GCFC2_MOUSE
ID GCFC2_MOUSE Reviewed; 769 AA.
AC Q8BKT3; Q3UWF7; Q8BK44;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Intron Large complex component GCFC2;
DE AltName: Full=GC-rich sequence DNA-binding factor;
DE AltName: Full=GC-rich sequence DNA-binding factor 2;
DE AltName: Full=Transcription factor 9;
DE Short=TCF-9;
GN Name=Gcfc2; Synonyms=Gcf, Tcf9;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 8-769 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Lung, Ovary, and Uterus;
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 [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-86, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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: Involved in pre-mRNA splicing through regulating spliceosome
CC C complex formation (By similarity). May play a role during late-stage
CC splicing events and turnover of excised introns (By similarity).
CC {ECO:0000250|UniProtKB:P16383}.
CC -!- SUBUNIT: Found in the Intron Large (IL) complex, a post-mRNA release
CC spliceosomal complex containing the excised intron, U2, U5 and U6
CC snRNPs, and splicing factors (By similarity). Interacts with TFIP11 and
CC DHX15 (By similarity). {ECO:0000250|UniProtKB:P16383}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:P16383}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P16383}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BKT3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BKT3-2; Sequence=VSP_021799, VSP_021800;
CC -!- SIMILARITY: Belongs to the GCF family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a DNA-binding transcriptional
CC repressor (By similarity). However, later work showed that the original
CC sequence was a chimera and that the DNA-binding activity was derived
CC from the incorrect N-terminal sequence (By similarity).
CC {ECO:0000250|UniProtKB:P16383}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC34411.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK050789; BAC34411.1; ALT_INIT; mRNA.
DR EMBL; AK077263; BAC36717.1; -; mRNA.
DR EMBL; AK136387; BAE22958.1; -; mRNA.
DR EMBL; AC129024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS20260.1; -. [Q8BKT3-1]
DR RefSeq; NP_808552.2; NM_177884.3. [Q8BKT3-1]
DR AlphaFoldDB; Q8BKT3; -.
DR SMR; Q8BKT3; -.
DR BioGRID; 236949; 4.
DR IntAct; Q8BKT3; 3.
DR STRING; 10090.ENSMUSP00000035644; -.
DR iPTMnet; Q8BKT3; -.
DR PhosphoSitePlus; Q8BKT3; -.
DR EPD; Q8BKT3; -.
DR jPOST; Q8BKT3; -.
DR MaxQB; Q8BKT3; -.
DR PaxDb; Q8BKT3; -.
DR PeptideAtlas; Q8BKT3; -.
DR PRIDE; Q8BKT3; -.
DR ProteomicsDB; 267779; -. [Q8BKT3-1]
DR ProteomicsDB; 267780; -. [Q8BKT3-2]
DR Antibodypedia; 31654; 175 antibodies from 27 providers.
DR DNASU; 330361; -.
DR Ensembl; ENSMUST00000043195; ENSMUSP00000035644; ENSMUSG00000035125. [Q8BKT3-1]
DR GeneID; 330361; -.
DR KEGG; mmu:330361; -.
DR UCSC; uc009clc.1; mouse. [Q8BKT3-2]
DR UCSC; uc009cld.1; mouse. [Q8BKT3-1]
DR CTD; 6936; -.
DR MGI; MGI:2141656; Gcfc2.
DR VEuPathDB; HostDB:ENSMUSG00000035125; -.
DR eggNOG; KOG2136; Eukaryota.
DR GeneTree; ENSGT00390000000455; -.
DR HOGENOM; CLU_010846_2_0_1; -.
DR InParanoid; Q8BKT3; -.
DR OMA; MKMYVEN; -.
DR OrthoDB; 1217358at2759; -.
DR PhylomeDB; Q8BKT3; -.
DR TreeFam; TF315109; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 330361; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Gcfc2; mouse.
DR PRO; PR:Q8BKT3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8BKT3; protein.
DR Bgee; ENSMUSG00000035125; Expressed in manus and 182 other tissues.
DR ExpressionAtlas; Q8BKT3; baseline and differential.
DR Genevisible; Q8BKT3; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0071008; C:U2-type post-mRNA release spliceosomal complex; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000245; P:spliceosomal complex assembly; ISS:UniProtKB.
DR InterPro; IPR012890; GCFC2-like.
DR InterPro; IPR022783; GCFC_dom.
DR PANTHER; PTHR12214; PTHR12214; 1.
DR Pfam; PF07842; GCFC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..769
FT /note="Intron Large complex component GCFC2"
FT /id="PRO_0000262647"
FT REGION 1..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 256..308
FT /evidence="ECO:0000255"
FT COMPBIAS 8..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16383"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16383"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16383"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16383"
FT MOD_RES 86
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16383"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16383"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16383"
FT VAR_SEQ 399..405
FT /note="MQRRQAR -> YLYKVQT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021799"
FT VAR_SEQ 406..769
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021800"
FT CONFLICT 121
FT /note="V -> F (in Ref. 1; BAE22958)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 769 AA; 87442 MW; FCD6573BFE1C0DB7 CRC64;
MALRPQRTFR RRQVESSDSD SDSDGAKEQS AEEPASAGGR TEGAERPRGA RSARGRGRVW
ASSRRSPGAA PRGDGGAECR TAELSTDEEE GTHTLTGSKG DRSPSSDSSC SLEERDVSPI
VEIPDAAFIQ AARRKRELAR TPGDYISLDV NHSCSTSDCK RSNEEDPESD PDDHEKRILF
TPKPQTLRQR MAEETSIRSE ESSEESQEDE NQDIWEQQQM RKAVRIPAGQ NTDLSHSSKS
QTLKKFDTSI SFPPVNLEII KKQLNNRLTL LQESHRSHQR EYEKYEQDIK SSKTAIQNLE
SASDHAQNYR FYRGMKSYVE NIIDCLNEKI VSIVELESSM YTLLLKRSEA LLKRRQDELK
CESSYLQQLS RKDETSANGS LAVDEKDQRI LEEIEARRMQ RRQARELSGS CDHQEGMSSD
DELSPAEMTN FHKCQGDILQ DCKKVFEDVH DDFCNVQNIL LKFQQWREKF PDSYYEAFVG
FCLPKLLSPL IRVQLLDWNP LKMDSIGLDK MPWFTAITEF MESSMDDIGK EDGSDKKILA
AVINKTVVPR LTDFVETIWD PLSTSQTRSL TVHCRVAFEQ FASENEVSKN KQDLLKSIVA
RMKKSIEDDI FIPLYPKSSE EGKMSPHSKF QERQFWGALK LFRNILLWNG LLPDDTLQDL
GLGKLLNRYL IISLTNAVPG PDVVKKCSQI AACLPERWFE NSAMRTSIPQ LENFIKFLLQ
SAQKLSSSEF RNEVSEIILI LVKVKALTQA ESLREERPLE PLPAQSTGV
