ID W5NSZ6_SHEEP Unreviewed; 833 AA.
AC W5NSZ6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Tuftelin-interacting protein 11 {ECO:0000256|ARBA:ARBA00015137, ECO:0000256|PIRNR:PIRNR017706};
GN Name=TFIP11 {ECO:0000313|Ensembl:ENSOARP00000001286.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000001286.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000001286.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000001286.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000001286.1}
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; AMGL01039711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01039712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01039713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01039714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5NSZ6; -.
DR SMR; W5NSZ6; -.
DR STRING; 9940.ENSOARP00000001286; -.
DR PaxDb; 9940-ENSOARP00000001286; -.
DR Ensembl; ENSOART00000001326.1; ENSOARP00000001286.1; ENSOARG00000001236.1.
DR eggNOG; KOG2184; Eukaryota.
DR HOGENOM; CLU_007977_1_1_1; -.
DR OMA; QNEFNPH; -.
DR Proteomes; UP000002356; Chromosome 17.
DR Bgee; ENSOARG00000001236; Expressed in adrenal cortex and 54 other cell types or tissues.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0000390; P:spliceosomal complex disassembly; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000002356};
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..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 346..373
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 54..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 833 AA; 95348 MW; 905FBEEAF1D6268A CRC64;
MSLSHLYRDG EGHMDDDEDE RENFEITDWD LQNEFNPNRQ RHWQTKEEAT YGVWAERDSD
EERPSFGGKR ARDYSAPVNF ISAGLKKGAA EEAELEDSDD EEKPVKQDEF PKDFGPKKLK
TGGNFKPSQK GFAGGTKSFM DFGSWERHTK GIGQKLLQKM GYVPGRGLGK NAQGIINPIE
AKQRKGKGAA GSERTTQSLQ DFPVVDSEEE AEEEFQKELS QWRKDPSGSK KKPKYSYKTV
EELKAKGRIS KKLTAPQKEL SQVKVIDMTG REQKVYYSYS QISHKHGVPD DGLPPQAQPP
PLPGKEARAP GFALPELEHN LQLLIELTEQ EIIRNDRQLQ YERDVVVNLT HELEKAAGAL
QQEQRAIASL SEVLALVEEC ERRLQPGCSD PLTLDECARV FQTLRDKYYE EYRMSDRVDL
AVAIVYPLMK DYFKEWDPLK DCTYGIETIS QWKSLLENDQ LLSHGGQDLS ADAFHRLIWE
VWMPFVRSII AQWQPRNCDP MVDFLDSWAP LIPVWVLDNI LEQLIFPKLQ KEVESWNPLT
DTVPIHSWVH PWLPLMQARL EPLYSPIRSK LASALQKWHP SDSSAKLILQ PWKDVFTPGS
WEAFMVKNIV PKLGMCLGEL VINPHQQHMD AFYWAIDWEG MVSVSSLVGL LEKHFFPKWL
QVLCSWLSNS PNYEEITKWY LGWKSMFSDQ VLAHPSVKDK FNEALDIMNR AVSSNVGAYM
QPGAREHIAY LTHTERRKDF QYEAMQERRE AGGAGGAGGW AASAVPMNFK DLIETKAEEH
NIVFMPVIGK RHEGKQLYTF GRIVIYIDRG VVFVQGEKTW VPTSLQSLID MAK
//
