CSTF3_MOUSE
ID CSTF3_MOUSE Reviewed; 717 AA.
AC Q99LI7;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Cleavage stimulation factor subunit 3;
DE AltName: Full=CF-1 77 kDa subunit;
DE AltName: Full=Cleavage stimulation factor 77 kDa subunit;
DE Short=CSTF 77 kDa subunit;
DE Short=CstF-77;
GN Name=Cstf3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: One of the multiple factors required for polyadenylation and
CC 3'-end cleavage of mammalian pre-mRNAs. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. The CSTF complex is composed of CSTF1 (50 kDa
CC subunit), CSTF2 (64 kDa subunit) and CSTF3 (77 kDa subunit). CSTF3
CC directly interacts with CSTF1 and CSTF2. Interacts with FIP1L1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; BC003241; AAH03241.1; -; mRNA.
DR CCDS; CCDS16490.1; -.
DR RefSeq; NP_663504.1; NM_145529.3.
DR PDB; 2OND; X-ray; 2.80 A; A/B=242-549.
DR PDB; 2OOE; X-ray; 3.00 A; A=21-549.
DR PDBsum; 2OND; -.
DR PDBsum; 2OOE; -.
DR AlphaFoldDB; Q99LI7; -.
DR SMR; Q99LI7; -.
DR BioGRID; 230731; 3.
DR STRING; 10090.ENSMUSP00000028599; -.
DR iPTMnet; Q99LI7; -.
DR PhosphoSitePlus; Q99LI7; -.
DR EPD; Q99LI7; -.
DR jPOST; Q99LI7; -.
DR MaxQB; Q99LI7; -.
DR PaxDb; Q99LI7; -.
DR PeptideAtlas; Q99LI7; -.
DR PRIDE; Q99LI7; -.
DR ProteomicsDB; 285383; -.
DR Antibodypedia; 25689; 222 antibodies from 28 providers.
DR DNASU; 228410; -.
DR Ensembl; ENSMUST00000028599; ENSMUSP00000028599; ENSMUSG00000027176.
DR GeneID; 228410; -.
DR KEGG; mmu:228410; -.
DR UCSC; uc008ljz.2; mouse.
DR CTD; 1479; -.
DR MGI; MGI:1351825; Cstf3.
DR VEuPathDB; HostDB:ENSMUSG00000027176; -.
DR eggNOG; KOG1914; Eukaryota.
DR GeneTree; ENSGT00390000006758; -.
DR HOGENOM; CLU_007630_3_1_1; -.
DR InParanoid; Q99LI7; -.
DR OMA; LCYIDYL; -.
DR OrthoDB; 331411at2759; -.
DR PhylomeDB; Q99LI7; -.
DR TreeFam; TF105867; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72187; mRNA 3'-end processing.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-MMU-77595; Processing of Intronless Pre-mRNAs.
DR BioGRID-ORCS; 228410; 26 hits in 77 CRISPR screens.
DR ChiTaRS; Cstf3; mouse.
DR EvolutionaryTrace; Q99LI7; -.
DR PRO; PR:Q99LI7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q99LI7; protein.
DR Bgee; ENSMUSG00000027176; Expressed in primitive streak and 267 other tissues.
DR Genevisible; Q99LI7; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0031124; P:mRNA 3'-end processing; IEA:InterPro.
DR GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR045243; Rna14-like.
DR InterPro; IPR008847; Suf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR19980; PTHR19980; 1.
DR Pfam; PF05843; Suf; 1.
DR SMART; SM00386; HAT; 10.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; mRNA processing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q12996"
FT CHAIN 2..717
FT /note="Cleavage stimulation factor subunit 3"
FT /id="PRO_0000205723"
FT REPEAT 45..77
FT /note="HAT 1"
FT REPEAT 79..110
FT /note="HAT 2"
FT REPEAT 117..152
FT /note="HAT 3"
FT REPEAT 163..196
FT /note="HAT 4"
FT REPEAT 221..261
FT /note="HAT 5"
FT REPEAT 271..303
FT /note="HAT 6"
FT REPEAT 319..352
FT /note="HAT 7"
FT REPEAT 354..387
FT /note="HAT 8"
FT REPEAT 458..494
FT /note="HAT 9"
FT REGION 683..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q12996"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT HELIX 21..27
FT /evidence="ECO:0007829|PDB:2OOE"
FT HELIX 32..43
FT /evidence="ECO:0007829|PDB:2OOE"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:2OOE"
FT HELIX 65..77
FT /evidence="ECO:0007829|PDB:2OOE"
FT HELIX 81..91
FT /evidence="ECO:0007829|PDB:2OOE"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:2OOE"
FT HELIX 98..111
FT /evidence="ECO:0007829|PDB:2OOE"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:2OOE"
FT HELIX 118..132
FT /evidence="ECO:0007829|PDB:2OOE"
FT HELIX 140..152
FT /evidence="ECO:0007829|PDB:2OOE"
FT HELIX 161..175
FT /evidence="ECO:0007829|PDB:2OOE"
FT HELIX 183..197
FT /evidence="ECO:0007829|PDB:2OOE"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:2OOE"
FT HELIX 210..229
FT /evidence="ECO:0007829|PDB:2OOE"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:2OOE"
FT HELIX 243..260
FT /evidence="ECO:0007829|PDB:2OND"
FT HELIX 269..287
FT /evidence="ECO:0007829|PDB:2OND"
FT HELIX 291..310
FT /evidence="ECO:0007829|PDB:2OND"
FT HELIX 315..332
FT /evidence="ECO:0007829|PDB:2OND"
FT TURN 333..338
FT /evidence="ECO:0007829|PDB:2OND"
FT HELIX 340..352
FT /evidence="ECO:0007829|PDB:2OND"
FT HELIX 356..367
FT /evidence="ECO:0007829|PDB:2OND"
FT STRAND 369..372
FT /evidence="ECO:0007829|PDB:2OND"
FT HELIX 375..389
FT /evidence="ECO:0007829|PDB:2OND"
FT HELIX 391..402
FT /evidence="ECO:0007829|PDB:2OND"
FT HELIX 410..421
FT /evidence="ECO:0007829|PDB:2OND"
FT HELIX 426..440
FT /evidence="ECO:0007829|PDB:2OND"
FT HELIX 444..455
FT /evidence="ECO:0007829|PDB:2OND"
FT HELIX 460..472
FT /evidence="ECO:0007829|PDB:2OND"
FT STRAND 473..476
FT /evidence="ECO:0007829|PDB:2OND"
FT HELIX 478..480
FT /evidence="ECO:0007829|PDB:2OND"
FT HELIX 482..495
FT /evidence="ECO:0007829|PDB:2OND"
FT HELIX 498..511
FT /evidence="ECO:0007829|PDB:2OND"
FT TURN 512..516
FT /evidence="ECO:0007829|PDB:2OND"
FT HELIX 520..525
FT /evidence="ECO:0007829|PDB:2OND"
FT TURN 526..528
FT /evidence="ECO:0007829|PDB:2OND"
FT HELIX 538..542
FT /evidence="ECO:0007829|PDB:2OND"
FT TURN 543..545
FT /evidence="ECO:0007829|PDB:2OND"
SQ SEQUENCE 717 AA; 82877 MW; 40CF9CC39D496645 CRC64;
MSGDAAAEQA AEYVPEKVKK AEKKLEENPY DLDAWSILIR EAQNQPIDKA RKTYERLVAQ
FPSSGRFWKL YIEAEIKAKN YDKVEKLFQR CLMKVLHIDL WKCYLSYVRE TKGKLPSYKE
KMAQAYDFAL DKIGMEIMSY QIWVDYINFL KGVEAVGSYA ENQRITAVRR VYQRGCVNPM
INIEQLWRDY NKYEEGINIH LAKKMIEDRS RDYMNARRVA KEYETVMKGL DRNAPSVPPQ
NTPQEAQQVD MWKKYIQWEK SNPLRTEDQT LITKRVMFAY EQCLLVLGHH PDIWYEAAQY
LEQSSKLLAE KGDMNNAKLF SDEAANIYER AISTLLKKNM LLYFAYADYE ESRMKYEKVH
SIYNRLLAIE DIDPTLVYIQ YMKFARRAEG IKSGRMIFKK AREDARTRHH VYVTAALMEY
YCSKDKSVAF KIFELGLKKY GDIPEYVLAY IDYLSHLNED NNTRVLFERV LTSGSLPPEK
SGEIWARFLA FESNIGDLAS ILKVEKRRFT AFREEYEGKE TALLVDRYKF MDLYPCSASE
LKALGYKDVS RAKLAAIIPD PVVAPSIVPV LKDEVDRKPE YPKPDTQQMI PFQPRHLAPP
GLHPVPGGVF PVPPAAVVLM KLLPPPICFQ GPFVQVDELM EIFRRCKIPN TVEEAVRIIT
GGAPELAVEG NGPVESSAVL TKAVKRPNED SDEDEEKGAV VPPVHDIYRA RQQKRIR
