ID F6YQH7_CALJA Unreviewed; 837 AA.
AC F6YQH7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Tuftelin-interacting protein 11 {ECO:0000256|ARBA:ARBA00015137, ECO:0000256|PIRNR:PIRNR017706};
GN Name=TFIP11 {ECO:0000313|EMBL:JAB16805.1,
GN ECO:0000313|Ensembl:ENSCJAP00000016002.1};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000016002.1, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000016002.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB16805.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cerebellum {ECO:0000313|EMBL:JAB42695.1}, Cerebral cortex
RC {ECO:0000313|EMBL:JAB31504.1}, Hippocampus
RC {ECO:0000313|EMBL:JAB16805.1}, and Skeletal muscle
RC {ECO:0000313|EMBL:JAB37268.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
RN [3] {ECO:0000313|Ensembl:ENSCJAP00000016002.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; GAMS01006331; JAB16805.1; -; mRNA.
DR EMBL; GAMR01002428; JAB31504.1; -; mRNA.
DR EMBL; GAMQ01004583; JAB37268.1; -; mRNA.
DR EMBL; GAMP01010060; JAB42695.1; -; mRNA.
DR RefSeq; XP_009006562.1; XM_009008314.2.
DR RefSeq; XP_009006567.1; XM_009008319.2.
DR RefSeq; XP_009006571.1; XM_009008323.2.
DR STRING; 9483.ENSCJAP00000016002; -.
DR Ensembl; ENSCJAT00000016907.4; ENSCJAP00000016002.1; ENSCJAG00000008628.4.
DR GeneID; 100401065; -.
DR KEGG; cjc:100401065; -.
DR CTD; 24144; -.
DR eggNOG; KOG2184; Eukaryota.
DR GeneTree; ENSGT00390000012739; -.
DR HOGENOM; CLU_007977_1_1_1; -.
DR OMA; QNEFNPH; -.
DR OrthoDB; 3060898at2759; -.
DR TreeFam; TF314887; -.
DR Proteomes; UP000008225; Chromosome 1.
DR Bgee; ENSCJAG00000008628; Expressed in cerebellum and 6 other cell types or tissues.
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 2: Evidence at transcript level;
KW Biomineralization {ECO:0000256|ARBA:ARBA00022591};
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 Reference proteome {ECO:0000313|Proteomes:UP000008225};
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 177..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 837 AA; 96849 MW; F3C89AA974DBC4BD CRC64;
MSLSHLYRDG EDRIDDDDDE RENFEITDWD LQNEFNPNRQ RHWQTKEEAT YGVWAERDSD
EERPSFGGKR ARDYSAPVNF ISAGLKKGAA EEAELEDSDD EETPVKQDDF PKDFGPKKLK
TGGNFKPSQK GFAGGTKSFM DFGSWERHTK GIGQKLLQKM GYVPGRGLGK NAQGIINPIE
AKQRKGKGAV GAYGSERTTQ SVQDFPVVDS EEEAEEEFQK ELSQWRKDPS GSKKKPKYSY
KTVEELKAKG RISKKLTAPQ KELSQVKVID MTGREQKVYY SYSQISHKHN VPDDGLPLQS
QQLPQSGKEA KAPGFALPEL EHNLQLLIDL TEQEIIQNDR QLQYERDMVV NLFHELEKMT
EVLDHEERVI SNLSKVLEMV EECERRMQPD CSNPLTLDEC ARIFETLQDK YYEEYRMSDR
VDLAVAIVYP LMKEYFKEWD PLKDCTYGTE IISKWKSLLE NDQLLSHGGQ DLSADAFHRL
IWEVWMPFVR NIVTQWQPRN CDPMVDFLDS WVHIIPVWIL DNILDQLIFP KLQKEVENWN
PLTDTVPIHS WIHPWLPLMQ ARLEPLYSPI RSKLSSALQK WHPSDSSAKL ILQPWKDVFT
PGSWEAFMVK NIVPKLGMCL GELVINPHQQ HMDAFYWVID WEGMISVSSL VGLLEKHFFP
KWLQVLCSWL SNSPNYEEIT KWYLGWKSMF SDQVLAHPSV KDKFNEALDI MNRAVSSNVG
AYMQPGAREN IAYLTHTERR KDFQYEAMQE RREAENMAQR GIGVATSSVP MNFKDLIETK
AEEHNIVFMP IIGKRHEGKQ LYTFGRIVIY IDRGVVFVQG EKTWVPTSLQ SLIDMAK
//
