HNRPQ_RAT
ID HNRPQ_RAT Reviewed; 533 AA.
AC Q7TP47;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein Q;
DE Short=hnRNP Q;
DE AltName: Full=Liver regeneration-related protein LRRG077;
DE AltName: Full=Synaptotagmin-binding, cytoplasmic RNA-interacting protein;
GN Name=Syncrip; Synonyms=Hnrpq; ORFNames=Ab2-339;
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 [LARGE SCALE MRNA].
RC TISSUE=Liver;
RA Xu C.S., Li W.Q., Li Y.C., Ma H., Wang L., Wang S.F., Han H.P., Wang G.P.,
RA Chai L.Q., Yuan J.Y., Yang K.J., Yan H.M., Chang C.F., Zhao L.F., Shi J.B.,
RA Rahman S., Wang Q.N., Zhang J.B.;
RT "Liver regeneration after PH.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Heterogenous nuclear ribonucleoprotein (hnRNP) implicated in
CC mRNA processing mechanisms. Component of the CRD-mediated complex that
CC promotes MYC mRNA stability. Is associated in vitro with pre-mRNA,
CC splicing intermediates and mature mRNA protein complexes. Binds to apoB
CC mRNA AU-rich sequences. Part of the APOB mRNA editosome complex and may
CC modulate the postranscriptional C to U RNA-editing of the APOB mRNA
CC through either by binding to A1CF (APOBEC1 complementation factor), to
CC APOBEC1 or to RNA itself. May be involved in translationally coupled
CC mRNA turnover. Implicated with other RNA-binding proteins in the
CC cytoplasmic deadenylation/translational and decay interplay of the FOS
CC mRNA mediated by the major coding-region determinant of instability
CC (mCRD) domain. Interacts in vitro preferentially with poly(A) and
CC poly(U) RNA sequences. May be involved in cytoplasmic vesicle-based
CC mRNA transport through interaction with synaptotagmins (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Identified in a histone pre-mRNA complex, at least composed of
CC ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1. Identified in the
CC spliceosome C complex (By similarity). Component of the coding region
CC determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1,
CC SYNCRIP and YBX1. Identified in a mRNP complex, at least composed of
CC DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2,
CC STAU1, STAU2, SYNCRIP and YBX1. Identified in a mRNP granule complex,
CC at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1,
CC HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2,
CC ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X,
CC RPS8, RPS9, SYNCRIP, YBX1 and untranslated mRNAs. Component of the APOB
CC mRNA editosome. Interacts with APOBEC1 and A1CF. Part of a complex
CC associated with the FOS mCRD domain and consisting of PABPC1, PAIP1,
CC CSDE1/UNR, HNRPD and SYNCRIP. Interacts with HNRPR, SMN, POLR2A
CC hyperphosphorylated C-terminal domain, minute virus of mice (MVM) NS1
CC protein and through its C-terminal domain with SYT7, SYT8 and SYT9. The
CC non-phosphorylated and phosphorylated forms are colocalized with PAIP1
CC in polysomes. Interacts with GTPBP1 (By similarity). Interacts with
CC HABP4 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:O43390}. Cytoplasm
CC {ECO:0000250|UniProtKB:O43390}. Nucleus {ECO:0000250|UniProtKB:Q7TMK9}.
CC Microsome {ECO:0000250|UniProtKB:Q7TMK9}. Note=Localized in cytoplasmic
CC mRNP granules containing untranslated mRNAs (By similarity). Expressed
CC predominantly in the nucleoplasm. The tyrosine phosphorylated form
CC bound to RNA is found in microsomes (By similarity).
CC {ECO:0000250|UniProtKB:O43390, ECO:0000250|UniProtKB:Q7TMK9}.
CC -!- DOMAIN: The domain containing eight Arg-Gly-Gly repeats (RGG/RXR-box)
CC may be involved in RNA-binding and protein-protein interactions. It is
CC methylated by PRMT1, and essential for nuclear localization (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine. The membrane-bound form found in
CC microsomes is phosphorylated in vitro by insulin receptor tyrosine
CC kinase (INSR). Phosphorylation is inhibited upon binding to RNA,
CC whereas the cytoplasmic form is poorly phosphorylated.
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DR EMBL; AY325202; AAP92603.1; -; mRNA.
DR RefSeq; NP_001041381.1; NM_001047916.2.
DR AlphaFoldDB; Q7TP47; -.
DR SMR; Q7TP47; -.
DR BioGRID; 263972; 3.
DR IntAct; Q7TP47; 3.
DR MINT; Q7TP47; -.
DR STRING; 10116.ENSRNOP00000048433; -.
DR iPTMnet; Q7TP47; -.
DR PhosphoSitePlus; Q7TP47; -.
DR jPOST; Q7TP47; -.
DR PaxDb; Q7TP47; -.
DR PRIDE; Q7TP47; -.
DR Ensembl; ENSRNOT00000041655; ENSRNOP00000048433; ENSRNOG00000000204.
DR GeneID; 363113; -.
DR KEGG; rno:363113; -.
DR UCSC; RGD:1305683; rat.
DR CTD; 10492; -.
DR RGD; 1305683; Syncrip.
DR eggNOG; KOG0117; Eukaryota.
DR GeneTree; ENSGT00940000153511; -.
DR InParanoid; Q7TP47; -.
DR OrthoDB; 1384330at2759; -.
DR PRO; PR:Q7TP47; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000000204; Expressed in thymus and 18 other tissues.
DR ExpressionAtlas; Q7TP47; baseline and differential.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD.
DR GO; GO:0070937; C:CRD-mediated mRNA stability complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0097452; C:GAIT complex; ISO:RGD.
DR GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; ISS:UniProtKB.
DR GO; GO:0106002; C:mCRD-mediated mRNA stability complex; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:1990635; C:proximal dendrite; IDA:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:RGD.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:RGD.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0008143; F:poly(A) binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:RGD.
DR GO; GO:0007623; P:circadian rhythm; IEP:RGD.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; ISO:RGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0090367; P:negative regulation of mRNA modification; IMP:RGD.
DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISO:RGD.
DR GO; GO:0017148; P:negative regulation of translation; ISO:RGD.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; ISO:RGD.
DR GO; GO:0045727; P:positive regulation of translation; IMP:RGD.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12483; RRM1_hnRNPQ; 1.
DR CDD; cd12489; RRM2_hnRNPQ; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR006535; HnRNP_R/Q_splicing_fac.
DR InterPro; IPR034544; hnRNPQ_RRM1.
DR InterPro; IPR034548; hnRNPQ_RRM2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 3.
DR TIGRFAMs; TIGR01648; hnRNP-R-Q; 1.
DR PROSITE; PS50102; RRM; 3.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Endoplasmic reticulum; Isopeptide bond;
KW Methylation; Microsome; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Spliceosome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT CHAIN 2..533
FT /note="Heterogeneous nuclear ribonucleoprotein Q"
FT /id="PRO_0000081869"
FT DOMAIN 72..151
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 153..235
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 248..318
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 358..360
FT /note="1-1"
FT REPEAT 361..363
FT /note="1-2"
FT REPEAT 370..374
FT /note="2-1"
FT REPEAT 379..382
FT /note="2-2"
FT REPEAT 388..390
FT /note="1-3"
FT REPEAT 395..398
FT /note="2-3"
FT REPEAT 408..410
FT /note="1-4"
FT REPEAT 436..438
FT /note="1-5"
FT REPEAT 449..451
FT /note="1-6"
FT REPEAT 464..466
FT /note="1-7"
FT REPEAT 467..469
FT /note="1-8"
FT REGION 310..471
FT /note="Interaction with APOBEC1"
FT /evidence="ECO:0000250"
FT REGION 358..469
FT /note="8 X 3 AA repeats of R-G-G"
FT REGION 370..398
FT /note="3 X 4 AA repeats of Y-Y-G-Y"
FT REGION 407..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..459
FT /note="Interaction with SMN"
FT /evidence="ECO:0000250"
FT MOTIF 474..488
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 484..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 131
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 273
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 283
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 354
FT /note="Asymmetric dimethylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 354
FT /note="Omega-N-methylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 406
FT /note="Omega-N-methylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 420
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 428
FT /note="Asymmetric dimethylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 428
FT /note="Omega-N-methylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 436
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 436
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 446
FT /note="Asymmetric dimethylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 446
FT /note="Omega-N-methylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 449
FT /note="Asymmetric dimethylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 449
FT /note="Omega-N-methylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT CROSSLNK 78
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60506"
FT CROSSLNK 517
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60506"
SQ SEQUENCE 533 AA; 59710 MW; EC218ECF4FC00FBF CRC64;
MATEHVNGNG TEEPMDTTSA VIHSENFQTL LDAGLPQKVA EKLDEIYVAG QRKYGGPPPD
SVYSGQQPSV GTEIFVGKIP RDLFEDELVP LFEKAGPIWD LRLMMDPLTG LNRGYAFVTF
CTKEAAQEAV KLYNNHEIRS GKHIGVCISV ANNRLFVGSI PKSKTKEQIL EEFSKVTEGL
TDVILYHQPD DKKKNRGFCF LEYEDHKTAA QARRRLMSGK VKVWGNVGTV EWADPIEDPD
PEVMAKVKVL FVRNLANTVT EEILEKSFSQ FGKLERVKKL KDYAFIHFDE RDGAVKAMEE
MNGKDLEGEN IEIVFAKPPD QKRKERKAQR QAAKNQMYDD YYYYGPPHMP PPTRGRGRGG
RGGYGYPPDY YGYEDYYDYY GYDYHNYRGG YEDPYYGYED FQVGARGRGG RGARGAAPSR
GRGAAPPRGR AGYSQRGGPG SARGVRGARG GAQQQRGRGV RGARGGRGGN VGGKRKADGY
NQPDSKRRQT NNQNWGSQPI AQQPLQGGDH SGNYGYKSEN EEFYQDTFGQ QWK
