TFP11_MONDO
ID TFP11_MONDO Reviewed; 834 AA.
AC A4UMC6;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
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 Monodelphis domestica (Gray short-tailed opossum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX NCBI_TaxID=13616;
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; EF443270; ABP04113.1; -; mRNA.
DR RefSeq; NP_001091078.1; NM_001097609.1.
DR RefSeq; XP_007490114.1; XM_007490052.2.
DR RefSeq; XP_007490115.1; XM_007490053.2.
DR AlphaFoldDB; A4UMC6; -.
DR SMR; A4UMC6; -.
DR STRING; 13616.ENSMODP00000013420; -.
DR Ensembl; ENSMODT00000013666; ENSMODP00000013420; ENSMODG00000010710.
DR GeneID; 100010097; -.
DR KEGG; mdo:100010097; -.
DR CTD; 24144; -.
DR eggNOG; KOG2184; Eukaryota.
DR GeneTree; ENSGT00390000012739; -.
DR HOGENOM; CLU_007977_1_1_1; -.
DR InParanoid; A4UMC6; -.
DR OMA; EFFPKWH; -.
DR OrthoDB; 1238995at2759; -.
DR TreeFam; TF314887; -.
DR Proteomes; UP000002280; Chromosome 3.
DR Bgee; ENSMODG00000010710; Expressed in extraembryonic membrane and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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..834
FT /note="Tuftelin-interacting protein 11"
FT /id="PRO_0000342273"
FT DOMAIN 148..194
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..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..731
FT /note="Required for nuclear speckle localization"
FT /evidence="ECO:0000250"
FT MOTIF 697..702
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U2Y6"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBB9"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBB9"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBB9"
SQ SEQUENCE 834 AA; 96427 MW; 065997A421C939A9 CRC64;
MSLSHLYREG EGAIDEEEDE MENFEITDWD LQNEFNPNRQ RHWQTKEEAT YGVWAERELE
DERPSFGGKR SRDFSAPVNF ISAGLKKAAD EADEEDSDEE EKPIKQEDFP KDFGPKKLKT
GGNFKPSQKG FVGGAKSFTD FGSWERHTKG IGQKLLQKMG YVPGKGLGKN AQGIINPIEA
KQRKGKGAVG AYGSERTTQS VQDFPVVDSE EEAEEEFQKE LSQWRKDPSG GKKKPKYSYK
TVEELKAKGR IGKKLSAPQK ELSQVKVIDM TGREQKVYYS YSQISHKHNI PEDGLQQQQL
PLPGKDAKPQ AFALPELEHN LQLLIDITEQ EIIQNDRQLQ YERDMVVNLS HELEKMSEVL
SHEETVITNL SKVLEMVEEC ERRMQPDCSD PLTLDECARI FETLQEKYYE EYRMSDRVDL
AVAIVYPLMK DYFKDWDPLK DCTYGTGIIA KWKSLLENDQ ILSHGGQDLA ADAFHRLIWE
MWMPFVRNIV TQWQPRNCDP MVDFLDSWVH IIPVWILDNI LDQLIFPKLQ KEVENWNPLT
DTVPIHSWIH PWLPLMQSRL EPLYSPIRNK LSSALQKWHP SDSSAKLILQ PWKDVFTPGS
WEAFMVKNIV PKLGMCLNEL IINPHQQHMD AFYWVIDWEG MISVSSLVGL LEKHFFPKWL
QVLCSWLSNS PNYEEITKWY LGWKSMFSDQ VLAHPSIKDK FNEALDIMNR AVSSNVGAYM
QPGARENIAY LTHTERRKDF QYEAMQERRE AENMAQRGIG MAASSVPMNF KDLIQTKAEE
HNIVFMPVIG KRHEGKQLYT FGRIVVYIDR GVVFVQGEKT WVPTSLQSLI DMAK
