TFP11_BOVIN
ID TFP11_BOVIN Reviewed; 837 AA.
AC Q29RR5; A1XD96;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 25-MAY-2022, entry version 83.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
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 STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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 EMBL; DQ342029; ABC69921.1; -; mRNA.
DR EMBL; BC114058; AAI14059.1; -; mRNA.
DR RefSeq; NP_001039495.2; NM_001046030.2.
DR AlphaFoldDB; Q29RR5; -.
DR SMR; Q29RR5; -.
DR STRING; 9913.ENSBTAP00000016296; -.
DR PaxDb; Q29RR5; -.
DR PRIDE; Q29RR5; -.
DR GeneID; 509349; -.
DR KEGG; bta:509349; -.
DR CTD; 24144; -.
DR eggNOG; KOG2184; Eukaryota.
DR InParanoid; Q29RR5; -.
DR OrthoDB; 1238995at2759; -.
DR Proteomes; UP000009136; Unplaced.
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..837
FT /note="Tuftelin-interacting protein 11"
FT /id="PRO_0000342269"
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 287..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..734
FT /note="Required for nuclear speckle localization"
FT /evidence="ECO:0000250"
FT MOTIF 700..705
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 COMPBIAS 296..311
FT /note="Pro 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"
FT CONFLICT 133
FT /note="A -> V (in Ref. 2; AAI14059)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="S -> A (in Ref. 1; ABC69921)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="C -> Y (in Ref. 1; ABC69921)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="L -> Q (in Ref. 2; AAI14059)"
FT /evidence="ECO:0000305"
FT CONFLICT 711
FT /note="M -> K (in Ref. 2; AAI14059)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 837 AA; 96085 MW; D3A148A4C13FFF7E 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 RISKKLTAPQ KELSQVKVID MTGREQKVYY SYSQISHKHS VPDDGLPPQA
QPPPPPGKEA RAPGFALPEL EHNLQLLIEL TEQEIIRNDR QLQYERDVVV NLTHELEKAS
GALQQEQRAI ASLSEVLALV EECERRLQPG CSDPLTLDEC ARVFQTLRDK YYEEYRMSDR
VDLAVAIVYP LMKDYFKEWD PLKDCTYGTE TISQWKSLLE NDQLLSHGGQ DLSADAFHRL
IWEVWMPFVR SIVAQWQPRN CDPMVDFLDS WAPLIPVWVL DNILEQLIFP KLQKEVESWN
PLTDTVPIHS WVHPWLPLMQ ARLEPLYSPI RSKLASALQK WHPSDSSAKL ILQPWKDVFT
PGSWEAFMVK NIVPKLGMCL GELVINPHQQ HMDAFYWVID WEGMVSVSSL VGLLEKHFFP
KWLQVLCSWL SNSPNYEEIT KWYLGWKSMF SDQVLAHPSV KDKFNEALDI MNRAVSSNVG
AYMQPGAREH IAYLTHTERR KDFQYEAMQE RREAENMAQR GIGVAASAVP MNFKDLIETK
AEEHNIVFMP VIGKRHEGKQ LYTFGRIVIY IDRGVVFVQG EKTWVPTSLQ SLIDMAK
