TFP11_XENLA
ID TFP11_XENLA Reviewed; 824 AA.
AC Q66J74;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Tuftelin-interacting protein 11;
DE AltName: Full=Septin and tuftelin-interacting protein 1;
DE Short=STIP-1;
GN Name=tfip11; Synonyms=stip;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=17289020; DOI=10.1016/j.yexcr.2007.01.003;
RA Ji Q., Huang C.-H., Peng J., Hashmi S., Ye T., Chen Y.;
RT "Characterization of STIP, a multi-domain nuclear protein, highly conserved
RT in metazoans, and essential for embryogenesis in Caenorhabditis elegans.";
RL Exp. Cell Res. 313:1460-1472(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in pre-mRNA splicing, specifically in spliceosome
CC disassembly during late-stage splicing events. {ECO:0000250}.
CC -!- SUBUNIT: Identified in the spliceosome C complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TFP11/STIP family. {ECO:0000305}.
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DR EMBL; DQ342033; ABC69925.1; -; mRNA.
DR EMBL; BC081033; AAH81033.1; -; mRNA.
DR RefSeq; NP_001087642.1; NM_001094173.1.
DR AlphaFoldDB; Q66J74; -.
DR SMR; Q66J74; -.
DR DNASU; 447466; -.
DR GeneID; 447466; -.
DR KEGG; xla:447466; -.
DR CTD; 447466; -.
DR Xenbase; XB-GENE-984527; tfip11.L.
DR OrthoDB; 1238995at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 447466; Expressed in oocyte and 19 other tissues.
DR GO; GO:0005681; C:spliceosomal complex; ISS:UniProtKB.
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; IPR024933; STIP.
DR InterPro; IPR022159; STIP/TFIP11_N.
DR InterPro; IPR045211; TFP11/STIP/Ntr1.
DR PANTHER; PTHR23329; PTHR23329; 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 mRNA processing; mRNA splicing; Nucleus; Reference proteome; Spliceosome.
FT CHAIN 1..824
FT /note="Tuftelin-interacting protein 11"
FT /id="PRO_0000342281"
FT DOMAIN 145..191
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT REGION 1..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 824 AA; 95245 MW; 85B6B494770FFD8A CRC64;
MSMSHLYGKD EDSDGVEMEN FEITDWDLQN EFNPNRRKHF QTKEEATYGM WAEHDSDDER
PSFGGKRSRD YSAPVNFISA GIRKPAAEEK SDSDSDSETQ SRRENFPKDF EAKKLRTGGN
FKPSQRTFAG GIKSNTDFGS WERHTKGIGQ KLLQKMGYMP GRGLGKNAQG IIAPIEAKQR
RGKGAVGAYG SERTKQSIKD FPVVDSEEEE EKDFQKEMSQ WRKEPGGGKK KPKYSYKTVE
ELKAKGRVGK SLSAPQKEIS QVKVIDMTGR EQKVYYSYSQ LAQKHNIPGE APGQGVKEEK
PQGFALPELE HNLQLLIDMT EQEIIQNDRQ LQYEQDMVVN LTHELEKLSE VLEREDKAIE
NLSKVLETVE ECERRIQPTC DNPLTLEECA RIFEMLQDKY YEEYKMSEKA DLSVAIVYPL
MKDYFKDWNP LRDPNYGTDV MSKWKNLLEE GHLSHSAHDA AMDPYHRLLW EMWVPFLRNI
IAQWQPRNCA PMADFLDSWV HLLPVWILDN ILDQLIFPKL QKEVENWNPL TDTVPIHSWI
HPWLPMMQSR LEPLFSPIRN KLSNALQKWH PSDSSAKLIL QPWKEVFTPG SWEAFMVKNI
VPKLGMCLSE FVINPHQQHM EVFHWVTDWE GMVALSSIVG LLEKHFFPKW LQVLCSWLSN
NPNYEEITKW YLGWKSMFSD LVLAHPAIKD KFNEALDIMN RAVSSSVGAY MQPGARESIA
YLTQTEKRKD FQYEAMQERR DAESIAQRGI GAAAAVPMNF KDLIQSKAEE HNIVFMPLIG
KRHEGKQLYN FNRIVIYIDR GVVFVQGEKT WVPTSLQSLI DMAK