ID M3YQ93_MUSPF Unreviewed; 881 AA.
AC M3YQ93;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Tuftelin-interacting protein 11 {ECO:0000256|ARBA:ARBA00015137, ECO:0000256|PIRNR:PIRNR017706};
GN Name=TFIP11 {ECO:0000313|Ensembl:ENSMPUP00000013502.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000013502.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000013502.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
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:0000256|ARBA:ARBA00024931,
CC ECO:0000256|PIRNR:PIRNR017706}.
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:0000256|ARBA:ARBA00026086}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR017706}.
CC -!- SIMILARITY: Belongs to the TFP11/STIP family.
CC {ECO:0000256|ARBA:ARBA00010900, ECO:0000256|PIRNR:PIRNR017706}.
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DR EMBL; AEYP01066176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3YQ93; -.
DR STRING; 9669.ENSMPUP00000013502; -.
DR Ensembl; ENSMPUT00000013718.1; ENSMPUP00000013502.1; ENSMPUG00000013605.1.
DR eggNOG; KOG2184; Eukaryota.
DR GeneTree; ENSGT00390000012739; -.
DR HOGENOM; CLU_007977_1_1_1; -.
DR InParanoid; M3YQ93; -.
DR OMA; QNEFNPH; -.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IEA:Ensembl.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0071008; C:U2-type post-mRNA release spliceosomal complex; IEA:Ensembl.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0000390; P:spliceosomal complex disassembly; IEA:Ensembl.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR022783; GCFC_dom.
DR InterPro; IPR022159; STIP/TFIP11_N.
DR InterPro; IPR024933; TFP11.
DR InterPro; IPR045211; TFP11/STIP/Ntr1.
DR PANTHER; PTHR23329:SF1; TUFTELIN-INTERACTING PROTEIN 11; 1.
DR PANTHER; PTHR23329; TUFTELIN-INTERACTING PROTEIN 11-RELATED; 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 3: Inferred from homology;
KW Biomineralization {ECO:0000256|ARBA:ARBA00022591};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|PIRNR:PIRNR017706};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW ECO:0000256|PIRNR:PIRNR017706};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR017706};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728, ECO:0000256|PIRNR:PIRNR017706}.
FT DOMAIN 149..195
FT /note="G-patch"
FT /evidence="ECO:0000259|PROSITE:PS50174"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 349..376
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 219..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 881 AA; 101384 MW; 3B2EA3E73002A0A4 CRC64;
MSLSHLYRDG EGHVDDDDDE RENFEITDWD LQNEFNPNRQ RHWQTKEEAT YGVWAERDSD
EERPSFGGKR ARDYSAPVNF ISAGLKKGAA EEAELEDSED EEKPVKQDDF PKDFGPKKLK
TGGNFKPSQK GFAGGTKSFM DFGSWERHTK GIGQKLLQKM GYVPGRGLGK NAQGIINPIE
AKQRKGKGAV GAYGSERTTQ SLQDFPVVDS EEEAEEEFQK ELSQWRKDPS GSKKKPKYSY
KTVEELKAKG RISKKLAAPQ KELSQVKVID MTGREQKVYY SYSQISHKHN VPDDGLPLQS
QQPPQPGKEA KTPGFALPEL EHNLQLLIDL TEQEIIQSDR QLQYERDMVV NLSHELEKMS
EVLEHEERVI ANLSKVLEMV EECERRLQPG CSDPLTLDEC ARVFETLQDK YYEEYRMSDR
VDLAVAIVYP LMKEYFKEWD PLKDCTYGTE VISKWKSLLE NDQLLSHGGQ DLSADAFHRL
IWEVWMPFVR SIVTQWQPRN CDPMVDFLDS WVHIIPVWIL DNILDQLIFP KLQKEVENWN
PLTDTVPIHS WVHPWLPLMQ ARLEPLYSPI RSKLSSALQK WHPSDSSAKL ILQPWKDVFT
PGSWEAFMVK NIVPKLGMCL GELVINPHQQ HMDAFYWVID WEGMISVSSL VGLLEKHFFP
KWLQVLCSWL SNSPNYEEIT KWYLGWKSMF SDQVLAHPSV KDKFNEALDI MNRAVSSNVG
AYMQPGAREN IAYLTHTERR KDFQYEAMQE RREAENMAQR GIGVAASSVP MNFKDLIETK
AEEHNIVFMP VIGKRHEGKQ LYTFGRIVIY IDRGVVFVQG LSGKPPQESP RHSLTGLLCA
CTHLSSSPLK LFPMMSILAR DSTDQLLHKR LLYRAVPQWG M
//
