SSRP1_ARATH
ID SSRP1_ARATH Reviewed; 646 AA.
AC Q05153; C0Z265; Q56X23; Q9LHA2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 25-MAY-2022, entry version 167.
DE RecName: Full=FACT complex subunit SSRP1;
DE AltName: Full=Facilitates chromatin transcription complex subunit SSRP1;
DE AltName: Full=High mobility group B protein 8;
DE AltName: Full=Nucleosome/chromatin assembly factor group D 08;
DE Short=Nucleosome/chromatin assembly factor group D 8;
DE AltName: Full=Protein NUCLEAR FUSION DEFECTIVE 8 {ECO:0000303|PubMed:16698901};
DE AltName: Full=Recombination signal sequence recognition protein 1;
GN Name=SSRP1; Synonyms=HMGB8, NFD8 {ECO:0000303|PubMed:16698901};
GN OrderedLocusNames=At3g28730; ORFNames=T19N8.2;
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 [MRNA] (ISOFORM 1).
RX PubMed=1480495; DOI=10.1093/nar/20.24.6737;
RA Yamaguchi-Shinozaki K., Shinozaki K.;
RT "A novel Arabidopsis DNA binding protein contains the conserved motif of
RT HMG-box proteins.";
RL Nucleic Acids Res. 20:6737-6737(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 438-646 (ISOFORM 1).
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15546350; DOI=10.1111/j.1365-313x.2004.02242.x;
RA Duroux M., Houben A., Ruzicka K., Friml J., Grasser K.D.;
RT "The chromatin remodelling complex FACT associates with actively
RT transcribed regions of the Arabidopsis genome.";
RL Plant J. 40:660-671(2004).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=16698901; DOI=10.1104/pp.106.079319;
RA Portereiko M.F., Sandaklie-Nikolova L., Lloyd A., Dever C.A., Otsuga D.,
RA Drews G.N.;
RT "NUCLEAR FUSION DEFECTIVE1 encodes the Arabidopsis RPL21M protein and is
RT required for karyogamy during female gametophyte development and
RT fertilization.";
RL Plant Physiol. 141:957-965(2006).
CC -!- FUNCTION: Component of the FACT complex, a general chromatin factor
CC that acts to reorganize nucleosomes. The FACT complex is involved in
CC multiple processes that require DNA as a template such as mRNA
CC elongation, DNA replication and DNA repair. During transcription
CC elongation the FACT complex acts as a histone chaperone that both
CC destabilizes and restores nucleosomal structure. It facilitates the
CC passage of RNA polymerase II and transcription by promoting the
CC dissociation of one histone H2A-H2B dimer from the nucleosome, then
CC subsequently promotes the reestablishment of the nucleosome following
CC the passage of RNA polymerase II. Binds specifically to double-stranded
CC DNA (Probable). Required for karyogamy during female gametophyte
CC development, when the two polar nuclei fuse to form the diploid central
CC cell nucleus (PubMed:16698901). {ECO:0000269|PubMed:16698901,
CC ECO:0000305|PubMed:15546350}.
CC -!- SUBUNIT: Component of the FACT complex, a stable heterodimer of SPT16
CC and SSRP1. {ECO:0000250}.
CC -!- INTERACTION:
CC Q05153; Q9M2K8: AGL18; NbExp=3; IntAct=EBI-15191543, EBI-15197363;
CC Q05153; C0SUU6: At1g11510; NbExp=3; IntAct=EBI-15191543, EBI-15191973;
CC Q05153; Q9C6K4: At1g76870; NbExp=3; IntAct=EBI-15191543, EBI-15193203;
CC Q05153; O23063: At4g00390; NbExp=3; IntAct=EBI-15191543, EBI-15195019;
CC Q05153; F4K5T4: At5g28040; NbExp=3; IntAct=EBI-15191543, EBI-15193831;
CC Q05153; Q9ASZ1: GEBP; NbExp=3; IntAct=EBI-15191543, EBI-15191723;
CC Q05153; Q8VYD2: GPL1; NbExp=4; IntAct=EBI-15191543, EBI-4426914;
CC Q05153; Q38829: IAA11; NbExp=3; IntAct=EBI-15191543, EBI-2367923;
CC Q05153; Q8LG05: STKL1; NbExp=3; IntAct=EBI-15191543, EBI-4424255;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC ECO:0000269|PubMed:15546350}. Chromosome {ECO:0000269|PubMed:15546350}.
CC Note=Colocalizes with RNA polymerase II on chromatin. Recruited to
CC actively transcribed loci.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q05153-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q05153-2; Sequence=VSP_039931, VSP_039932;
CC -!- TISSUE SPECIFICITY: Widely expressed. Present in embryos, shoots and
CC roots, whereas it is not present in terminally differentiated cells
CC such as mature trichoblasts or cells of the root cap (at protein
CC level). {ECO:0000269|PubMed:15546350}.
CC -!- DISRUPTION PHENOTYPE: Failure of fusion of the polar nuclei during
CC megagametogenesis. {ECO:0000269|PubMed:16698901}.
CC -!- SIMILARITY: Belongs to the SSRP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA02719.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D13491; BAA02719.1; ALT_FRAME; mRNA.
DR EMBL; AP002057; BAB03170.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77484.1; -; Genomic_DNA.
DR EMBL; BT002507; AAO00867.1; -; mRNA.
DR EMBL; AK318679; BAH56794.1; -; mRNA.
DR EMBL; AK221855; BAD94127.1; -; mRNA.
DR PIR; S35511; S35511.
DR RefSeq; NP_189515.1; NM_113794.4. [Q05153-1]
DR AlphaFoldDB; Q05153; -.
DR SMR; Q05153; -.
DR BioGRID; 7834; 37.
DR IntAct; Q05153; 27.
DR STRING; 3702.AT3G28730.1; -.
DR iPTMnet; Q05153; -.
DR PaxDb; Q05153; -.
DR PRIDE; Q05153; -.
DR ProteomicsDB; 228335; -. [Q05153-1]
DR EnsemblPlants; AT3G28730.1; AT3G28730.1; AT3G28730. [Q05153-1]
DR GeneID; 822505; -.
DR Gramene; AT3G28730.1; AT3G28730.1; AT3G28730. [Q05153-1]
DR KEGG; ath:AT3G28730; -.
DR Araport; AT3G28730; -.
DR TAIR; locus:2098413; AT3G28730.
DR eggNOG; KOG0526; Eukaryota.
DR HOGENOM; CLU_017374_2_2_1; -.
DR InParanoid; Q05153; -.
DR OMA; SKQPGKC; -.
DR PhylomeDB; Q05153; -.
DR PRO; PR:Q05153; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q05153; baseline and differential.
DR Genevisible; Q05153; AT.
DR GO; GO:0000791; C:euchromatin; IDA:TAIR.
DR GO; GO:0035101; C:FACT complex; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0000741; P:karyogamy; IMP:UniProtKB.
DR GO; GO:0010197; P:polar nucleus fusion; IMP:UniProtKB.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR Gene3D; 1.10.30.10; -; 1.
DR Gene3D; 2.30.29.220; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR013719; DUF1747.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR035417; POB3_N.
DR InterPro; IPR000969; SSrcognition.
DR InterPro; IPR024954; SSRP1_dom.
DR InterPro; IPR038167; SSRP1_sf.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF17292; POB3_N; 1.
DR Pfam; PF08512; Rtt106; 1.
DR Pfam; PF03531; SSrecog; 1.
DR PRINTS; PR00887; SSRCOGNITION.
DR SMART; SM00398; HMG; 1.
DR SMART; SM01287; Rtt106; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Developmental protein; DNA damage;
KW DNA repair; DNA replication; DNA-binding; Karyogamy; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..646
FT /note="FACT complex subunit SSRP1"
FT /id="PRO_0000048610"
FT DNA_BIND 561..630
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 471..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..505
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 240..268
FT /note="NDFKIQYSSVVRLFLLPKSNQPHTFVVIS -> MTLKSSTVALSVCSCFQSQ
FT TNHTRLLLSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_039931"
FT VAR_SEQ 269..646
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_039932"
FT CONFLICT 6..7
FT /note="SF -> FL (in Ref. 1; BAA02719)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="G -> E (in Ref. 1; BAA02719)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="D -> N (in Ref. 6; BAD94127)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 646 AA; 71646 MW; DC45C2C13E2FCA0B CRC64;
MADGHSFNNI SLSGRGGKNP GLLKINSGGI QWKKQGGGKA VEVDRSDIVS VSWTKVTKSN
QLGVKTKDGL YYKFVGFRDQ DVPSLSSFFQ SSYGKTPDEK QLSVSGRNWG EVDLHGNTLT
FLVGSKQAFE VSLADVSQTQ LQGKNDVTLE FHVDDTAGAN EKDSLMEISF HIPNSNTQFV
GDENRPPSQV FNDTIVAMAD VSPGVEDAVV TFESIAILTP RGRYNVELHL SFLRLQGQAN
DFKIQYSSVV RLFLLPKSNQ PHTFVVISLD PPIRKGQTMY PHIVMQFETD TVVESELSIS
DELMNTKFKD KLERSYKGLI HEVFTTVLRW LSGAKITKPG KFRSSQDGFA VKSSLKAEDG
VLYPLEKGFF FLPKPPTLIL HDEIDYVEFE RHAAGGANMH YFDLLIRLKT DHEHLFRNIQ
RNEYHNLYTF ISSKGLKIMN LGGAGTADGV AAVLGDNDDD DAVDPHLTRI RNQAADESDE
EDEDFVMGED DDGGSPTDDS GGDDSDASEG GVGEIKEKSI KKEPKKEASS SKGLPPKRKT
VAADEGSSKR KKPKKKKDPN APKRAMSGFM FFSQMERDNI KKEHPGIAFG EVGKVLGDKW
RQMSADDKEP YEAKAQVDKQ RYKDEISDYK NPQPMNVDSG NDSDSN