TFP11_PIG
ID TFP11_PIG Reviewed; 836 AA.
AC Q06AK6;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
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).
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 (By similarity). {ECO:0000250}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=In the nucleus localizes to unique speckle domains in close
CC proximity to nuclear speckles and not identical to paraspeckles.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TFP11/STIP family. {ECO:0000305}.
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DR EMBL; DQ923315; ABI95149.1; -; mRNA.
DR RefSeq; NP_001070682.1; NM_001077214.1.
DR AlphaFoldDB; Q06AK6; -.
DR SMR; Q06AK6; -.
DR STRING; 9823.ENSSSCP00000010632; -.
DR PaxDb; Q06AK6; -.
DR PeptideAtlas; Q06AK6; -.
DR PRIDE; Q06AK6; -.
DR Ensembl; ENSSSCT00000010917; ENSSSCP00000010632; ENSSSCG00000009962.
DR Ensembl; ENSSSCT00005041345; ENSSSCP00005025280; ENSSSCG00005025953.
DR Ensembl; ENSSSCT00005041383; ENSSSCP00005025306; ENSSSCG00005025953.
DR Ensembl; ENSSSCT00005041415; ENSSSCP00005025327; ENSSSCG00005025953.
DR Ensembl; ENSSSCT00025059673; ENSSSCP00025025312; ENSSSCG00025043966.
DR Ensembl; ENSSSCT00030050869; ENSSSCP00030023134; ENSSSCG00030036572.
DR Ensembl; ENSSSCT00035045312; ENSSSCP00035018124; ENSSSCG00035034188.
DR Ensembl; ENSSSCT00040022063; ENSSSCP00040009223; ENSSSCG00040016403.
DR Ensembl; ENSSSCT00045027924; ENSSSCP00045019314; ENSSSCG00045016417.
DR Ensembl; ENSSSCT00050008832; ENSSSCP00050003792; ENSSSCG00050006451.
DR Ensembl; ENSSSCT00055043959; ENSSSCP00055035011; ENSSSCG00055022375.
DR Ensembl; ENSSSCT00060075747; ENSSSCP00060032738; ENSSSCG00060055577.
DR Ensembl; ENSSSCT00065022741; ENSSSCP00065009228; ENSSSCG00065017108.
DR Ensembl; ENSSSCT00070002293; ENSSSCP00070001915; ENSSSCG00070001218.
DR Ensembl; ENSSSCT00070002302; ENSSSCP00070001923; ENSSSCG00070001218.
DR Ensembl; ENSSSCT00070002337; ENSSSCP00070001957; ENSSSCG00070001218.
DR GeneID; 768099; -.
DR KEGG; ssc:768099; -.
DR CTD; 24144; -.
DR VGNC; VGNC:109426; TFIP11.
DR eggNOG; KOG2184; Eukaryota.
DR GeneTree; ENSGT00390000012739; -.
DR InParanoid; Q06AK6; -.
DR OMA; EFFPKWH; -.
DR OrthoDB; 1238995at2759; -.
DR Proteomes; UP000008227; Chromosome 14.
DR Proteomes; UP000314985; Chromosome 14.
DR Bgee; ENSSSCG00000009962; Expressed in oocyte and 42 other tissues.
DR ExpressionAtlas; Q06AK6; baseline and differential.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IEA:Ensembl.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0005681; C:spliceosomal complex; ISS:UniProtKB.
DR GO; GO:0071008; C:U2-type post-mRNA release spliceosomal complex; ISS:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0000390; P:spliceosomal complex disassembly; ISS:UniProtKB.
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 Biomineralization; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Spliceosome.
FT CHAIN 1..836
FT /note="Tuftelin-interacting protein 11"
FT /id="PRO_0000342275"
FT DOMAIN 149..195
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT REGION 1..50
FT /note="Required for interaction with DHX15"
FT /evidence="ECO:0000250"
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..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..733
FT /note="Required for nuclear speckle localization"
FT /evidence="ECO:0000250"
FT MOTIF 699..704
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 54..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"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U2Y6"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBB9"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBB9"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBB9"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBB9"
SQ SEQUENCE 836 AA; 96501 MW; D23C681963CF06FB CRC64;
MSLSHLYRDG EGHMDDDEDE RENFEITDWD LQNEFNPNRQ RHWQTKEEAT YGVWAERDSD
EERPSFGGKR ARDYSAPVNF ISAGLKKGAA EEAELEDSDD EEKPVKQDEF PKDFGPKKLK
TGGNFKPSQK GFAGGTKSFM DFGSWERHTK GIGQKLLQKM GYVPGRGLGK NAQGIINPIE
AKQRKGKGAV GAYGSERTTQ SLQDFPVVDS EEEAEEEFQK ELSQWRKDPS GSKKKPKYSY
KTVEELKAKG RISKKLSAPQ KEISQVKVID MTGREQKVYY SYSQISHKHN VPDDGLPLQS
QLPQPGKEAK APGFALPELE HNLQLLIELT EQEIIQNDRQ LQYERDMVVN LSHELEKMAE
VLEHEERVIS NLSKVLEMVE ECERRLQPGC SNPLTLDECA RIFETLQDKY YEEYRMSDRV
DLAVAIVYPL MKDYFKEWDP LKDCTYGTEI ISKWKSLLEN DQLLSHGGQD LSADAFHRLI
WEVWMPFVRN IVTQWQPRNC DPMVDFLDSW VHIIPVWILD NILDQLVFPK LQKEVENWNP
LTDTVPIHSW IHPWLPLMQA RLEPLYSPIR SKLASALQKW HPSDSSAKLI LQPWKDVFTP
GSWEAFMVKN IVPKLGMCLG ELVINPHQQH MDAFYWVIDW EGMISVSSLV GLLEKHFFPK
WLQVLCSWLS NSPNYEEITK WYLGWKSMFS DQVLAHPSVK DKFNEALDIM NRAVSSNVGA
YMQPGARENI AYLTHTERRK DFQYEAMQER REAENMAQRG IGVAASSVPM NFKDLIETKA
EEHNIVFMPV IGKRHEGKQL YTFGRIVIYI DRGVVFVQGE KTWVPTSLQS LIDMAK
