TAF7L_MOUSE
ID TAF7L_MOUSE Reviewed; 471 AA.
AC Q9D3R9; A2AFB9; Q99MW7;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Transcription initiation factor TFIID subunit 7-like;
DE AltName: Full=TATA box binding protein-associated factor RNA polymerase II subunit Q;
DE AltName: Full=TATA box-binding protein-associated factor 50 kDa;
DE AltName: Full=Transcription initiation factor TFIID 50 kDa subunit;
GN Name=Taf7l; Synonyms=Taf2q;
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 2), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11279525; DOI=10.1038/86927;
RA Wang P.J., McCarrey J.R., Yang F., Page D.C.;
RT "An abundance of X-linked genes expressed in spermatogonia.";
RL Nat. Genet. 27:422-426(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 247-262,
RP FUNCTION, AND INTERACTION WITH TBP AND TAF1.
RX PubMed=12665565; DOI=10.1242/jcs.00391;
RA Pointud J.-C., Mengus G., Brancorsini S., Monaco L., Parvinen M.,
RA Sassone-Corsi P., Davidson I.;
RT "The intracellular localisation of TAF7L, a paralogue of transcription
RT factor TFIID subunit TAF7, is developmentally regulated during male germ-
RT cell differentiation.";
RL J. Cell Sci. 116:1847-1858(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17242199; DOI=10.1128/mcb.01722-06;
RA Cheng Y., Buffone M.G., Kouadio M., Goodheart M., Page D.C., Gerton G.L.,
RA Davidson I., Wang P.J.;
RT "Abnormal sperm in mice lacking the Taf7l gene.";
RL Mol. Cell. Biol. 27:2582-2589(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: Probably functions as a spermatogenesis-specific component of
CC the DNA-binding general transcription factor complex TFIID, a
CC multimeric protein complex that plays a central role in mediating
CC promoter responses to various activators and repressors. May play a
CC role in spermatogenesis. {ECO:0000269|PubMed:12665565}.
CC -!- SUBUNIT: TFIID is composed of TATA binding protein (TBP) and a number
CC of TBP-associated factors (TAFs). TAF7L may replace TAF7 in a
CC spermatogenesis-specific form of TFIID. Interacts with TBP; the
CC interaction occurs in a sub-population of cells (pachytene and haploid
CC round spermatids) and is developmentally regulated through differential
CC intracellular localization of the two proteins. Interacts with TAF1.
CC {ECO:0000269|PubMed:12665565}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Cytoplasmic in
CC spermatogonia and early spermatocytes (preleptotene, leptotene, and
CC zygotene); translocates into the nuclei of pachytene spermatocytes and
CC round spermatids.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D3R9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D3R9-2; Sequence=VSP_028849;
CC -!- TISSUE SPECIFICITY: Testis-specific (at protein level). Expressed
CC during spermatogenesis from spermatogonia stage up to the stage of
CC round spermatids. {ECO:0000269|PubMed:11279525,
CC ECO:0000269|PubMed:17242199}.
CC -!- DISRUPTION PHENOTYPE: Reduced sperm count and motility.
CC {ECO:0000269|PubMed:17242199}.
CC -!- SIMILARITY: Belongs to the TAF7 family. {ECO:0000305}.
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DR EMBL; AF285574; AAK31953.1; -; mRNA.
DR EMBL; AK017109; BAB30600.1; -; mRNA.
DR EMBL; AL672064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC106854; AAI06855.1; -; mRNA.
DR CCDS; CCDS53184.1; -. [Q9D3R9-1]
DR RefSeq; NP_083234.2; NM_028958.4. [Q9D3R9-1]
DR AlphaFoldDB; Q9D3R9; -.
DR SMR; Q9D3R9; -.
DR BioGRID; 216775; 4.
DR CORUM; Q9D3R9; -.
DR STRING; 10090.ENSMUSP00000009740; -.
DR iPTMnet; Q9D3R9; -.
DR PhosphoSitePlus; Q9D3R9; -.
DR PaxDb; Q9D3R9; -.
DR PRIDE; Q9D3R9; -.
DR ProteomicsDB; 254853; -. [Q9D3R9-1]
DR ProteomicsDB; 254854; -. [Q9D3R9-2]
DR DNASU; 74469; -.
DR Ensembl; ENSMUST00000009740; ENSMUSP00000009740; ENSMUSG00000009596. [Q9D3R9-1]
DR GeneID; 74469; -.
DR KEGG; mmu:74469; -.
DR UCSC; uc009ugc.2; mouse. [Q9D3R9-1]
DR CTD; 54457; -.
DR MGI; MGI:1921719; Taf7l.
DR VEuPathDB; HostDB:ENSMUSG00000009596; -.
DR eggNOG; KOG4011; Eukaryota.
DR GeneTree; ENSGT00940000161565; -.
DR HOGENOM; CLU_037860_0_0_1; -.
DR InParanoid; Q9D3R9; -.
DR OMA; NWKHGIT; -.
DR OrthoDB; 1348389at2759; -.
DR PhylomeDB; Q9D3R9; -.
DR TreeFam; TF313044; -.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-MMU-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-MMU-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-MMU-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR BioGRID-ORCS; 74469; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Taf7l; mouse.
DR PRO; PR:Q9D3R9; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9D3R9; protein.
DR Bgee; ENSMUSG00000009596; Expressed in placenta labyrinth and 18 other tissues.
DR ExpressionAtlas; Q9D3R9; baseline and differential.
DR Genevisible; Q9D3R9; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005669; C:transcription factor TFIID complex; IBA:GO_Central.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IBA:GO_Central.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR CDD; cd08047; TAF7; 1.
DR InterPro; IPR037817; TAF7.
DR InterPro; IPR006751; TAFII55_prot_cons_reg.
DR PANTHER; PTHR12228; PTHR12228; 1.
DR Pfam; PF04658; TAFII55_N; 1.
DR SMART; SM01370; TAFII55_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Developmental protein;
KW Differentiation; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Spermatogenesis; Transcription;
KW Transcription regulation.
FT CHAIN 1..471
FT /note="Transcription initiation factor TFIID subunit 7-
FT like"
FT /id="PRO_0000307862"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 358..433
FT /evidence="ECO:0000255"
FT COMPBIAS 343..375
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..93
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11279525,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_028849"
FT CONFLICT 15
FT /note="E -> D (in Ref. 3; BAB30600)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 471 AA; 52905 MW; B7137077480EFB18 CRC64;
MERGEEAPTE GAPPEGALVE AKAPVIPEAP ATDVSTTEEA GSKEPQVPSG PRPEGAGDTC
DTRGARGPPT PGRAKSQKTP RQGTARCQTL ESAMRSMSVR LECHDVEEQF ILRLPPEQAY
AVRKIIHSRN AAWKDKLKID FSPDGHHAVV QVDNVSLPAK LVNLPCVIGS LKTIDRKTFY
KTADVSQMLV CSPEGEPHSP PEEPVVSTGP TVIGISEGKA ERKKYNWKHG ITPPLKNVRK
KRFRKTTKKL PDVKQVDEIN FSEYTQSPSV EKEVKRLLYS DAEAVSVRWE VVDDDDAKEI
ESQGSMPTTP GISQMGGASL SDYDVFREMM GDSGSNSNDV EEKSNEGDDD DDEDEDDEDY
GNEKEEEETD NSEEELEKEL QAKFNEFSLH EADQDYSSIT MAIQKLIFIK EKRLQMIYKK
AQRQKELLRK VENLTLKRHF QNVLGKLNIM EKEKCEQIYH LQEQLKCFLK E
