ID   A0A3B5ASV6_9TELE        Unreviewed;       833 AA.
AC   A0A3B5ASV6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Tuftelin-interacting protein 11 {ECO:0000256|ARBA:ARBA00015137, ECO:0000256|PIRNR:PIRNR017706};
GN   Name=tfip11 {ECO:0000313|RefSeq:XP_008280232.1};
OS   Stegastes partitus (bicolor damselfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Stegastes.
OX   NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000023516.1, ECO:0000313|Proteomes:UP000261400};
RN   [1] {ECO:0000313|Ensembl:ENSSPAP00000023516.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_008280232.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Involved in pre-mRNA splicing, specifically in spliceosome
CC       disassembly during late-stage splicing events.
CC       {ECO:0000256|PIRNR:PIRNR017706}.
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}.
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   RefSeq; XP_008280232.1; XM_008282010.1.
DR   AlphaFoldDB; A0A3B5ASV6; -.
DR   STRING; 144197.ENSSPAP00000023516; -.
DR   Ensembl; ENSSPAT00000023895.1; ENSSPAP00000023516.1; ENSSPAG00000017719.1.
DR   GeneID; 103357449; -.
DR   CTD; 24144; -.
DR   GeneTree; ENSGT00390000012739; -.
DR   OrthoDB; 3060898at2759; -.
DR   Proteomes; UP000261400; Unplaced.
DR   Proteomes; UP000694891; Unplaced.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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   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:UP000694891};
KW   Spliceosome {ECO:0000256|ARBA:ARBA00022728, ECO:0000256|PIRNR:PIRNR017706}.
FT   DOMAIN          153..199
FT                   /note="G-patch"
FT                   /evidence="ECO:0000259|PROSITE:PS50174"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          28..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..68
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..243
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   833 AA;  94547 MW;  309BF28C0C0FA434 CRC64;
     MSMSHLYGRR DEEEEGVEIE SFEVTDWDLA NEFNPDRRRH RQTKEQATYG IWADRDSDED
     ERPSFGGKKS KDYTAPVSFV SAGLRKTAAE EKQQQKGEGD SDDSDEDAPA APPPPRSTAP
     KKLQMGTFRG NQSQRFAGGI QSGQGIGNWE KHTKGIGQKL LQKMGYQPGK GLGKNAQGIV
     NPIEAKVRKG KGAVGAYGNE RTQQSLQDFP VVDSEEEEEK EFQKELGQWR KDPAGPAGKK
     KPKYSYRTAD ELKAKGKVAG RSTAASAGEL AQVKVIDMTG REQKVYYSYS QMSNKHSVPD
     EGPPSMSTRD QKGSGFALPE LEHNLQLLID LTEQDILQSA RRLQHEKDVV VSLSHESRAL
     QNRLDAEQDS IQRMEAVLAL VERFPSAEAA PGEGPSLQEC ARIFETLQTD YYEEYKTMGL
     ADLAVAVVHP LLKEKLCSWD PLKDSSYCLE DIGQWRAILE SRDLLSSGPD SNMDPYHRLL
     WEVWIPVMRT CVSGWQPRMV GPMVDCVEVW APLLPLWILD HILEQLILPR LQREVDNWNP
     LTDTVPIHSW VHPWLPLLQT RLEPLYPPIR SKLSNALQRW HPSDASARLI LQPWKDVFTP
     GAWEAFMVKN IIPKLALCLE ELVINPHQQQ MEPFYWVMDW EGMLSPSSLV SLLDKNFFTK
     WLQVLCSWLS NSPNYEEITK WYLGWKSKFS DVLLAQPLIK EKFNEALDIM NRAVSSGMGG
     YMQPGARENI AYLTQTERRK DFQYEAMQER RDAESVAHRG ISAGVPTNFK DLIQTKAEEN
     NIVFMPLVAK RHEGKQLYTF GRIVIYIDRG VVFVQGEKTW VPTSLQSLID MAK
//