TFP11_MACFA
ID TFP11_MACFA Reviewed; 837 AA.
AC A1XD95; Q4R9D5;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 51.
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; ORFNames=QtsA-10256;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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] (ISOFORM 2).
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A1XD95-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A1XD95-2; Sequence=VSP_034413;
CC -!- SIMILARITY: Belongs to the TFP11/STIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE00286.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ342028; ABC69920.1; -; mRNA.
DR EMBL; AB168161; BAE00286.1; ALT_FRAME; mRNA.
DR AlphaFoldDB; A1XD95; -.
DR SMR; A1XD95; -.
DR STRING; 9541.XP_005567787.1; -.
DR eggNOG; KOG2184; Eukaryota.
DR Proteomes; UP000233100; 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 Alternative splicing; Biomineralization; Cytoplasm; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Spliceosome.
FT CHAIN 1..837
FT /note="Tuftelin-interacting protein 11"
FT /id="PRO_0000342271"
FT DOMAIN 149..195
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..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 53..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..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"
FT VAR_SEQ 18..59
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_034413"
SQ SEQUENCE 837 AA; 96774 MW; AB95991105703273 CRC64;
MSLSHLYRDG EGRIDDDDDE RENFEITDWD LQNEFNPNRQ RHWQTKEEAT YGVWAERDSD
DERPSFGGKR ARDYSAPVNF ISAGLKKGAA EEAELEDSDD EERPVKQDDF PKDFGPRKLK
TGGNFKPSQK GFAGGTKSFM DFGSWERHTK GIGQKLLQKM GYVPGRGLGK NAQGIINPIE
AKQRKGKGAV GAYGSERTTQ SMQDFPVVDS EEEAEEEFQK GLSQWRKDPS GSKKKPKYSY
KTVEELKAKG RISKKLTAPQ KELSQVKVID MTGREQKVYY SYSQISHKHN VPDDGLPLQS
QQLPQSGKEA KAPGFALPEL EHNLQLLIDL TEQEIIQNDR QLQYERDMVV NLFHELEKMT
EVLDHEERVI SNLSKVLEMV EECERRMQPD CSNPLTLDEC ARIFETLQDK YYEEYRMSDR
VDLAVAIVYP LMKEYFKEWD PLKDCTYGTE IISKWKSLLE NDQLLSHGGQ DLSADAFHRL
IWEVWMPFVR NIVTQWQPRN CDPMVDFLDS WVHIIPVWIL DNILDQLIFP KLQKEVENWN
PLTDTVPIHS WIHPWLPLMQ ARLEPLYSPI RSKLSSALQK WHPSDSSAKL ILQPWKDVFT
PGSWEAFMVK NIVPKLGMCL GELVINPHQQ HMDAFYWVID WEGMISVSSL VGLLEKHFFP
KWLQVLCSWL SNSPNYEEIT KWYLGWKSMF SDQVLAHPSV KDKFNEALDI MNRAVSSNVG
AYMQPGAREN IAYLTHTERR KDFQYEATRE RREAENMAQR GIGVAASSVP MNFKDLIETK
AEEHNIVFMP VIGKRHEGKQ LYTFGRIVIY IDRGVVFVQG EKTWVPTSLQ SLIDMAK
