STIP1_ARATH
ID STIP1_ARATH Reviewed; 849 AA.
AC Q9SHG6; Q56W84; Q8LEM9;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Septin and tuftelin-interacting protein 1 homolog 1 {ECO:0000303|PubMed:23110899};
DE AltName: Full=Nineteen complex-related protein 1 homolog {ECO:0000303|PubMed:25568310};
DE Short=AtNTR1 {ECO:0000303|PubMed:25568310};
DE AltName: Full=Protein SPLICEOSOMAL TIMEKEEPER LOCUS 1 {ECO:0000303|PubMed:23110899};
GN Name=STIPL1 {ECO:0000303|PubMed:23110899};
GN Synonyms=NTR1 {ECO:0000303|PubMed:25568310};
GN OrderedLocusNames=At1g17070 {ECO:0000312|Araport:AT1G17070};
GN ORFNames=F20D23.23 {ECO:0000312|EMBL:AAD50023.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 704-849.
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=23110899; DOI=10.1105/tpc.112.104828;
RA Jones M.A., Williams B.A., McNicol J., Simpson C.G., Brown J.W.,
RA Harmer S.L.;
RT "Mutation of Arabidopsis spliceosomal timekeeper locus1 causes circadian
RT clock defects.";
RL Plant Cell 24:4066-4082(2012).
RN [6]
RP FUNCTION, INTERACTION WITH ILP1, AND SUBCELLULAR LOCATION.
RX PubMed=25568310; DOI=10.15252/embj.201489478;
RA Dolata J., Guo Y., Kolowerzo A., Smolinski D., Brzyzek G., Jarmolowski A.,
RA Swiezewski S.;
RT "NTR1 is required for transcription elongation checkpoints at alternative
RT exons in Arabidopsis.";
RL EMBO J. 34:544-558(2015).
CC -!- FUNCTION: Involved in pre-mRNA splicing, specifically in spliceosome
CC disassembly during late-stage splicing events (By similarity). Involved
CC in snRNPs recycling (PubMed:25568310). Required for efficient splicing
CC of genes that act within the plant circadian clock (PubMed:23110899).
CC Part of a transcription elongation checkpoint at alternative exons
CC (PubMed:25568310). Required for correct expression and splicing of
CC DOG1, a regulator of seed dormancy (PubMed:25568310). May induce
CC transient transcriptional pausing of polymerase II at slices sites
CC (PubMed:25568310). {ECO:0000250|UniProtKB:Q9UBB9,
CC ECO:0000269|PubMed:23110899, ECO:0000269|PubMed:25568310}.
CC -!- SUBUNIT: Identified in the spliceosome C complex (By similarity).
CC Interacts with ILP1 (PubMed:25568310). {ECO:0000250|UniProtKB:Q9UBB9,
CC ECO:0000269|PubMed:25568310}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23110899,
CC ECO:0000269|PubMed:25568310}. Note=Excluded from the nucleolus. Co-
CC localizes with polymerase II. {ECO:0000269|PubMed:25568310}.
CC -!- DISRUPTION PHENOTYPE: Long circadian-period phenotype under free-
CC running conditions. {ECO:0000269|PubMed:23110899}.
CC -!- MISCELLANEOUS: Physically located at the target splice sites.
CC {ECO:0000269|PubMed:25568310}.
CC -!- SIMILARITY: Belongs to the TFP11/STIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM62572.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AK228772; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD95266.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC007651; AAD50023.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29537.1; -; Genomic_DNA.
DR EMBL; AK222163; BAD95266.1; ALT_INIT; mRNA.
DR EMBL; AK228772; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY085341; AAM62572.1; ALT_INIT; mRNA.
DR PIR; E86306; E86306.
DR RefSeq; NP_173150.1; NM_101567.3.
DR AlphaFoldDB; Q9SHG6; -.
DR SMR; Q9SHG6; -.
DR STRING; 3702.AT1G17070.1; -.
DR PaxDb; Q9SHG6; -.
DR PRIDE; Q9SHG6; -.
DR ProteomicsDB; 228421; -.
DR EnsemblPlants; AT1G17070.1; AT1G17070.1; AT1G17070.
DR GeneID; 838277; -.
DR Gramene; AT1G17070.1; AT1G17070.1; AT1G17070.
DR KEGG; ath:AT1G17070; -.
DR Araport; AT1G17070; -.
DR TAIR; locus:2020332; AT1G17070.
DR eggNOG; KOG2184; Eukaryota.
DR HOGENOM; CLU_007977_1_0_1; -.
DR InParanoid; Q9SHG6; -.
DR OMA; EFFPKWH; -.
DR OrthoDB; 1238995at2759; -.
DR PhylomeDB; Q9SHG6; -.
DR PRO; PR:Q9SHG6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SHG6; baseline and differential.
DR Genevisible; Q9SHG6; AT.
DR GO; GO:0031981; C:nuclear lumen; IDA:TAIR.
DR GO; GO:0071008; C:U2-type post-mRNA release spliceosomal complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:1990446; F:U1 snRNP binding; IDA:TAIR.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:TAIR.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:TAIR.
DR GO; GO:0000390; P:spliceosomal complex disassembly; IBA:GO_Central.
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 Coiled coil; DNA-binding; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Spliceosome.
FT CHAIN 1..849
FT /note="Septin and tuftelin-interacting protein 1 homolog 1"
FT /id="PRO_0000429430"
FT DOMAIN 200..245
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 354..401
FT /evidence="ECO:0000255"
FT MOTIF 60..75
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 156..186
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 849 AA; 96884 MW; 9900CCA70667E464 CRC64;
MDEYQDMERF SMDNDYEGGR WEGDEFVYQK RKEKRKQTKN DATYGIFAES DSDSDDSGGG
GSRRKRRKDR DSGRKADLTK PVNFVSTGTV MPNQEIDKDS REHNDEKDRD KIEDNDMIDE
DVEVRGGLGI GSSGLGLGFN ANGFDDEDNL LPGALGKKIA DRAKMRGKAK VEKRGQEGGG
AKGGKKNTLG SDIGQFEKST KGIGMKLLEK MGYKGGGLGK NQQGIVAPIE AQLRPKNMGM
GYNDFKEAKL PDLKKVEEKK IIGVSVSENE QSHGDRGGKN LWKKKKVRKA VYVTAEELLE
KKQEAGFGGG QTIIDMRGPQ VRVVTNLENL DAEEKAKEAD VPMPELQHNL RLIVDLVEHE
IQKIDRDLRN ERESALSLQQ EKEMLINEEE KQKRHLENME YIADEISRIE LENTSGNLTL
DSLAIRFEDL QTSYPDDYKL CSLSTIACSL ALPLFIRMFQ GWDPLSDAVH GLKAISSWRK
LLEVEEDHNI WVVSTPYSQL VSEVVLPAVR IAGINTWEPR DPEPMLRFLE TWETLLPSSV
LQTILDTVVL PKLSTAVEYW DPRRELVAIH VWVHPWLPIL GQKLEFLYQI IQMKLSNVLD
AWHPSDSSAY TILSPWKTVF DTTSWEQLMR RYIVPKLQLA LQEFQVNPAN QNLERFDWVM
KWASAVPIHL MADMMERFFF PKWLDVLYHW LRAKPRFEEI QGWYYGWKEL FPQELTANER
IRIQLKRGLD MLMEAVEGVE VSQPRAKANE RTQSVPAQAQ AQAKAQMDST EVLSLKEVLE
VFAQEQELLF KPKPNRMHNG LQIYGFGNVS VIIDSVNQKL LAQKDGGWFL VTPDDLLRMH
NNTTVSAKR
