CSTF2_MOUSE
ID CSTF2_MOUSE Reviewed; 580 AA.
AC Q8BIQ5; A2AEJ9; A2AEK0; Q8K1Y6; Q9ERC2;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 149.
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 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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=CD-1; TISSUE=Testis;
RX PubMed=11369601; DOI=10.1095/biolreprod64.6.1722;
RA Dass B., Attaya E.N., Michelle Wallace A., MacDonald C.C.;
RT "Overexpression of the CstF-64 and CPSF-160 polyadenylation protein
RT messenger RNAs in mouse male germ cells.";
RL Biol. Reprod. 64:1722-1729(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Thymus, and Wolffian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [5]
RP INDUCTION.
RX PubMed=9736695; DOI=10.1073/pnas.95.19.11095;
RA Martincic K., Campbell R., Edwalds-Gilbert G., Souan L., Lotze M.T.,
RA Milcarek C.;
RT "Increase in the 64-kDa subunit of the polyadenylation/cleavage stimulatory
RT factor during the G0 to S phase transition.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11095-11100(1998).
RN [6]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=14681198; DOI=10.1095/biolreprod.103.022947;
RA Wallace A.M., Denison T.L., Attaya E.N., MacDonald C.C.;
RT "Developmental distribution of the polyadenylation protein CstF-64 and the
RT variant tauCstF-64 in mouse and rat testis.";
RL Biol. Reprod. 70:1080-1087(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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. 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:0000269|PubMed:14681198}.
CC Note=Localized with DDX1 in cleavage bodies. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BIQ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BIQ5-2; Sequence=VSP_014844, VSP_014845;
CC -!- TISSUE SPECIFICITY: Expressed in most somatic cell types (at protein
CC level). Highly expressed in testis, except in meiotic spermatocytes.
CC {ECO:0000269|PubMed:11369601, ECO:0000269|PubMed:14681198}.
CC -!- INDUCTION: Up-regulated during the G to S phase transition.
CC {ECO:0000269|PubMed:9736695}.
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DR EMBL; AF317552; AAG31814.1; -; mRNA.
DR EMBL; AK032817; BAC28037.1; -; mRNA.
DR EMBL; AK088260; BAC40243.1; -; mRNA.
DR EMBL; AL671915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036719; AAH36719.1; -; mRNA.
DR CCDS; CCDS30389.1; -. [Q8BIQ5-1]
DR CCDS; CCDS81170.1; -. [Q8BIQ5-2]
DR RefSeq; NP_001277328.1; NM_001290399.1. [Q8BIQ5-2]
DR RefSeq; NP_573459.1; NM_133196.6. [Q8BIQ5-1]
DR AlphaFoldDB; Q8BIQ5; -.
DR BMRB; Q8BIQ5; -.
DR SMR; Q8BIQ5; -.
DR BioGRID; 223801; 8.
DR IntAct; Q8BIQ5; 2.
DR MINT; Q8BIQ5; -.
DR STRING; 10090.ENSMUSP00000033609; -.
DR iPTMnet; Q8BIQ5; -.
DR PhosphoSitePlus; Q8BIQ5; -.
DR REPRODUCTION-2DPAGE; IPI00607981; -.
DR EPD; Q8BIQ5; -.
DR jPOST; Q8BIQ5; -.
DR MaxQB; Q8BIQ5; -.
DR PaxDb; Q8BIQ5; -.
DR PeptideAtlas; Q8BIQ5; -.
DR PRIDE; Q8BIQ5; -.
DR ProteomicsDB; 285381; -. [Q8BIQ5-1]
DR ProteomicsDB; 285382; -. [Q8BIQ5-2]
DR Antibodypedia; 411; 349 antibodies from 33 providers.
DR DNASU; 108062; -.
DR Ensembl; ENSMUST00000033609; ENSMUSP00000033609; ENSMUSG00000031256. [Q8BIQ5-1]
DR Ensembl; ENSMUST00000113286; ENSMUSP00000108911; ENSMUSG00000031256. [Q8BIQ5-2]
DR GeneID; 108062; -.
DR KEGG; mmu:108062; -.
DR UCSC; uc009ufi.2; mouse. [Q8BIQ5-2]
DR UCSC; uc009ufj.2; mouse. [Q8BIQ5-1]
DR CTD; 1478; -.
DR MGI; MGI:1343054; Cstf2.
DR VEuPathDB; HostDB:ENSMUSG00000031256; -.
DR eggNOG; KOG0108; Eukaryota.
DR GeneTree; ENSGT00940000158987; -.
DR InParanoid; Q8BIQ5; -.
DR OMA; CEPEDAP; -.
DR OrthoDB; 1455080at2759; -.
DR PhylomeDB; Q8BIQ5; -.
DR TreeFam; TF314948; -.
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; 108062; 12 hits in 77 CRISPR screens.
DR ChiTaRS; Cstf2; mouse.
DR PRO; PR:Q8BIQ5; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8BIQ5; protein.
DR Bgee; ENSMUSG00000031256; Expressed in ventromedial nucleus of hypothalamus and 252 other tissues.
DR ExpressionAtlas; Q8BIQ5; baseline and differential.
DR Genevisible; Q8BIQ5; MM.
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:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
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 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Methylation; mRNA processing;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Ubl conjugation.
FT CHAIN 1..580
FT /note="Cleavage stimulation factor subunit 2"
FT /id="PRO_0000081532"
FT DOMAIN 16..94
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 413..417
FT /note="1; approximate"
FT REPEAT 418..422
FT /note="2"
FT REPEAT 423..427
FT /note="3"
FT REPEAT 428..432
FT /note="4; approximate"
FT REPEAT 433..437
FT /note="5; approximate"
FT REPEAT 438..442
FT /note="6"
FT REPEAT 443..447
FT /note="7"
FT REPEAT 448..452
FT /note="8"
FT REPEAT 453..457
FT /note="9"
FT REPEAT 458..462
FT /note="10"
FT REPEAT 463..467
FT /note="11"
FT REPEAT 468..472
FT /note="12; approximate"
FT REGION 108..248
FT /note="Interactions with CSTF3 and SYMPK"
FT /evidence="ECO:0000250"
FT REGION 311..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..472
FT /note="12 X 5 AA tandem repeats of M-E-A-R-[AG]"
FT REGION 511..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..580
FT /note="Interaction with RPO2TC1"
FT /evidence="ECO:0000250"
FT COMPBIAS 514..536
FT /note="Polar 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 471
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P33240"
FT MOD_RES 478
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P33240"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33240"
FT MOD_RES 527
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"
FT VAR_SEQ 505..510
FT /note="PVMQGA -> MLVAYT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014844"
FT VAR_SEQ 511..580
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014845"
FT CONFLICT 299
FT /note="M -> V (in Ref. 2; BAC28037)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 580 AA; 61341 MW; DF61B2F5E5EAB1B7 CRC64;
MAGLPVRDPA VDRSLRSVFV GNIPYEATEE QLKDIFSEVG PVVSFRLVYD RETGKPKGYG
FCEYQDQETA LSAMRNLNGR EFSGRALRVD NAASEKNKEE LKSLGTGAPV IESPYGESIS
PEDAPESISK AVASLPPEQM FELMKQMKLC VQNSPQEARN MLLQNPQLAY ALLQAQVVMR
IVDPEIALKI LHRQTNIPTL ISGNPQPVHV AGPGSGPNVS MNQQNPQAPQ AQSLGGMHVN
GAPPMMQASM PGGVPAPVQM AAAVGGPGPG SLAPAGVMQA QVGMQGAGPV PMERGQVPMQ
DPRAAMQRGA LPTNVPTPRG LLGDAPNDPR GGTLMTVTGD VEPRAYLGPP PPPHQGPPMH
HVPGHEGRGP PPHDMRGGPL AEPRPLMAEP RGPMLDQRGP PLDARGGRDP RGLDARGMEA
RAMEARGLDA RGLEARAMEA RAMEARAMEA RAMEARAMEA RAMEARGMDT RGPVPGPRGP
MPSGIQGPNP MNMGAVVPQG SRQVPVMQGA GMQGASMQGG SQPGGFSPGQ SQVTPQDHEK
AALIMQVLQL TADQIAMLPP EQRQSILILK EQIQKSTGAP
