SART3_PONAB
ID SART3_PONAB Reviewed; 981 AA.
AC Q5REG1;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Squamous cell carcinoma antigen recognized by T-cells 3 {ECO:0000305};
DE Short=SART-3 {ECO:0000305};
GN Name=SART3 {ECO:0000305};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: U6 snRNP-binding protein that functions as a recycling factor
CC of the splicing machinery. Promotes the initial reassembly of U4 and U6
CC snRNPs following their ejection from the spliceosome during its
CC maturation. Also binds U6atac snRNPs and may function as a recycling
CC factor for U4atac/U6atac spliceosomal snRNP, an initial step in the
CC assembly of U12-type spliceosomal complex. The U12-type spliceosomal
CC complex plays a role in the splicing of introns with non-canonical
CC splice sites. May also function as a substrate-targeting factor for
CC deubiquitinases like USP4 and USP15. Recruits USP4 to ubiquitinated
CC PRPF3 within the U4/U5/U6 tri-snRNP complex, promoting PRPF3
CC deubiquitination and thereby regulating the spliceosome U4/U5/U6 tri-
CC snRNP spliceosomal complex disassembly. May also recruit the
CC deubiquitinase USP15 to histone H2B and mediate histone
CC deubiquitination, thereby regulating gene expression and/or DNA repair.
CC May play a role in hematopoiesis probably through transcription
CC regulation of specific genes including MYC.
CC {ECO:0000250|UniProtKB:Q15020, ECO:0000250|UniProtKB:Q9JLI8}.
CC -!- SUBUNIT: Component of the 7SK snRNP complex at least composed of P-TEFb
CC (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2, BCDIN3, SART3
CC proteins and 7SK and U6 snRNAs. Interacts with AGO1 and AGO2. Interacts
CC with PRPF3 and USP4; the interaction with PRPF3 is direct and recruits
CC USP4 to its substrate PRPF3. Interacts with USP15; the interaction is
CC direct. {ECO:0000250|UniProtKB:Q15020}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q15020}. Nucleus, Cajal body
CC {ECO:0000250|UniProtKB:Q15020}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q15020}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q15020}.
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DR EMBL; CR857568; CAH89846.1; -; mRNA.
DR RefSeq; NP_001124858.1; NM_001131386.1.
DR AlphaFoldDB; Q5REG1; -.
DR SMR; Q5REG1; -.
DR STRING; 9601.ENSPPYP00000005611; -.
DR GeneID; 100171719; -.
DR KEGG; pon:100171719; -.
DR CTD; 9733; -.
DR eggNOG; KOG0128; Eukaryota.
DR InParanoid; Q5REG1; -.
DR OrthoDB; 867827at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0017070; F:U6 snRNA binding; ISS:UniProtKB.
DR GO; GO:0030624; F:U6atac snRNA binding; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
DR GO; GO:1903586; P:positive regulation of histone deubiquitination; ISS:UniProtKB.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; ISS:UniProtKB.
DR CDD; cd12391; RRM1_SART3; 1.
DR CDD; cd12392; RRM2_SART3; 1.
DR Gene3D; 1.25.40.10; -; 2.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR008669; LSM_interact.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034217; SART3_RRM1.
DR InterPro; IPR034218; SART3_RRM2.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF05391; Lsm_interact; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00386; HAT; 7.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Cytoplasm; Methylation; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT CHAIN 2..981
FT /note="Squamous cell carcinoma antigen recognized by T-
FT cells 3"
FT /id="PRO_0000223315"
FT REPEAT 126..158
FT /note="HAT 1"
FT REPEAT 164..195
FT /note="HAT 2"
FT REPEAT 201..237
FT /note="HAT 3"
FT REPEAT 260..293
FT /note="HAT 4"
FT REPEAT 342..374
FT /note="HAT 5"
FT REPEAT 377..409
FT /note="HAT 6"
FT REPEAT 412..448
FT /note="HAT 7"
FT REPEAT 505..538
FT /note="HAT 8"
FT DOMAIN 722..800
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 819..896
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..369
FT /note="Mediates interaction with PRPF3"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT REGION 49..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..538
FT /note="Required for interaction with USP4"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT REGION 555..971
FT /note="Necessary and sufficient for U6 snRNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT REGION 608..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..688
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT REGION 895..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 21..46
FT /evidence="ECO:0000255"
FT COILED 82..110
FT /evidence="ECO:0000255"
FT COILED 577..637
FT /evidence="ECO:0000255"
FT COMPBIAS 16..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..712
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:Q15020"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT MOD_RES 675
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT MOD_RES 813
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT MOD_RES 870
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT MOD_RES 924
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
SQ SEQUENCE 981 AA; 111861 MW; 387400B61AA11ED1 CRC64;
MATAAATSAS EPEAESKAGP KADGEEDEVK AARTRRKVLS RAVAAATYKT MGPGWDQQEE
GVSESDGDEY AMASSAESSP GEYEWEYDEE EEKNQLEIER LEEQLSINVY DYNCHVDLIR
LLRLEGELTK VRMARQKMSE IFPLTEELWL EWLHDEISMA QDGLDREHVY DLFEKAVKDY
ICPNIWLEYG QYSVGGIGQK GGLEKVRSVF ERALSSVGLH MTKGLALWEA YREFESAIVE
AARPVAGFLS PFDREQTFDS QLEKVHSLFR RQLAIPLYDM EATFAEYEEW SEDPIPESVI
QNYNKALQQL EKYKPYEEAL LQAEAPRLAE YQAYIDFEMK IGDPARIQLI FERALVENCL
VPDLWIRYSQ YLDRQLKVKD LVLSVHNRAI RNCPWTVALW SRYLLAMERH GVDHQVISVT
FEKALNAGFI QATDYVEIWQ AYLDYLRRRV DFKQDSSKEL EELRAAFTRA LEYLKQEVEE
RFNESGDPSC VIMQNWARIE ARLCNNMQKA RELWDSIMTR GNAKYANMWL EYYNLERAHG
DTQHCRKALH RAVQCTSDYP EHVCEVLLTM ERTEGSLEDW DIAVQKTETR LARVNEQRMK
AAEKEAALVQ QEEEKAEQRK RARAEKKALK KKKKIRGPEK RGADEDDEKE WGDDEEEQPS
KRRRVENSIP AAGETQNVEV APGPAGKCAA VDVEPPSKQK EKAASLKRDM PKVLHDSSKD
SITVFVSNLP YSMQEPDAKL RPLFEACGEV VQIRPIFSNR GDFRGYRYVE FKEEKSALQA
LEMDRKSVEG RPMFVSPCVD KSKNPDFKVF RYSTSLEKHK LFISGLPFSC TKEELEEICK
AHGTVKDLRL VTNRAGKPKG LAYVEYENES QASQAVMKMD GMTIKENVIK VAISNPPQRK
VPEKPETRKA PGGPTLLPQT YGARGKGRTQ LSLLPRALQR PGAAAPQAEN GPAAAPAVAA
PAATEAPKMS NADFAKLFLR K
