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   02-JUN-2021, entry version 157.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   BioGRID; 207728; 39.
DR   IntAct; Q9ERA6; 4.
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; 118 antibodies.
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   eggNOG; KOG2184; Eukaryota.
DR   GeneTree; ENSGT00390000012739; -.
DR   HOGENOM; CLU_007977_1_1_1; -.
DR   InParanoid; Q9ERA6; -.
DR   OMA; VWEWHEL; -.
DR   OrthoDB; 1238995at2759; -.
DR   PhylomeDB; Q9ERA6; -.
DR   TreeFam; TF314887; -.
DR   Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR   BioGRID-ORCS; 54723; 15 hits in 52 CRISPR screens.
DR   ChiTaRS; Tfip11; mouse.
DR   PRO; PR:Q9ERA6; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q9ERA6; protein.
DR   Bgee; ENSMUSG00000029345; Expressed in frontal cortex and 335 other tissues.
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   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
//