CSTF2_PONAB
ID CSTF2_PONAB Reviewed; 577 AA.
AC Q5RDA3;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Cleavage stimulation factor subunit 2;
DE AltName: Full=CF-1 64 kDa subunit;
DE AltName: Full=Cleavage stimulation factor 64 kDa subunit;
DE Short=CSTF 64 kDa subunit;
DE Short=CstF-64;
GN Name=CSTF2;
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: One of the multiple factors required for polyadenylation and
CC 3'-end cleavage of mammalian pre-mRNAs. This subunit is directly
CC involved in the binding to pre-mRNAs (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The CSTF complex is composed of CSTF1 (50 kDa subunit), CSTF2
CC (64 kDa subunit) and CSTF3 (77 kDa subunit). CSTF2 directly interacts
CC with CSTF3, SYMPK and RPO2TC1. Interacts with HSF1 in heat-stressed
CC cells (By similarity). Interacts with CPSF2, CPSF3 and FIP1L1.
CC Interacts with DDX1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Localized with DDX1
CC in cleavage bodies. {ECO:0000250}.
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DR EMBL; CR858012; CAH90254.1; -; mRNA.
DR RefSeq; NP_001125111.1; NM_001131639.2.
DR AlphaFoldDB; Q5RDA3; -.
DR BMRB; Q5RDA3; -.
DR SMR; Q5RDA3; -.
DR STRING; 9601.ENSPPYP00000022995; -.
DR PRIDE; Q5RDA3; -.
DR GeneID; 100171993; -.
DR KEGG; pon:100171993; -.
DR CTD; 1478; -.
DR eggNOG; KOG0108; Eukaryota.
DR InParanoid; Q5RDA3; -.
DR OrthoDB; 1455080at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0071920; C:cleavage body; ISS:UniProtKB.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006378; P:mRNA polyadenylation; IEA:InterPro.
DR Gene3D; 1.10.20.70; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR033105; CSTF2.
DR InterPro; IPR025742; CSTF2_hinge.
DR InterPro; IPR026896; CSTF_C.
DR InterPro; IPR038192; CSTF_C_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR45735:SF6; PTHR45735:SF6; 1.
DR Pfam; PF14327; CSTF2_hinge; 1.
DR Pfam; PF14304; CSTF_C; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW Isopeptide bond; Methylation; mRNA processing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Ubl conjugation.
FT CHAIN 1..577
FT /note="Cleavage stimulation factor subunit 2"
FT /id="PRO_0000081533"
FT DOMAIN 16..94
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 410..414
FT /note="1; approximate"
FT REPEAT 415..419
FT /note="2"
FT REPEAT 420..424
FT /note="3"
FT REPEAT 425..429
FT /note="4; approximate"
FT REPEAT 430..434
FT /note="5; approximate"
FT REPEAT 435..439
FT /note="6"
FT REPEAT 440..444
FT /note="7"
FT REPEAT 445..449
FT /note="8"
FT REPEAT 450..454
FT /note="9"
FT REPEAT 455..459
FT /note="10; approximate"
FT REPEAT 460..464
FT /note="11"
FT REPEAT 465..469
FT /note="12; approximate"
FT REGION 108..248
FT /note="Interactions with CSTF3 and SYMPK"
FT /evidence="ECO:0000250"
FT REGION 207..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..469
FT /note="12 X 5 AA tandem repeats of M-E-A-R-[AG]"
FT REGION 509..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..577
FT /note="Interaction with RPO2TC1"
FT /evidence="ECO:0000250"
FT COMPBIAS 211..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..385
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33240"
FT MOD_RES 308
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P33240"
FT MOD_RES 468
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P33240"
FT MOD_RES 475
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P33240"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33240"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33240"
FT CROSSLNK 189
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P33240"
SQ SEQUENCE 577 AA; 60923 MW; 428F2FFDBDE8DAA8 CRC64;
MAGLTVRDPA VDRSLRSVFV GNIPYEATEE QLKDIFSEVG PVVSFRLVYD RETGKPKGYG
FCEYQDQETA LSAMRNLNGR EFSGRALRVD NAASEKNKEE LKSLGTGAPV IESPYGETIS
PEDAPESISK AVASLPPEQM FELMKQMKLC VQNSPQEARN MLLQNPQLAY ALLQAQVVMR
IVDPEIALKI LHRQTNIPTL IAGNPQPVHG AGPGSGSNVS MNQQNPQAPQ AQSLGGMHVN
GAPPLMQASM QGGVPAPGQI PAAVTGPGPG SLAPGGGMQA QVGMPGSGPV SMERGQVPMQ
DPRAAMQRGS LPANVPTPRG LLGDAPNDPR GGTLLSVTGE VEPRGYLGPP HQGPPMHHVP
GHESRGPPPH ELRGGPLPEP RPLMAEPRGP MLDQRGPPLD GRGGRDPRGI DARGMEARAM
EARGLDARGL EARAMEARAM EARAMEARAM EARAMEVRGM EARGMDTRGP VPGPRGPIPS
GMQGPSPINM GAVVPQGSRQ VPVMQGTGLQ GASIQGGSQP GGFSPGQNQV TPQDHEKAAL
IMQVLQLTAD QIAMLPPEQR QSILILKEQI QKSTGAP
