SF3B3_BOVIN
ID SF3B3_BOVIN Reviewed; 1217 AA.
AC A0JN52;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Splicing factor 3B subunit 3;
DE AltName: Full=Pre-mRNA-splicing factor SF3b 130 kDa subunit;
DE Short=SF3b130;
DE AltName: Full=Spliceosome-associated protein 130;
DE Short=SAP 130;
GN Name=SF3B3;
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=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in pre-mRNA splicing as a component of the splicing
CC factor SF3B complex, a constituent of the spliceosome. SF3B complex is
CC required for 'A' complex assembly formed by the stable binding of U2
CC snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence
CC independent binding of SF3A/SF3B complex upstream of the branch site is
CC essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved
CC in the assembly of the 'E' complex. Belongs also to the minor U12-
CC dependent spliceosome, which is involved in the splicing of rare class
CC of nuclear pre-mRNA intron. {ECO:0000250|UniProtKB:Q15393}.
CC -!- SUBUNIT: Identified in the spliceosome A complex; remains associated
CC with the spliceosome throughout the splicing process. Component of the
CC spliceosome B complex. Identified in the spliceosome C complex.
CC Identified in the spliceosome E complex. Component of the U11/U12
CC snRNPs that are part of the U12-type spliceosome. Component of splicing
CC factor SF3B complex which is composed of at least eight subunits;
CC SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6, PHF5A and DDX42. SF3B
CC associates with the splicing factor SF3A and a 12S RNA unit to form the
CC U2 small nuclear ribonucleoproteins complex (U2 snRNP). Interaction
CC between SF3B3 and SF3B1 is tighter than the interaction between SF3B3
CC and SF3B2. Within the SF3B complex interacts directly with SF3B1 (via
CC HEAT domain), SF3B5 and PHF5A. The SF3B complex composed of SF3B1,
CC SF3B2, SF3B3, SF3B4, SF3B5, SF3B6 and PHF5A interacts with U2AF2.
CC Associates with the STAGA transcription coactivator-HAT complex.
CC Interacts with SUPT3H. Interacts with TAF3.
CC {ECO:0000250|UniProtKB:Q15393}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15393}.
CC -!- DOMAIN: The core of the protein consists of three beta-propeller
CC domains. {ECO:0000250|UniProtKB:Q15393}.
CC -!- SIMILARITY: Belongs to the RSE1 family. {ECO:0000305}.
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DR EMBL; BC126518; AAI26519.1; -; mRNA.
DR RefSeq; NP_001071319.1; NM_001077851.1.
DR AlphaFoldDB; A0JN52; -.
DR SMR; A0JN52; -.
DR STRING; 9913.ENSBTAP00000014050; -.
DR PaxDb; A0JN52; -.
DR PeptideAtlas; A0JN52; -.
DR PRIDE; A0JN52; -.
DR Ensembl; ENSBTAT00000014050; ENSBTAP00000014050; ENSBTAG00000010627.
DR GeneID; 504962; -.
DR KEGG; bta:504962; -.
DR CTD; 23450; -.
DR VEuPathDB; HostDB:ENSBTAG00000010627; -.
DR VGNC; VGNC:34511; SF3B3.
DR eggNOG; KOG1898; Eukaryota.
DR GeneTree; ENSGT00950000183151; -.
DR HOGENOM; CLU_003246_0_0_1; -.
DR InParanoid; A0JN52; -.
DR OMA; FFLVQTE; -.
DR OrthoDB; 97116at2759; -.
DR TreeFam; TF105685; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000010627; Expressed in ileum and 106 other tissues.
DR ExpressionAtlas; A0JN52; baseline and differential.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005689; C:U12-type spliceosomal complex; IEA:Ensembl.
DR GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0030620; F:U2 snRNA binding; IBA:GO_Central.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IEA:Ensembl.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF03178; CPSF_A; 1.
DR Pfam; PF10433; MMS1_N; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 2: Evidence at transcript level;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Spliceosome.
FT CHAIN 1..1217
FT /note="Splicing factor 3B subunit 3"
FT /id="PRO_0000276754"
FT REGION 105..119
FT /note="Interaction with PHF5A, SF3B1 and SF3B5"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT REGION 145..168
FT /note="Interaction with PHF5A, SF3B1 and SF3B5"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT REGION 193..231
FT /note="Interaction with SF3B1 and SF3B5"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT REGION 786..804
FT /note="Interaction with SF3B1 and SF3B5"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT REGION 1028..1049
FT /note="Interaction with SF3B1"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT REGION 1100..1123
FT /note="Interaction with SF3B5"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT SITE 284
FT /note="Interaction with SF3B5"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT SITE 306
FT /note="Interaction with SF3B5"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT SITE 352
FT /note="Interaction with SF3B5"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT SITE 429
FT /note="Interaction with SF3B5"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT SITE 916
FT /note="Interaction with SF3B5"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT SITE 988
FT /note="Interaction with SF3B1"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT SITE 1171
FT /note="Interaction with SF3B1"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT MOD_RES 1200
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
SQ SEQUENCE 1217 AA; 135577 MW; 35CACAF5ACC32512 CRC64;
MFLYNLTLQR ATGISFAIHG NFSGTKQQEI VVSRGKILEL LRPDPNTGKV HTLLTVEVFG
VIRSLMAFRL TGGTKDYIVV GSDSGRIVIL EYQPSKNMFE KIHQETFGKS GCRRIVPGQF
LAVDPKGRAV MISAIEKQKL VYILNRDAAA RLTISSPLEA HKANTLVYHV VGVDVGFENP
MFACLEMDYE EADNDPTGEA AANTQQTLTF YELDLGLNHV VRKYSEPLEE HGNFLITVPG
GSDGPSGVLI CSENYITYKN FGDQPDIRCP IPRRRNDLDD PERGMIFVCS ATHKTKSMFF
FLAQTEQGDI FKITLETDED MVTEIRLKYF DTVPVAAAMC VLKTGFLFVA SEFGNHYLYQ
IAHLGDDDEE PEFSSAMPLE EGDTFFFQPR PLKNLVLVDE LDSLSPILFC QIADLANEDT
PQLYVACGRG PRSSLRVLRH GLEVSEMAVS ELPGNPNAVW TVRRHIEDEF DAYIIVSFVN
ATLVLSIGET VEEVTDSGFL GTTPTLSCSL LGDDALVQVY PDGIRHIRAD KRVNEWKTPG
KKTIVKCAVN QRQVVIALTG GELVYFEMDP SGQLNEYTER KEMSADVVCM SLANVPPGEQ
RSRFLAVGLV DNTVRIISLD PSDCLQPLSM QALPAQPESL CIVEMGGTEK QDELGERGSI
GFLYLNIGLQ NGVLLRTVLD PVTGDLSDTR TRYLGSRPVK LFRVRMQGQE AVLAMSSRSW
LSYSYQSRFH LTPLSYETLE FASGFASEQC PEGIVAISTN TLRILALEKL GAVFNQVAFP
LQYTPRKFVI HPESNNLIII ETDHNAYTEA TKAQRKQQMA EEMVEAAGED ERELAAEMAA
AFLNENLPES IFGAPKAGNG QWASVIRVMN PIQGNTLDLV QLEQNEAAFS VAVCRFSNTG
EDWYVLVGVA KDLILNPRSV AGGFVYTYKL VNNGEKLEFL HKTPVEEVPA AIAPFQGRVL
IGVGKLLRVY DLGKKKLLRK CENKHIANYI SGIQTIGHRV IVSDVQESFI WVRYKRNENQ
LIIFADDTYP RWVTTASLLD YDTVAGADKF GNICVVRLPP NTNDEVDEDP TGNKALWDRG
LLNGASQKAE VIMNYHVGET VLSLQKTTLI PGGSESLVYT TLSGGIGILV PFTSHEDHDF
FQHVEMHLRS EHPPLCGRDH LSFRSYYFPV KNVIDGDLCE QFNSMEPNKQ KNVSEELDRT
PPEVSKKLED IRTRYAF
