SF1_ARATH
ID SF1_ARATH Reviewed; 804 AA.
AC Q9LU44; Q94KA0;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 156.
DE RecName: Full=Splicing factor-like protein 1 {ECO:0000303|PubMed:24580679};
DE Short=AtSF1 {ECO:0000303|PubMed:24580679};
DE Short=SF1 homolog protein {ECO:0000303|PubMed:24580679};
GN Name=SF1 {ECO:0000303|PubMed:24580679};
GN OrderedLocusNames=At5g51300 {ECO:0000312|Araport:AT5G51300};
GN ORFNames=MWD22.25 {ECO:0000312|EMBL:BAA97393.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia; TISSUE=Flower, Rosette leaf, and Silique;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16807317; DOI=10.1093/nar/gkl429;
RA de la Fuente van Bentem S., Anrather D., Roitinger E., Djamei A.,
RA Hufnagl T., Barta A., Csaszar E., Dohnal I., Lecourieux D., Hirt H.;
RT "Phosphoproteomics reveals extensive in vivo phosphorylation of Arabidopsis
RT proteins involved in RNA metabolism.";
RL Nucleic Acids Res. 34:3267-3278(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH
RP U2AF65A AND U2AF65B, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=24580679; DOI=10.1111/tpj.12491;
RA Jang Y.H., Park H.-Y., Lee K.C., Thu M.P., Kim S.-K., Suh M.C., Kang H.,
RA Kim J.-K.;
RT "A homolog of splicing factor SF1 is essential for development and is
RT involved in the alternative splicing of pre-mRNA in Arabidopsis thaliana.";
RL Plant J. 78:591-603(2014).
CC -!- FUNCTION: Necessary for the splicing of pre-mRNA. Required during
CC development and for abscisic acid (ABA) responses.
CC {ECO:0000269|PubMed:24580679}.
CC -!- SUBUNIT: Component of the spliceosome (Probable). Interacts with
CC U2AF65a and U2AF65b in the nucleus (PubMed:24580679).
CC {ECO:0000269|PubMed:24580679, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24580679}.
CC -!- TISSUE SPECIFICITY: Expressed in the shoot apex, flowers, stems,
CC leaves, roots and seedling. {ECO:0000269|PubMed:24580679}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in germinating seeds and in young
CC seedlings. During the reproductive phase, strongly expressed in leaves
CC and flowers. Barely detectable in stems, pedicels and siliques.
CC {ECO:0000269|PubMed:24580679}.
CC -!- DISRUPTION PHENOTYPE: Pleiotropic developmental defects, including
CC early flowering and hypersensitivity to abscisic acid (ABA). Enhanced
CC accumulation of many mRNAs, including heat shock mRNAs, with altered
CC alternative splicing pattern. {ECO:0000269|PubMed:24580679}.
CC -!- SIMILARITY: Belongs to the BBP/SF1 family. {ECO:0000305}.
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DR EMBL; AB023044; BAA97393.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96063.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96064.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96065.1; -; Genomic_DNA.
DR EMBL; AF370132; AAK43947.1; -; mRNA.
DR EMBL; AY142629; AAN13087.1; -; mRNA.
DR EMBL; AK316802; BAH19518.1; -; mRNA.
DR EMBL; AK317057; BAH19750.1; -; mRNA.
DR RefSeq; NP_001032055.1; NM_001036978.2.
DR RefSeq; NP_199943.1; NM_124509.4.
DR RefSeq; NP_851169.1; NM_180838.2.
DR AlphaFoldDB; Q9LU44; -.
DR SMR; Q9LU44; -.
DR IntAct; Q9LU44; 1.
DR STRING; 3702.AT5G51300.1; -.
DR iPTMnet; Q9LU44; -.
DR PaxDb; Q9LU44; -.
DR PRIDE; Q9LU44; -.
DR ProteomicsDB; 232582; -.
DR EnsemblPlants; AT5G51300.1; AT5G51300.1; AT5G51300.
DR EnsemblPlants; AT5G51300.2; AT5G51300.2; AT5G51300.
DR EnsemblPlants; AT5G51300.3; AT5G51300.3; AT5G51300.
DR GeneID; 835204; -.
DR Gramene; AT5G51300.1; AT5G51300.1; AT5G51300.
DR Gramene; AT5G51300.2; AT5G51300.2; AT5G51300.
DR Gramene; AT5G51300.3; AT5G51300.3; AT5G51300.
DR KEGG; ath:AT5G51300; -.
DR Araport; AT5G51300; -.
DR TAIR; locus:2176222; AT5G51300.
DR eggNOG; KOG0119; Eukaryota.
DR HOGENOM; CLU_013550_0_0_1; -.
DR InParanoid; Q9LU44; -.
DR OMA; GAAPWHQ; -.
DR OrthoDB; 887669at2759; -.
DR PhylomeDB; Q9LU44; -.
DR PRO; PR:Q9LU44; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LU44; baseline and differential.
DR GO; GO:0005730; C:nucleolus; IDA:CACAO.
DR GO; GO:0005654; C:nucleoplasm; IDA:CACAO.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IMP:UniProtKB.
DR Gene3D; 3.30.1370.10; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR045071; BBP-like.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR032570; SF1-HH.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR11208; PTHR11208; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF16275; SF1-HH; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF54791; SSF54791; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Metal-binding; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Spliceosome; Zinc; Zinc-finger.
FT CHAIN 1..804
FT /note="Splicing factor-like protein 1"
FT /id="PRO_0000441280"
FT DOMAIN 256..328
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 480..558
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 363..378
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 389..403
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 123..127
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..586
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..652
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 122
FT /note="G -> E (in Ref. 3; AAK43947)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 804 AA; 87050 MW; 82E39348503F5B97 CRC64;
MESVEMNNPN SQTLDQPPPS SNGDTAPLAL DHMNPQNSES VALNGSSTPI PDTNGSSAKP
ELLRPLLSEN GVSKTLSGND KDQSGGEEET TSRRKRRSRW DPPPSESINN PSAEGGTDSG
TGTRKRKSRW ADDEPRTQIQ LPDFMKDFTG GIEFDPEIQA LNSRLLEISR MLQSGMPLDD
RPEGQRSPSP EPVYDNMGIR INTREYRARE RLNRERQEII AQIIKKNPAF KPPADYRPPK
LHKKLFIPMK EFPGYNFIGL IIGPRGNTQK RMERETGAKI VIRGKGSVKE GRHQQKKDLK
YDPSENEDLH VLVEAETQEA LEAAAGMVEK LLQPVDEVLN EHKRQQLREL ATLNGTIRDE
EFCRLCGEPG HRQYACPSRT NTFKSDVLCK ICGDGGHPTI DCPVKGTTGK KMDDEYQNFL
AELGGTVPES SLKQSATLAL GPGSSGSNPP WANNAGNGAS AHPGLGSTPT KPPSKEYDET
NLYIGFLPPM LEDDGLINLF SSFGEIVMAK VIKDRVTGLS KGYGFVKYAD VQMANTAVQA
MNGYRFEGRT LAVRIAGKSP PPIAPPGPPA PQPPTQGYPP SNQPPGAYPS QQYATGGYST
APVPWGPPVP SYSPYALPPP PPGSYHPVHG QHMPPYGMQY PPPPPHVTQA PPPGTTQNPS
SSEPQQSFPP GVQADSGAAT SSIPPNVYGS SVTAMPGQPP YMSYPSYYNA VPPPTPPAPA
SSTDHSQNMG NMPWANNPSV STPDHSQGLV NAPWAPNPPM PPTVGYSQSM GNVPWAPKPP
VQPPAENPSS VGESEYEKFM AEMK
