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   24-JAN-2024, entry version 157.
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,
RC   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. 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; 10090-ENSMUSP00000033609; -.
DR   PeptideAtlas; Q8BIQ5; -.
DR   ProteomicsDB; 285381; -. [Q8BIQ5-1]
DR   ProteomicsDB; 285382; -. [Q8BIQ5-2]
DR   Pumba; Q8BIQ5; -.
DR   Antibodypedia; 411; 413 antibodies from 33 providers.
DR   DNASU; 108062; -.
DR   Ensembl; ENSMUST00000033609.9; ENSMUSP00000033609.3; ENSMUSG00000031256.12. [Q8BIQ5-1]
DR   Ensembl; ENSMUST00000113286.8; ENSMUSP00000108911.2; ENSMUSG00000031256.12. [Q8BIQ5-2]
DR   GeneID; 108062; -.
DR   KEGG; mmu:108062; -.
DR   UCSC; uc009ufi.2; mouse. [Q8BIQ5-2]
DR   UCSC; uc009ufj.2; mouse. [Q8BIQ5-1]
DR   AGR; MGI:1343054; -.
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; 179465at2759; -.
DR   PhylomeDB; Q8BIQ5; -.
DR   TreeFam; TF314948; -.
DR   Reactome; R-MMU-72187; mRNA 3'-end processing.
DR   Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA.
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 82 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 256 other cell types or tissues.
DR   ExpressionAtlas; Q8BIQ5; 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: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:0031124; P:mRNA 3'-end processing; IEA:InterPro.
DR   CDD; cd12671; RRM_CSTF2_CSTF2T; 1.
DR   Gene3D; 1.25.40.630; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 1.10.20.70; Transcription termination and cleavage factor, C-terminal domain; 1.
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; CLEAVAGE STIMULATION FACTOR SUBUNIT 2; 1.
DR   PANTHER; PTHR45735:SF6; CLEAVAGE STIMULATION FACTOR SUBUNIT 2; 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; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   Genevisible; Q8BIQ5; MM.
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
//