLLAKKL KRESQEHTKE LDKELEEYMH
GGKKTGPKEE ENGQGHPKRK RPVKDRVGDR LEMNYKGRYE ITEDDSQERV ADEISFRLQE
PKKDLIARVV RIIGNKKAIE LLMETAEVEQ NGGLFIMNGS RRRTPGGVFL NLLKNTPSIS
EEQIKDIFYL ENQKEYENKK AARKRRIQVM GKKMKQAIKN LNFQEDDDTS RETFASDTNE
ALASLDESQE GHGETKLDAE EAIEVDHSHD LDMF
