DSUP_RAMVA
ID DSUP_RAMVA Reviewed; 445 AA.
AC P0DOW4; A0A1D1W292;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=Damage suppressor protein {ECO:0000303|PubMed:27649274};
GN Name=Dsup {ECO:0000303|PubMed:27649274};
GN ORFNames=RvY_17224 {ECO:0000303|PubMed:27649274};
OS Ramazzottius varieornatus (Water bear) (Tardigrade).
OC Eukaryota; Metazoa; Ecdysozoa; Tardigrada; Eutardigrada; Parachela;
OC Hypsibioidea; Ramazzottiidae; Ramazzottius.
OX NCBI_TaxID=947166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA / MRNA], IDENTIFICATION BY
RP MASS SPECTROMETRY, SUBCELLULAR LOCATION, DNA-BINDING, AND FUNCTION.
RC STRAIN=YOKOZUNA-1;
RX PubMed=27649274; DOI=10.1038/ncomms12808;
RA Hashimoto T., Horikawa D.D., Saito Y., Kuwahara H., Kozuka-Hata H.,
RA Shin-I T., Minakuchi Y., Ohishi K., Motoyama A., Aizu T., Enomoto A.,
RA Kondo K., Tanaka S., Hara Y., Koshikawa S., Sagara H., Miura T.,
RA Yokobori S., Miyagawa K., Suzuki Y., Kubo T., Oyama M., Kohara Y.,
RA Fujiyama A., Arakawa K., Katayama T., Toyoda A., Kunieda T.;
RT "Extremotolerant tardigrade genome and improved radiotolerance of human
RT cultured cells by tardigrade-unique protein.";
RL Nat. Commun. 7:12808-12808(2016).
RN [2]
RP FUNCTION, REGION, AND MUTAGENESIS OF 360-GLU--LYS-445 AND 363-ARG--ARG-367.
RX PubMed=31571581; DOI=10.7554/elife.47682;
RA Chavez C., Cruz-Becerra G., Fei J., Kassavetis G.A., Kadonaga J.T.;
RT "The tardigrade damage suppressor protein binds to nucleosomes and protects
RT DNA from hydroxyl radicals.";
RL Elife 8:0-0(2019).
CC -!- FUNCTION: Unique chromatin-associating protein that contributes to the
CC organism's exceptional tolerance to harsh environmental stresses
CC (PubMed:27649274, PubMed:31571581). Binds with a higher affinity to
CC nucleosomes than to free DNA (PubMed:31571581). Protects chromatin from
CC damage caused by hydroxyl radical-mediated cleavage induced by X-rays
CC or treatment with hydrogen peroxide (PubMed:27649274, PubMed:31571581).
CC Suppresses X-ray-induced DNA damage that includes single-strand breaks
CC (SSBs) as well as more hazardous double-strand breaks (DSBs), and
CC improves radiotolerance (PubMed:27649274). Shields also DNA against
CC reactive oxygen species (ROS) (PubMed:27649274).
CC {ECO:0000269|PubMed:27649274, ECO:0000269|PubMed:31571581}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27649274}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=A walk on the rough side
CC - Issue 188 of February 2017;
CC URL="https://web.expasy.org/spotlight/back_issues/188/";
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DR EMBL; LC050827; BAV59442.1; -; mRNA.
DR EMBL; BDGG01000015; GAV07386.1; -; Genomic_DNA.
DR AlphaFoldDB; P0DOW4; -.
DR Proteomes; UP000186922; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW DNA damage; DNA-binding; Nucleus; Reference proteome.
FT CHAIN 1..445
FT /note="Damage suppressor protein"
FT /id="PRO_0000438665"
FT REGION 1..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..445
FT /note="Required and sufficient for DNA-binding and co-
FT localization with nuclear DNA"
FT /evidence="ECO:0000269|PubMed:27649274"
FT REGION 360..445
FT /note="Required for nucleosome binding and for the
FT protection of chromatin from hydroxyl radical-mediated DNA
FT damage"
FT /evidence="ECO:0000269|PubMed:31571581"
FT COMPBIAS 27..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 360..445
FT /note="Missing: In M1; loss of binding to nucleosomes and
FT reduced ability to protect chromatin from hydroxyl radical-
FT mediated DNA damage."
FT /evidence="ECO:0000269|PubMed:31571581"
FT MUTAGEN 363..367
FT /note="RRSSR->EESSE: In M2; decreased binding to
FT nucleosomes and reduced ability to protect chromatin from
FT hydroxyl radical-mediated DNA damage."
FT /evidence="ECO:0000269|PubMed:31571581"
SQ SEQUENCE 445 AA; 42848 MW; 143D9A85814C5805 CRC64;
MASTHQSSTE PSSTGKSEET KKDASQGSGQ DSKNVTVTKG TGSSATSAAI VKTGGSQGKD
SSTTAGSSST QGQKFSTTPT DPKTFSSDQK EKSKSPAKEV PSGGDSKSQG DTKSQSDAKS
SGQSQGQSKD SGKSSSDSSK SHSVIGAVKD VVAGAKDVAG KAVEDAPSIM HTAVDAVKNA
ATTVKDVASS AASTVAEKVV DAYHSVVGDK TDDKKEGEHS GDKKDDSKAG SGSGQGGDNK
KSEGETSGQA ESSSGNEGAA PAKGRGRGRP PAAAKGVAKG AAKGAAASKG AKSGAESSKG
GEQSSGDIEM ADASSKGGSD QRDSAATVGE GGASGSEGGA KKGRGRGAGK KADAGDTSAE
PPRRSSRLTS SGTGAGSAPA AAKGGAKRAA SSSSTPSNAK KQATGGAGKA AATKATAAKS
AASKAPQNGA GAKKKGGKAG GRKRK
