ID SPT16_ARATH Reviewed; 1074 AA.
AC O82491; C0SVH5;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 24-JAN-2024, entry version 144.
DE RecName: Full=FACT complex subunit SPT16;
DE AltName: Full=Facilitates chromatin transcription complex subunit SPT16;
GN Name=SPT16; OrderedLocusNames=At4g10710; ORFNames=T12H20.3;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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].
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
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).
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 (Probable).
CC {ECO:0000305|PubMed:15546350}.
CC -!- SUBUNIT: Component of the FACT complex, a stable heterodimer of SPT16
CC and SSRP.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15546350}. Chromosome
CC {ECO:0000269|PubMed:15546350}. Note=Colocalizes with RNA polymerase II
CC on chromatin. Recruited to actively transcribed loci.
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 -!- SIMILARITY: Belongs to the peptidase M24 family. SPT16 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Although related to the peptidase M24 family, this protein
CC lacks conserved active site residues suggesting that it may lack
CC peptidase activity. {ECO:0000305}.
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DR EMBL; AF080119; AAC35521.1; -; Genomic_DNA.
DR EMBL; AL161518; CAB81172.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82919.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67190.1; -; Genomic_DNA.
DR EMBL; AB493678; BAH30516.1; -; mRNA.
DR PIR; T01906; T01906.
DR RefSeq; NP_001329034.1; NM_001340681.1.
DR RefSeq; NP_192809.1; NM_117139.3.
DR AlphaFoldDB; O82491; -.
DR SMR; O82491; -.
DR BioGRID; 11964; 27.
DR STRING; 3702.O82491; -.
DR iPTMnet; O82491; -.
DR PaxDb; 3702-AT4G10710-1; -.
DR ProteomicsDB; 234097; -.
DR EnsemblPlants; AT4G10710.1; AT4G10710.1; AT4G10710.
DR EnsemblPlants; AT4G10710.2; AT4G10710.2; AT4G10710.
DR GeneID; 826665; -.
DR Gramene; AT4G10710.1; AT4G10710.1; AT4G10710.
DR Gramene; AT4G10710.2; AT4G10710.2; AT4G10710.
DR KEGG; ath:AT4G10710; -.
DR Araport; AT4G10710; -.
DR TAIR; AT4G10710; SPT16.
DR eggNOG; KOG1189; Eukaryota.
DR HOGENOM; CLU_004627_1_0_1; -.
DR InParanoid; O82491; -.
DR OMA; AYSVMKN; -.
DR OrthoDB; 169847at2759; -.
DR PhylomeDB; O82491; -.
DR PRO; PR:O82491; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O82491; baseline and differential.
DR Genevisible; O82491; AT.
DR GO; GO:0000791; C:euchromatin; IDA:TAIR.
DR GO; GO:0035101; C:FACT complex; IDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR CDD; cd01091; CDC68-like; 1.
DR Gene3D; 2.30.29.150; -; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR Gene3D; 2.30.29.210; FACT complex subunit Spt16p/Cdc68p; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR029148; FACT-Spt16_Nlobe.
DR InterPro; IPR013953; FACT_Spt16.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR013719; RTT106/SPT16-like_middle_dom.
DR InterPro; IPR040258; Spt16.
DR InterPro; IPR048969; SPT16_C.
DR InterPro; IPR033825; Spt16_M24.
DR PANTHER; PTHR13980; CDC68 RELATED; 1.
DR PANTHER; PTHR13980:SF18; FACT COMPLEX SUBUNIT SPT16; 1.
DR Pfam; PF14826; FACT-Spt16_Nlob; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF08512; Rttp106-like_middle; 1.
DR Pfam; PF08644; SPT16; 1.
DR Pfam; PF21091; SPT16_C; 1.
DR SMART; SM01285; FACT-Spt16_Nlob; 1.
DR SMART; SM01287; Rtt106; 1.
DR SMART; SM01286; SPT16; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
PE 1: Evidence at protein level;
KW Chromosome; Coiled coil; DNA damage; DNA repair; DNA replication; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..1074
FT /note="FACT complex subunit SPT16"
FT /id="PRO_0000245175"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 493..520
FT /evidence="ECO:0000255"
FT COILED 637..658
FT /evidence="ECO:0000255"
FT COILED 782..802
FT /evidence="ECO:0000255"
FT COMPBIAS 962..976
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..1007
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1043
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1074 AA; 120586 MW; 1AA6FA6475DDBB25 CRC64;
MADSRNGNAR APPSGVPPKA GNTYSIDVKN FISRARALYE HWKKHSADLW GSADALAIAT
PPASDDLRYL KSSALNIWLL GYEFPDTIMV FTKKQIHFLC SRNKASLLEV VKKPAHDELK
LDVIMHVKPK GDDGTGLMDA IFRAIRDLSR GDGNDSQVVG HIAREAPEGK LLETWTERLK
NANFQFVDIT GGLSDLFAVK DDTEVMSVKK AAYLAYSVMK NVVVPNLESA IDEEKDVTHS
ALMDLTEKAI LEPTKASVKL KPENVDICYP PIFQSGGKFD LKPSAASNDE LLTYDPASII
ICAVGARYNS YCSNVARTYL IDATSLQSKA YEVLLKAHEA AIDALRSGRK INTVYQAALS
VVEKNAPEFV DKLTKSAGTG IGLEFRESGL NINAKNDKVL RPKMAFNVSL GFQNLECESE
SRSKNKKFSL LLADTVLVTD QKPELLTKCS KSVKDVAYSF KEDEEEEKPR KKARTSGSEN
YITKTALRSD DHVVSKEELR KQHQAELARQ KNEETARRLA GDSSGAGDSR STAKTSADVV
AYKNVNDMPH KELMIQVDTR NEAVLLPIYG SLVPFHVATI RTVSGNQDTN RNCYIRIIFN
VPGTPFNPHD SNSLKNQGAI YLKEVSFRTK DSRHSSEVTQ QIKTLRRQVM ARESERAERA
TLVTQEKLQL AGNKFKPLRL SELWIRPPFS GRKKIPGTLE AHANGFRYST TRPDERVDVL
FANIKHAFFQ PAEKEMITLL HFHLHNHIMV GTKKTKDVQF YVEVMDVVQS LGGGRRSAYD
PDEIDEEQRE RDRKNKINMD FNHFANRVND MWQLPQFASL DLEFDQPLRE LGFHGVPHKT
SAFIIPTSSC LVELIEYPFL VVSLSEIEIV NLERVGFGQK NFDMAIIFKD FKKDVLRVDS
VPTSSLEGIK EWLDTTDIKY YESKLNLNWR QILKTITDDP QSFIDDGGWE FLNLDGSDSE
SGGSEESDKG YEPSDVEVES ESEDEASESE SLVESDDDEE EDSEQESEEE KGKTWDELER
EATNADREHG VESDSEEERK RRKMKAFGKS RPGTSGGGGS SSMKNMPPSK RKHR
//
