TFP11_MOUSE
ID TFP11_MOUSE Reviewed; 838 AA.
AC Q9ERA6; Q8VD06;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Tuftelin-interacting protein 11;
DE AltName: Full=Septin and tuftelin-interacting protein 1;
DE Short=STIP-1;
DE AltName: Full=Tuftelin-interacting protein 39;
GN Name=Tfip11; Synonyms=Stip, Tip39;
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].
RC STRAIN=Swiss Webster; TISSUE=Tooth;
RX PubMed=11063033; DOI=10.3109/03008209809017046;
RA Paine C.T., Paine M.L., Snead M.L.;
RT "Identification of tuftelin- and amelogenin-interacting proteins using the
RT yeast two-hybrid system.";
RL Connect. Tissue Res. 38:257-267(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND INTERACTION WITH
RP TUFT1.
RC STRAIN=Swiss Webster; TISSUE=Tooth;
RX PubMed=10806191; DOI=10.1074/jbc.m000118200;
RA Paine C.T., Paine M.L., Luo W., Okamoto C.T., Lyngstadaas S.P., Snead M.L.;
RT "A tuftelin-interacting protein (TIP39) localizes to the apical secretory
RT pole of mouse ameloblasts.";
RL J. Biol. Chem. 275:22284-22292(2000).
RN [3]
RP SEQUENCE REVISION.
RA Paine C.T., Paine M.L., Snead M.L.;
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, 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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15868102; DOI=10.1007/s00018-005-4547-z;
RA Wen X., Lei Y.P., Zhou Y.L., Okamoto C.T., Snead M.L., Paine M.L.;
RT "Structural organization and cellular localization of tuftelin-interacting
RT protein 11 (TFIP11).";
RL Cell. Mol. Life Sci. 62:1038-1046(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-96 AND SER-211, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP SUBCELLULAR LOCATION, INTERACTION WITH DHX15, AND MUTAGENESIS OF GLY-166;
RP GLY-168 AND GLY-170.
RX PubMed=19165350; DOI=10.3390/ijms9112105;
RA Wen X., Tannukit S., Paine M.L.;
RT "TFIP11 interacts with mDEAH9, an RNA helicase involved in spliceosome
RT disassembly.";
RL Int. J. Mol. Sci. 9:2105-2113(2008).
RN [9]
RP FUNCTION IN SPLICEOSOME DISASSEMBLY, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF 701-VAL--ASN-706.
RX PubMed=19857462; DOI=10.1016/j.bbrc.2009.10.111;
RA Tannukit S., Crabb T.L., Hertel K.J., Wen X., Jans D.A., Paine M.L.;
RT "Identification of a novel nuclear localization signal and speckle-
RT targeting sequence of tuftelin-interacting protein 11, a splicing factor
RT involved in spliceosome disassembly.";
RL Biochem. Biophys. Res. Commun. 390:1044-1050(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-96 AND SER-211, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, 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: Involved in pre-mRNA splicing, specifically in spliceosome
CC disassembly during late-stage splicing events. Intron turnover seems to
CC proceed through reactions in two lariat-intron associated complexes
CC termed Intron Large (IL) and Intron Small (IS). In cooperation with
CC DHX15 seems to mediate the transition of the U2, U5 and U6 snRNP-
CC containing IL complex to the snRNP-free IS complex leading to efficient
CC debranching and turnover of excised introns. May play a role in the
CC differentiation of ameloblasts and odontoblasts or in the forming of
CC the enamel extracellular matrix. {ECO:0000269|PubMed:15868102,
CC ECO:0000269|PubMed:19857462}.
CC -!- SUBUNIT: Identified in the spliceosome C complex. Found in the Intron
CC Large (IL) complex, a post-mRNA release spliceosomal complex containing
CC the excised intron, U2, U5 and U6 snRNPs, and splicing factors.
CC Interacts with TUFT1. Interacts with DHX15; indicative for a
CC recruitment of DHX15 to the IL complex. Interacts with GCFC2.
CC {ECO:0000269|PubMed:10806191, ECO:0000269|PubMed:19165350}.
CC -!- INTERACTION:
CC Q9ERA6; O35286: Dhx15; NbExp=3; IntAct=EBI-8338752, EBI-8322087;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=In the nucleus localizes
CC to unique speckle domains in close proximity to nuclear speckles and
CC not identical to paraspeckles.
CC -!- TISSUE SPECIFICITY: Widely expressed. In tooth it is expressed in
CC ameloblasts and odontoblasts.
CC -!- DEVELOPMENTAL STAGE: Expressed as early as 14 dpc and continues into
CC postnatal development. Within the developing tooth, expression is
CC localized at the apical region of the ameloblast cells and to the
CC apical regions of the newly formed enamel matrix.
CC -!- SIMILARITY: Belongs to the TFP11/STIP family. {ECO:0000305}.
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DR EMBL; AF290474; AAG10198.2; -; mRNA.
DR EMBL; BC017682; AAH17682.1; -; mRNA.
DR CCDS; CCDS19539.1; -.
DR RefSeq; NP_061253.2; NM_018783.4.
DR AlphaFoldDB; Q9ERA6; -.
DR BioGRID; 207728; 39.
DR IntAct; Q9ERA6; 3.
DR MINT; Q9ERA6; -.
DR STRING; 10090.ENSMUSP00000031288; -.
DR iPTMnet; Q9ERA6; -.
DR PhosphoSitePlus; Q9ERA6; -.
DR EPD; Q9ERA6; -.
DR jPOST; Q9ERA6; -.
DR MaxQB; Q9ERA6; -.
DR PaxDb; Q9ERA6; -.
DR PRIDE; Q9ERA6; -.
DR ProteomicsDB; 258863; -.
DR Antibodypedia; 9983; 132 antibodies from 22 providers.
DR DNASU; 54723; -.
DR Ensembl; ENSMUST00000031288; ENSMUSP00000031288; ENSMUSG00000029345.
DR GeneID; 54723; -.
DR KEGG; mmu:54723; -.
DR UCSC; uc008ysy.1; mouse.
DR CTD; 24144; -.
DR MGI; MGI:1930075; Tfip11.
DR VEuPathDB; HostDB:ENSMUSG00000029345; -.
DR eggNOG; KOG2184; Eukaryota.
DR GeneTree; ENSGT00390000012739; -.
DR HOGENOM; CLU_007977_1_1_1; -.
DR InParanoid; Q9ERA6; -.
DR OMA; EFFPKWH; -.
DR OrthoDB; 1238995at2759; -.
DR PhylomeDB; Q9ERA6; -.
DR TreeFam; TF314887; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 54723; 16 hits in 73 CRISPR screens.
DR ChiTaRS; Tfip11; mouse.
DR PRO; PR:Q9ERA6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9ERA6; protein.
DR Bgee; ENSMUSG00000029345; Expressed in superior surface of tongue and 295 other tissues.
DR ExpressionAtlas; Q9ERA6; baseline and differential.
DR Genevisible; Q9ERA6; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISA:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISA:MGI.
DR GO; GO:0005681; C:spliceosomal complex; ISS:UniProtKB.
DR GO; GO:0071008; C:U2-type post-mRNA release spliceosomal complex; ISS:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; NAS:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; NAS:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0000390; P:spliceosomal complex disassembly; IMP:UniProtKB.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR022783; GCFC_dom.
DR InterPro; IPR024933; STIP.
DR InterPro; IPR022159; STIP/TFIP11_N.
DR InterPro; IPR045211; TFP11/STIP/Ntr1.
DR PANTHER; PTHR23329; PTHR23329; 1.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF07842; GCFC; 1.
DR Pfam; PF12457; TIP_N; 1.
DR PIRSF; PIRSF017706; TFIP11; 1.
DR SMART; SM00443; G_patch; 1.
DR PROSITE; PS50174; G_PATCH; 1.
PE 1: Evidence at protein level;
KW Biomineralization; Cytoplasm; Direct protein sequencing; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Spliceosome.
FT CHAIN 1..838
FT /note="Tuftelin-interacting protein 11"
FT /id="PRO_0000072502"
FT DOMAIN 150..196
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..51
FT /note="Required for interaction with DHX15"
FT /evidence="ECO:0000250"
FT REGION 86..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..735
FT /note="Required for nuclear speckle localization"
FT MOTIF 701..706
FT /note="Nuclear localization signal"
FT COMPBIAS 41..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U2Y6"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBB9"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBB9"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MUTAGEN 166
FT /note="G->A: No effect on nuclear speckled pattern
FT localization; when associated with A-168 and R-170."
FT /evidence="ECO:0000269|PubMed:19165350"
FT MUTAGEN 168
FT /note="G->A: No effect on nuclear speckled pattern
FT localization; when associated with A-166 and R-170."
FT /evidence="ECO:0000269|PubMed:19165350"
FT MUTAGEN 170
FT /note="G->R: No effect on nuclear speckled pattern
FT localization; when associated with A-166 and A-168."
FT /evidence="ECO:0000269|PubMed:19165350"
FT MUTAGEN 701..706
FT /note="VKDKFN->TTTTT: Predominant cytoplasmic
FT localization."
FT /evidence="ECO:0000269|PubMed:19857462"
FT CONFLICT 393
FT /note="A -> T (in Ref. 4; AAH17682)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 838 AA; 96305 MW; B50842BF12733930 CRC64;
MSLSHLYRDG EGHLDDDDDD ERENFEITDW DLQNEFNPNR QRHWQTKEEA TYGVWAERDS
DEERPSFGGK RARDYSAPVN FISAGLKKGA AEEADSEDSD AEEKPVKQED FPKDLGPKKL
KTGGNFKPSQ KGFSGGTKSF MDFGSWERHT KGIGQKLLQK MGYVPGRGLG KNAQGIINPI
EAKQRKGKGA VGAYGSERTT QSLQDFPVAD SEEEAEEEFQ KELSQWRKDP SGSKKKPKYS
YKTVEELKAK GRVSKKLTAP QKELSQVKVI DMTGREQKVY YSYSQISHKH SVPDEGVPLL
AQLPPTAGKE ARMPGFALPE LEHNLQLLIE RTEQEIIQSD RQLQYERDMV VSLSHELEKT
AEVLAHEERV ISNLSKVLAL VEECERRMQP HGADPLTLDE CARIFETLQD KYYEEYRLAD
RADLAVAIVY PLVKDYFKDW HPLEDGSYGT QIISKWKSLL ENDQLLSHSS QDLSSDAFHR
LMWEVWMPFV RNVVAQWQPR NCEPMVDFLD SWAHIIPVWI LDNILDQLIF PKLQKEVDNW
NPLTDTVPIH SWIHPWLPLM QARLEPLYSP VRSKLSSALQ KWHPSDASAK LILQPWKEVL
TPGSWEAFML RNIVPKLGMC LGELVINPHQ QHMDAFYWVM DWEGMISVSS LVGLLEKHFF
PKWLQVLCSW LSNSPNYEEI TKWYLGWKSM FSDQVLAHPS VKDKFNEALD IMNRAVSSNV
GAYMQPGARE NIAYLTHTER RKDFQYEAMQ ERREAENMAQ RGIGVAASSV PMNFKDLIET
KAEEHNIVFM PVIGKRHEGK QLYTFGRIVI YIDRGVVFVQ GEKTWVPTSL QSLIDMAK
