ID A0A096NRG4_PAPAN Unreviewed; 837 AA.
AC A0A096NRG4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Tuftelin-interacting protein 11 {ECO:0000256|ARBA:ARBA00015137, ECO:0000256|PIRNR:PIRNR017706};
GN Name=TFIP11 {ECO:0000313|Ensembl:ENSPANP00000015634.2};
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000015634.2, ECO:0000313|Proteomes:UP000028761};
RN [1] {ECO:0000313|Ensembl:ENSPANP00000015634.2, ECO:0000313|Proteomes:UP000028761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT "Whole Genome Assembly of Papio anubis.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPANP00000015634.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A096NRG4; -.
DR STRING; 9555.ENSPANP00000015634; -.
DR Ensembl; ENSPANT00000026788.3; ENSPANP00000015634.2; ENSPANG00000018711.3.
DR eggNOG; KOG2184; Eukaryota.
DR GeneTree; ENSGT00390000012739; -.
DR HOGENOM; CLU_007977_1_1_1; -.
DR OMA; QNEFNPH; -.
DR OrthoDB; 3060898at2759; -.
DR Proteomes; UP000028761; Chromosome 16.
DR Bgee; ENSPANG00000018711; Expressed in lateral hypothalamic nucleus and 66 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 3: Inferred from homology;
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:UP000028761};
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 38..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..69
FT /note="Basic and acidic residues"
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; 96821 MW; D00FE301A5F9D785 CRC64;
MSLSHLYRDG EGRIDDDDDE RENFEITDWD LQNEFNPNRQ RHWQTKEEAT YGVWAERDSD
DERPSFGGKR ARDYSAPVSF ISAGLKKGAA EEAELEDSDD EERPVKQDDF PKDFGPRKLK
TGGNFKPSQK GFAGGTKSFM DFGSWERHTK GIGQKLLQKM GYVPGRGLGK NAQGIINPIE
AKQRKGKGAV GAYGSERTTQ SMQDFPVVDS 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 GIGVAASSVP MNFKDLIETK
AEEHNIVFMP VIGKRHEGKQ LYTFGRIVIY IDRGVVFVQG EKTWVPTSLQ SLIDMAK
//
