CSTFT_MOUSE
ID CSTFT_MOUSE Reviewed; 632 AA.
AC Q8C7E9; Q6A016; Q8BHH7; Q8C3W7; Q8R2Y1; Q9EPU3;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Cleavage stimulation factor subunit 2 tau variant;
DE AltName: Full=CF-1 64 kDa subunit tau variant;
DE AltName: Full=Cleavage stimulation factor 64 kDa subunit tau variant;
DE Short=CSTF 64 kDa subunit tau variant;
DE AltName: Full=TauCstF-64;
GN Name=Cstf2t; Synonyms=Kiaa0689;
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], RNA-BINDING, AND FUNCTION.
RC STRAIN=CD-1; TISSUE=Testis;
RX PubMed=11113135; DOI=10.1074/jbc.m009091200;
RA Dass B., McMahon K.W., Jenkins N.A., Gilbert D.J., Copeland N.G.,
RA MacDonald C.C.;
RT "The gene for a variant form of the polyadenylation protein CstF-64 is on
RT chromosome 19 and is expressed in pachytene spermatocytes in mice.";
RL J. Biol. Chem. 276:8044-8050(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Heart, and Liver;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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: May play a significant role in AAUAAA-independent mRNA
CC polyadenylation in germ cells. Directly involved in the binding to pre-
CC mRNAs. {ECO:0000269|PubMed:11113135}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14681198}.
CC -!- TISSUE SPECIFICITY: Expressed in testes, where it is restricted to
CC pachytene spermatocytes and spermatids, and in the brain (at protein
CC level). {ECO:0000269|PubMed:14681198}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39256.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD32280.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF322194; AAG40327.1; -; mRNA.
DR EMBL; AK173002; BAD32280.1; ALT_INIT; mRNA.
DR EMBL; AK034853; BAC28855.1; -; mRNA.
DR EMBL; AK050407; BAC34240.1; -; mRNA.
DR EMBL; AK082910; BAC38683.1; -; mRNA.
DR EMBL; AK084696; BAC39256.1; ALT_FRAME; mRNA.
DR EMBL; BC026995; AAH26995.1; -; mRNA.
DR CCDS; CCDS37958.1; -.
DR RefSeq; NP_112539.2; NM_031249.2.
DR AlphaFoldDB; Q8C7E9; -.
DR SMR; Q8C7E9; -.
DR BioGRID; 219918; 30.
DR STRING; 10090.ENSMUSP00000093831; -.
DR iPTMnet; Q8C7E9; -.
DR PhosphoSitePlus; Q8C7E9; -.
DR REPRODUCTION-2DPAGE; IPI00467932; -.
DR EPD; Q8C7E9; -.
DR jPOST; Q8C7E9; -.
DR MaxQB; Q8C7E9; -.
DR PaxDb; Q8C7E9; -.
DR PeptideAtlas; Q8C7E9; -.
DR PRIDE; Q8C7E9; -.
DR ProteomicsDB; 283970; -.
DR Antibodypedia; 27941; 203 antibodies from 28 providers.
DR DNASU; 83410; -.
DR Ensembl; ENSMUST00000066039; ENSMUSP00000093831; ENSMUSG00000053536.
DR GeneID; 83410; -.
DR KEGG; mmu:83410; -.
DR UCSC; uc008her.1; mouse.
DR CTD; 23283; -.
DR MGI; MGI:1932622; Cstf2t.
DR VEuPathDB; HostDB:ENSMUSG00000053536; -.
DR eggNOG; KOG0108; Eukaryota.
DR GeneTree; ENSGT00940000161661; -.
DR HOGENOM; CLU_028601_3_1_1; -.
DR InParanoid; Q8C7E9; -.
DR OMA; GMQGTGI; -.
DR OrthoDB; 1455080at2759; -.
DR PhylomeDB; Q8C7E9; -.
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; 83410; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Cstf2t; mouse.
DR PRO; PR:Q8C7E9; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8C7E9; protein.
DR Bgee; ENSMUSG00000053536; Expressed in pineal body and 256 other tissues.
DR Genevisible; Q8C7E9; MM.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
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; IDA:MGI.
DR GO; GO:0006378; P:mRNA polyadenylation; TAS:MGI.
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; 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 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 mRNA processing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding.
FT CHAIN 1..632
FT /note="Cleavage stimulation factor subunit 2 tau variant"
FT /id="PRO_0000081535"
FT DOMAIN 16..94
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 428..432
FT /note="1-1; approximate"
FT REPEAT 433..437
FT /note="1-2; approximate"
FT REPEAT 438..442
FT /note="1-3; approximate"
FT REPEAT 443..446
FT /note="1-4; approximate"
FT REPEAT 447..451
FT /note="1-5; approximate"
FT REPEAT 452..456
FT /note="1-6"
FT REPEAT 457..461
FT /note="1-7; approximate"
FT REPEAT 462..466
FT /note="1-8; approximate"
FT REPEAT 508..512
FT /note="2-1; approximate"
FT REPEAT 513..517
FT /note="2-2"
FT REPEAT 518..522
FT /note="2-3; approximate"
FT REPEAT 523..527
FT /note="2-4"
FT REPEAT 528..532
FT /note="2-5; approximate"
FT REPEAT 533..537
FT /note="2-6"
FT REPEAT 538..542
FT /note="2-7; approximate"
FT REPEAT 543..547
FT /note="2-8"
FT REPEAT 548..551
FT /note="2-9; approximate"
FT REPEAT 552..556
FT /note="2-10; approximate"
FT REPEAT 557..560
FT /note="2-11; approximate"
FT REPEAT 561..565
FT /note="2-12"
FT REGION 201..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..466
FT /note="8 X 5 AA tandem repeats of M-E-T-R-[AG]"
FT REGION 508..565
FT /note="12 X 5 AA tandem repeats of G-[AT]-G-[MI]-Q"
FT REGION 519..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..233
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..257
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 213..227
FT /note="PGGPGPSGPGGPGPG -> LVGWASGLAAGPA (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 214..216
FT /note="GGP -> WWAL (in Ref. 3; BAC39256)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="P -> S (in Ref. 3; BAC34240)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="M -> MEARGM (in Ref. 4; AAH26995)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 632 AA; 65862 MW; 1CDB48EEC5B814B8 CRC64;
MSSLAVRDPA MDRSLRSVFV GNIPYEATEE QLKDIFSEVG SVVSFRLVYD RETGKPKGYG
FCEYQDQETA LSAMRNLNGR EFSGRALRVD NAASEKNKEE LKSLGPAAPI IDSPYGDPID
PEDAPESITR AVASLPPEQM FELMKQMKLC VQNSHQEARN MLLQNPQLAY ALLQAQVVMR
IMDPEIALKI LHRKIHVTPL IPGKSQPVSG PGPGGPGPSG PGGPGPGPAP GLCPGPNVML
NQQNPPAPQP QHLPRRPVKD IPPLMQTSIQ GGIPAPGPIP AAVPGPGPGS LTPGGAMQPQ
VGMPVVGPVP LERGQMQISD PRPPMPRGPM PSGGIPPRGL LGDAPNDPRG GTLLSVTGEV
EPRGYMGPPH QGPPMHHGHD NRGPASHDMR GGPLAADPRM LIGEPRGPMI DQRGLPMDGR
GGRESRGMET RPMETEVLEP RGMERRMETC AMETRGMDAR GLEMRGPGPS SRGPMTGGIQ
GPGPINMGAG GPQGPRQVPN IAGVGNPGGT MQGAGIQGGG MQGAGMQGGG MQGAGMQGGG
MQGAGMQAGM QGASMQGGMQ GAGMQGASKQ GGGQPSSFSP GQSQVTPQDQ EKAALIMQVL
QLTADQIAML PPEQRQSILI LKEQIQKSTG AS
