CSTF2_BOVIN
ID CSTF2_BOVIN Reviewed; 572 AA.
AC Q8HXM1;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 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 [MRNA].
RX PubMed=12408968; DOI=10.1006/geno.2002.6862;
RA Dass B., McDaniel L., Schultz R.A., Attaya E., MacDonald C.C.;
RT "The gene CSTF2T, encoding the human variant CstF-64 polyadenylation
RT protein CstF-64, lacks introns and may be associated with male sterility.";
RL Genomics 80:509-514(2002).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY130297; AAN05427.1; -; mRNA.
DR RefSeq; NP_777110.1; NM_174685.2.
DR AlphaFoldDB; Q8HXM1; -.
DR BMRB; Q8HXM1; -.
DR SMR; Q8HXM1; -.
DR PaxDb; Q8HXM1; -.
DR PeptideAtlas; Q8HXM1; -.
DR PRIDE; Q8HXM1; -.
DR Ensembl; ENSBTAT00000004619; ENSBTAP00000004619; ENSBTAG00000003547.
DR GeneID; 282588; -.
DR KEGG; bta:282588; -.
DR CTD; 1478; -.
DR VEuPathDB; HostDB:ENSBTAG00000003547; -.
DR VGNC; VGNC:27781; CSTF2.
DR eggNOG; KOG0108; Eukaryota.
DR GeneTree; ENSGT00940000158987; -.
DR HOGENOM; CLU_028601_3_1_1; -.
DR InParanoid; Q8HXM1; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000003547; Expressed in conceptus and 106 other tissues.
DR ExpressionAtlas; Q8HXM1; baseline and differential.
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:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0006378; P:mRNA polyadenylation; IEA:InterPro.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IBA:GO_Central.
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..572
FT /note="Cleavage stimulation factor subunit 2"
FT /id="PRO_0000081530"
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; approximate"
FT REPEAT 425..429
FT /note="4; approximate"
FT REPEAT 430..434
FT /note="5"
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; approximate"
FT REPEAT 455..459
FT /note="10"
FT REPEAT 460..464
FT /note="11; approximate"
FT REGION 108..248
FT /note="Interactions with CSTF3 and SYMPK"
FT /evidence="ECO:0000250"
FT REGION 208..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..464
FT /note="11 X 5 AA tandem repeats of M-E-A-R-[AG]"
FT REGION 509..572
FT /note="Interaction with RPO2TC1"
FT /evidence="ECO:0000250"
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 463
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P33240"
FT MOD_RES 470
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P33240"
FT MOD_RES 519
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 572 AA; 60438 MW; 809140409D380209 CRC64;
MAGLTVRDPA VDRSLRSVFV GNIPYEATEE QLKDIFSEVG PVVSFRLVYD RETGKPKGYG
FCEYQDQETA LSAMRNLNGR EFSGRALRVD NAASEKNKEE LKSLGTGAPV IESPYGETIS
PEDAPESISK AVASLPPEQM FELMKQMKLC VQNSPQEARN MLLQNPQLAY ALLQAQVVMR
IVDPEIALKI LHRQTNIPTL IAGNPQTVHS AGPGSGSSVS MNQQNPQTPQ AQTLSGMHVN
GAPPLMQASL QAGVAAPGQI PATVTGPGPG SLAPAGGMQA QVGMPGSGPV SMERGQVPMQ
DPRAAMQRGP LPANVPTPRG LLGDAPNDPR GGTLLSVTGE VEPRGYLGPP HQGPPMHHVP
GHDSRGPPPH EMRGGPLTEP RPLMAEPRGP MIDQRGPPLD GRGGRDPRGI DARAMEARGL
DARGLEARAM EARAMEARAM EARAMEARAM EVRGMEARSM DTRGPVPGPR GPMPSGIQGP
SPINMGAVGP QGSRQVPVMQ GAGMQGASIQ GGGQPGGFSP GQNQVTPQDH EKAALIMQVL
QLTADQIAML PPEQRQSILI LKEQIQKSTG AP
