PHAX_RAT
ID PHAX_RAT Reviewed; 385 AA.
AC Q63068; Q4QQW9; Q5RJZ7;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Phosphorylated adapter RNA export protein;
DE AltName: Full=26 kDa resiniferatoxin-binding protein;
DE AltName: Full=RBP-26;
DE AltName: Full=RNA U small nuclear RNA export adapter protein;
DE AltName: Full=RTX-42;
DE AltName: Full=Resiniferatoxin-binding protein 2;
DE Short=RBP-2;
GN Name=Phax; Synonyms=Rnuxa;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=8015392; DOI=10.1016/0169-328x(94)90030-2;
RA Ninkina N., Willoughby J., Beech M., Coore P., Wood J.;
RT "Molecular cloning of a resiniferatoxin-binding protein.";
RL Brain Res. Mol. Brain Res. 22:39-48(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, and Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-56; SER-57; SER-60;
RP SER-63 AND SER-217, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 {ECO:0000250|UniProtKB:Q9H814}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:Q9H814}. Nucleus, Cajal body
CC {ECO:0000250|UniProtKB:Q9H814}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9H814}. Note=Shuttles between the nucleus and
CC the cytoplasm. Shuttles between the nucleoplasm and Cajal bodies.
CC {ECO:0000250|UniProtKB:Q9H814}.
CC -!- TISSUE SPECIFICITY: Expressed in dorsal root ganglia and sensory neuron
CC cell bodies. {ECO:0000269|PubMed:8015392}.
CC -!- PTM: Phosphorylated in the nucleus. Dephosphorylated in the cytoplasm.
CC -!- SIMILARITY: Belongs to the PHAX family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA48076.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X67877; CAA48076.1; ALT_FRAME; mRNA.
DR EMBL; BC086410; AAH86410.1; -; mRNA.
DR EMBL; BC097932; AAH97932.1; -; mRNA.
DR PIR; I60184; S33448.
DR RefSeq; NP_775156.2; NM_173133.2.
DR AlphaFoldDB; Q63068; -.
DR SMR; Q63068; -.
DR BioGRID; 251908; 1.
DR STRING; 10116.ENSRNOP00000019627; -.
DR iPTMnet; Q63068; -.
DR PhosphoSitePlus; Q63068; -.
DR jPOST; Q63068; -.
DR PaxDb; Q63068; -.
DR PRIDE; Q63068; -.
DR Ensembl; ENSRNOT00000019627; ENSRNOP00000019627; ENSRNOG00000014459.
DR GeneID; 286917; -.
DR KEGG; rno:286917; -.
DR UCSC; RGD:708448; rat.
DR CTD; 51808; -.
DR RGD; 708448; Phax.
DR eggNOG; KOG3948; Eukaryota.
DR GeneTree; ENSGT00390000011084; -.
DR HOGENOM; CLU_058840_1_0_1; -.
DR InParanoid; Q63068; -.
DR OMA; EEGCIKK; -.
DR OrthoDB; 1223195at2759; -.
DR PhylomeDB; Q63068; -.
DR TreeFam; TF321050; -.
DR Reactome; R-RNO-6807505; RNA polymerase II transcribes snRNA genes.
DR PRO; PR:Q63068; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000014459; Expressed in cerebellum and 20 other tissues.
DR Genevisible; Q63068; RN.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
DR GO; GO:0140262; F:mRNA cap binding complex binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0015643; F:toxic substance binding; IPI:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0043489; P:RNA stabilization; ISO:RGD.
DR GO; GO:0006408; P:snRNA export from nucleus; ISO:RGD.
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 1: Evidence at protein 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..385
FT /note="Phosphorylated adapter RNA export protein"
FT /id="PRO_0000239777"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..320
FT /note="Necessary for interaction with CBP80"
FT /evidence="ECO:0000250"
FT REGION 72..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..319
FT /note="Sufficient for poly U RNA-binding"
FT /evidence="ECO:0000250"
FT REGION 270..278
FT /note="Necessary for poly U RNA-binding and snRNA export"
FT /evidence="ECO:0000250"
FT REGION 334..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 71..74
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 120..129
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT MOTIF 189..192
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 164..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..385
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:0007744|PubMed:22673903"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H814"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 287
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H814"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H814"
FT CONFLICT 96
FT /note="P -> Q (in Ref. 1; CAA48076)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="E -> D (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 43166 MW; C53797EA193EAD5B CRC64;
MALEAGDMEE GQLSDSDSDM TVVPSDRPLQ MAKVLGGGGA ACAPVSNYRT VKHVDSSEES
LDSDDDCSLW KRKRQKCHSP PPKPEPFPFG QSGQKPALNG GKKVNNIWGA VLQEQNQDAV
ATELGILGME GTIDRSRQSE TYNYLLAKKL AKKESQEYTK ELDKDLDEYM HGDKKPGSKE
EENGQGHLKR KRPVRDRLGN RVEMNYKGRY DITEEDSPEK VADEIAFRLQ EPKKDLIARV
VTILGNKKAI ELLMETAEVE QNGGLFIMNG SRRRTPGGVF LNLLKNTPSI SEEQIKDIFY
IENQKEYENK KAARKRRTQL LGKKMKEAIK SLNFQEDDDT SRETFASDTN EALASLDEAQ
EGPGETKLDA EDAIEVDHPQ DLDIF
