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SF3B3_PONAB
ID   SF3B3_PONAB             Reviewed;        1217 AA.
AC   Q5RBI5;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 67.
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   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: 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; CR858662; CAH90875.1; -; mRNA.
DR   RefSeq; NP_001125500.1; NM_001132028.1.
DR   AlphaFoldDB; Q5RBI5; -.
DR   SMR; Q5RBI5; -.
DR   STRING; 9601.ENSPPYP00000008511; -.
DR   GeneID; 100172409; -.
DR   KEGG; pon:100172409; -.
DR   CTD; 23450; -.
DR   eggNOG; KOG1898; Eukaryota.
DR   InParanoid; Q5RBI5; -.
DR   OrthoDB; 97116at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
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_0000276756"
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;  135504 MW;  8EF13748756F8839 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 GLEVSETAVS 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 IFGAPKAGSG QWASVIRVMN PIQGNTLDLV QLEQNEAAFS VAVCRFSNTG
     EDWYVLVGVA KDLILNPRSV AGGFVYTYKL VNNGEKLEFL HKTPVEEVPA AIAPFQGRVL
     IGVGKLLRVY DLGKKKLLRK CENKHIANYI SGIQTIGHRV IVSDVQESFI WVRYKRNENQ
     LIIFADDTYP RWVTTASLLD YDTVAGADKF GNICVVRLPP NTNDEVDEDP TGNKALRDRG
     LLNGASQKAE VIMNYHVGET VLSLQKTTLI PGGSESLVYT TLSGGIGILV PFTSHEDHDF
     FQHVEMHLRS EHPPLCGRDH LSFRSYYFPV KNVIDGDLCE QFNSMEPNKQ KNVSEELDRT
     PPEVTKKLED IRTRYAF
 
 
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