CSTF3_PONAB
ID CSTF3_PONAB Reviewed; 717 AA.
AC Q5RDW9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 77.
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 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=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR857774; CAH90038.1; -; mRNA.
DR RefSeq; NP_001127228.1; NM_001133756.1.
DR AlphaFoldDB; Q5RDW9; -.
DR SMR; Q5RDW9; -.
DR STRING; 9601.ENSPPYP00000003876; -.
DR GeneID; 100174283; -.
DR KEGG; pon:100174283; -.
DR CTD; 1479; -.
DR eggNOG; KOG1914; Eukaryota.
DR InParanoid; Q5RDW9; -.
DR OrthoDB; 331411at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031124; P:mRNA 3'-end processing; IEA:InterPro.
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 2: Evidence at transcript level;
KW Acetylation; mRNA processing; Nucleus; Phosphoprotein; Reference proteome;
KW 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_0000205724"
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 684..705
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:0000250|UniProtKB:Q12996"
SQ SEQUENCE 717 AA; 82910 MW; A03C9D45466AE894 CRC64;
MSGDGATEQA AEYVPEKVKK AEKKLEENPY DLDAWSTLIR 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 AREDTRTRHH VYVTAALMEY
YCSKDKSVAF KIFELGLKKY GDIPEYVLAY IDYLSHLNED NNTRVLFERV LTSGSLPPEK
SGEIWARFLA FESNIGDLAS ILKVEKRRFT AFKEEYEGKE TALLVDRYKF MDLYPCSASE
LKALGYKDVS RAKLAAIIPD PVVAPSIVPV LKDEVDRKPE YPKPDTQQMI PFQPRHLAPP
GLHPVPGGVF PVPPAAVVLM KLLPPPICFQ GPFVQVDELM EIFRRCKIPN TVEEAVRIIT
GGAPELAVEG NGPVESNAVL TKAVKRPNED SDEDEEKGAV VPPVHDIYRA RQQKRIR