ID A0A1S3GHN3_DIPOR Unreviewed; 562 AA.
AC A0A1S3GHN3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Heterogeneous nuclear ribonucleoprotein Q isoform X2 {ECO:0000313|RefSeq:XP_012888316.1};
GN Name=Syncrip {ECO:0000313|RefSeq:XP_012888316.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012888316.1};
RN [1] {ECO:0000313|RefSeq:XP_012888316.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012888316.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR RefSeq; XP_012888316.1; XM_013032862.1.
DR AlphaFoldDB; A0A1S3GHN3; -.
DR SMR; A0A1S3GHN3; -.
DR STRING; 10020.ENSDORP00000020342; -.
DR GeneID; 105998211; -.
DR CTD; 10492; -.
DR OrthoDB; 3184171at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IEA:Ensembl.
DR GO; GO:0070937; C:CRD-mediated mRNA stability complex; IEA:Ensembl.
DR GO; GO:0097452; C:GAIT complex; IEA:Ensembl.
DR GO; GO:0106002; C:mCRD-mediated mRNA stability complex; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0071346; P:cellular response to type II interferon; IEA:Ensembl.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; IEA:Ensembl.
DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IEA:Ensembl.
DR GO; GO:0017148; P:negative regulation of translation; IEA:Ensembl.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IEA:Ensembl.
DR CDD; cd21066; NURR_hnRNPQ; 1.
DR CDD; cd12483; RRM1_hnRNPQ; 1.
DR CDD; cd12489; RRM2_hnRNPQ; 1.
DR CDD; cd12495; RRM3_hnRNPQ; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR041337; hnRNP_Q_AcD.
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 NCBIfam; TIGR01648; hnRNP-R-Q; 1.
DR PANTHER; PTHR21245; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; 1.
DR PANTHER; PTHR21245:SF11; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN Q; 1.
DR Pfam; PF18360; hnRNP_Q_AcD; 1.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 3.
DR PROSITE; PS50102; RRM; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Ribonucleoprotein {ECO:0000313|RefSeq:XP_012888316.1};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 162..241
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 243..325
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 338..408
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 497..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 562 AA; 62656 MW; 32F5C37178197E45 CRC64;
MATEHVNGNG TEEPMDTTSA VIHSENFQTL LDAGLPQKVA EKLDEIYVAG LVAHSDLDER
AIEALKEFNE DGALAVLQQF KDSDLSHVQN KSAFLCGVMK TYRQREKQGT KVADSSKGPD
EAKIKALLER TGYTLDVTTG QRKYGGPPPD SVYSGQQPSV GTEIFVGKIP RDLFEDELVP
LFEKAGPIWD LRLMMDPLTG LNRGYAFVTF CTKEAAQEAV KLYNNHEIRS GKHIGVCISV
ANNRLFVGSI PKSKTKEQIL EEFSKVTEGL TDVILYHQPD DKKKNRGFCF LEYEDHKTAA
QARRRLMSGK VKVWGNVGTV EWADPIEDPD PEVMAKVKVL FVRNLANTVT EEILEKAFSQ
FGKLERVKKL KDYAFIHFDE RDGAVKAMEE MNGKDLEGEN IEIVFAKPPD QKRKERKAQR
QAAKNQMYDD YYYYGPPHMP PPTRGRGRGG RGGYGYPPDY YGYEDYYDYY GYDYHNYRGG
YEDPYYGYED FQVGARGRGG RGARGAAPSR GRGAAPPRGR AGYSQRGGPG SARGVRGARG
GAQQQRGRGQ GKGVEAGPDL LQ
//
