TFP11_RAT
ID TFP11_RAT Reviewed; 837 AA.
AC Q5U2Y6;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
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=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-95; SER-98 AND
RP SER-210, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; DQ342031; ABC69923.1; -; mRNA.
DR EMBL; BC085809; AAH85809.1; -; mRNA.
DR RefSeq; NP_001008292.1; NM_001008291.1.
DR AlphaFoldDB; Q5U2Y6; -.
DR IntAct; Q5U2Y6; 1.
DR STRING; 10116.ENSRNOP00000000828; -.
DR iPTMnet; Q5U2Y6; -.
DR PhosphoSitePlus; Q5U2Y6; -.
DR jPOST; Q5U2Y6; -.
DR PaxDb; Q5U2Y6; -.
DR PRIDE; Q5U2Y6; -.
DR Ensembl; ENSRNOT00000000828; ENSRNOP00000000828; ENSRNOG00000000663.
DR GeneID; 288718; -.
DR KEGG; rno:288718; -.
DR CTD; 24144; -.
DR RGD; 1311449; Tfip11.
DR eggNOG; KOG2184; Eukaryota.
DR GeneTree; ENSGT00390000012739; -.
DR HOGENOM; CLU_007977_1_1_1; -.
DR InParanoid; Q5U2Y6; -.
DR OMA; EFFPKWH; -.
DR OrthoDB; 1238995at2759; -.
DR PhylomeDB; Q5U2Y6; -.
DR TreeFam; TF314887; -.
DR PRO; PR:Q5U2Y6; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000000663; Expressed in testis and 19 other tissues.
DR Genevisible; Q5U2Y6; RN.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:RGD.
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 1: Evidence at protein 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_0000342278"
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..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 34..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..135
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 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 40..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..116
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:0007744|PubMed:22673903"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBB9"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBB9"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 837 AA; 96152 MW; 512828055F41B243 CRC64;
MSLSHLYRDG EGHLDDDDDE RENFEITDWD LQNEFNPNRQ RHWQTKEEAT YGVWAERDSD
EERPSFGGKR ARDYSAPVNF ISAGLKKGAA EEADSEDSDA EEKPVKQEDF PKDLGPKKLK
TGGNFKPSQK GFAGGTKSFM DFGSWERHTK GIGQKLLQKM GYVPGRGLGK NAQGIINPIE
AKQRKGKGAV GAYGSERTTQ SLQDFPVADS EEEAEEEFQK ELSQWRKDPS GSKKKPKYSY
KTVEELKAKG RVSKKLTAPQ KELSQVKVID MTGREQKVYY SYSQISHKHS VPDEGVPLLA
QLPPTAGKEA KVPGFALPEL EHNLQLLIER TEQEIIQSDR QLQYERDMVV SLSHELEKTA
EVLAHEERVI SNLSKVLALV EECEHRMQPH GADPLTLDEC ARIFETLQDK YYEEYRLADR
ADLAVAIVYP LVKDYFKDWH PLEDSNYGTQ IISKWKSLLE NDQLLSHSSQ DLSSDAFHRL
MWEVWMPFVR NVVAQWQPRN CEPMVDFLDS WAHIIPVWIL DNILDQLIFP KLQKEVDNWN
PLTDTVPIHS WIHPWLPLMQ ARLEPLYSPV RSKLSSALQK WHPSDASAKL ILQPWKEVLT
PGSWEAFMLR NIVPKLGMCL GELVINPHQQ HMDAFYWVMD WEGMISVSSL VGLLEKHFFP
KWLQVLCSWL SNSPNYEEIT KWYLGWKSMF SDQVLAHPSV KDKFNEALDI MNRAVSSNVG
AYMQPGAREN IAYLTHTERR KDFQYEAMQE RREAENMAQR GIGVAASSVP MNFKDLIETK
AEEHNIVFMP VIGKRHEGKQ LYTFGRIVIY IDRGVVFVQG EKTWVPTSLQ SLIDMAK
