SUUR_DROME
ID SUUR_DROME Reviewed; 962 AA.
AC Q9VTE2; Q9N6U5;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein suppressor of underreplication;
GN Name=SuUR; Synonyms=Su(UR)ES; ORFNames=CG7869;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=11901119; DOI=10.1093/genetics/160.3.1023;
RA Makunin I.V., Volkova E.I., Belyaeva E.S., Nabirochkina E.N., Pirrotta V.,
RA Zhimulev I.F.;
RT "The Drosophila suppressor of underreplication protein binds to late-
RT replicating regions of polytene chromosomes.";
RL Genetics 160:1023-1034(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=12644953; DOI=10.1007/s00412-002-0218-0;
RA Zhimulev I.F., Belyaeva E.S., Makunin I.V., Pirrotta V., Volkova E.I.,
RA Alekseyenko A.A., Andreyeva E.N., Makarevich G.F., Boldyreva L.V.,
RA Nanayev R.A., Demakova O.V.;
RT "Influence of the SuUR gene on intercalary heterochromatin in Drosophila
RT melanogaster polytene chromosomes.";
RL Chromosoma 111:377-398(2003).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12456726; DOI=10.1242/jcs.00196;
RA Zhimulev I.F., Belyaeva E.S., Semeshin V.F., Shloma V.V., Makunin I.V.,
RA Volkova E.I.;
RT "Overexpression of the SuUR gene induces reversible modifications at
RT pericentric, telomeric and intercalary heterochromatin of Drosophila
RT melanogaster polytene chromosomes.";
RL J. Cell Sci. 116:169-176(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432; THR-438; THR-466;
RP SER-468; THR-810; SER-827; SER-833; SER-834 AND SER-838, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [8]
RP FUNCTION, INTERACTION WITH RIF1, SUBCELLULAR LOCATION, DOMAIN, AND
RP MUTAGENESIS OF 2-TYR--GLY-278.
RX PubMed=30277458; DOI=10.7554/elife.39140;
RA Munden A., Rong Z., Sun A., Gangula R., Mallal S., Nordman J.T.;
RT "Rif1 inhibits replication fork progression and controls DNA copy number in
RT Drosophila.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Required for underreplication of DNA, which is found in many
CC late replicating euchromatic regions of salivary gland polytene
CC chromosomes (PubMed:11901119, PubMed:12456726, PubMed:30277458).
CC Functions by promoting the localization and retention of Rif1 to active
CC DNA replication forks where Rif1 inhibits replication fork progression
CC (PubMed:30277458). Controls chromatin organization in polytene
CC chromosomes (PubMed:12456726). {ECO:0000269|PubMed:11901119,
CC ECO:0000269|PubMed:12456726, ECO:0000269|PubMed:30277458}.
CC -!- SUBUNIT: Interacts (via SNF2-like region) with Rif1.
CC {ECO:0000269|PubMed:30277458}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30277458}. Chromosome
CC {ECO:0000269|PubMed:30277458}. Note=Localizes to the DNA replication
CC forks and heterochromatin in amplifying ovarian follicle cells
CC (PubMed:30277458). Binds to polytene chromosomes from salivary glands.
CC Localized at late-replicating intercalary heterochromatin and
CC pericentric heterochromatin. Colocalizes with many Polycomb Group
CC proteins binding sites on polytene chromosomes.
CC {ECO:0000269|PubMed:30277458}.
CC -!- TISSUE SPECIFICITY: Expressed throughout development. Weakly expressed.
CC Expressed at higher level in embryos and adult females.
CC {ECO:0000269|PubMed:11901119}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:11901119}.
CC -!- DOMAIN: The SNF2-like region is essential for localization to DNA
CC replication forks and for promoting underreplication. It is not
CC required for localization to heterochromatin.
CC {ECO:0000269|PubMed:30277458}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ277592; CAB89187.1; -; mRNA.
DR EMBL; AE014296; AAF50110.3; -; Genomic_DNA.
DR EMBL; BT010066; AAQ22535.1; -; mRNA.
DR RefSeq; NP_524835.1; NM_080096.3.
DR AlphaFoldDB; Q9VTE2; -.
DR BioGRID; 69842; 10.
DR DIP; DIP-22909N; -.
DR IntAct; Q9VTE2; 2.
DR STRING; 7227.FBpp0075933; -.
DR iPTMnet; Q9VTE2; -.
DR PaxDb; Q9VTE2; -.
DR PRIDE; Q9VTE2; -.
DR DNASU; 45739; -.
DR EnsemblMetazoa; FBtr0076203; FBpp0075933; FBgn0025355.
DR GeneID; 45739; -.
DR KEGG; dme:Dmel_CG7869; -.
DR CTD; 45739; -.
DR FlyBase; FBgn0025355; SuUR.
DR VEuPathDB; VectorBase:FBgn0025355; -.
DR eggNOG; ENOG502TBHQ; Eukaryota.
DR HOGENOM; CLU_303532_0_0_1; -.
DR InParanoid; Q9VTE2; -.
DR OMA; LEQMFEP; -.
DR PhylomeDB; Q9VTE2; -.
DR SignaLink; Q9VTE2; -.
DR BioGRID-ORCS; 45739; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 45739; -.
DR PRO; PR:Q9VTE2; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0025355; Expressed in gastric caecum (Drosophila) and 12 other tissues.
DR Genevisible; Q9VTE2; DM.
DR GO; GO:0000792; C:heterochromatin; IDA:FlyBase.
DR GO; GO:0005725; C:intercalary heterochromatin; IDA:UniProtKB.
DR GO; GO:0043596; C:nuclear replication fork; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:UniProtKB.
DR GO; GO:0005700; C:polytene chromosome; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEP:UniProtKB.
DR GO; GO:0051276; P:chromosome organization; IMP:FlyBase.
DR GO; GO:0042023; P:DNA endoreduplication; IMP:FlyBase.
DR GO; GO:0006260; P:DNA replication; IEP:UniProtKB.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0045185; P:maintenance of protein location; IMP:UniProtKB.
DR GO; GO:0008156; P:negative regulation of DNA replication; TAS:FlyBase.
DR GO; GO:2000104; P:negative regulation of DNA-templated DNA replication; IMP:FlyBase.
DR GO; GO:0032877; P:positive regulation of DNA endoreduplication; IMP:FlyBase.
DR GO; GO:0034502; P:protein localization to chromosome; IMP:UniProtKB.
DR Gene3D; 3.40.50.10810; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Chromosome; Developmental protein; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..962
FT /note="Protein suppressor of underreplication"
FT /id="PRO_0000072323"
FT REGION 1..278
FT /note="SNF2-like"
FT /evidence="ECO:0000269|PubMed:30277458"
FT REGION 351..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 438
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 466
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 810
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 833
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 834
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 2..278
FT /note="Missing: Underreplication is suppressed in larval
FT salivary glands."
FT /evidence="ECO:0000269|PubMed:30277458"
SQ SEQUENCE 962 AA; 107625 MW; 5063FB88E875C4F9 CRC64;
MYHFVSEQTP EVRLTDEALV TSHVTQYLKS FQLDAVRFVY DRLAKREFCI LNDESGLGKV
ATVAALLSAL PPAKKTLVVL QNDEQLLTGW RFHLDTLTDL QVYIIQGVQD TTDSPHSVYL
AKWSQLRSIG DLSRLKFDYI MVDNRGHSLN NSFCTSMLLK QFEGRVNVLI SSVDVTSDVR
LLYNVLRLGG RLEHQYKSFA SFDRKFHLPD PKEVFSKRID LEEYYKQRGF LSEYIKDFRL
RRFRHQFDKS LPLVAPEQYK HNLNLWLASK NSQSTISGSD VCSTIASIDN NPAQQNKTGL
FEETDRLSEH SVDDVAMSPL IFEYSESDDE PLTVEPDADQ NPVLVVSSDD CEIVTPPSTP
QNRTPSLNES PRTKSKKKFS KKTSPRKKAD LTDSEEDDEA TDNMPPRKRT RAATVHLTPK
TRRLNVRILR VSLDTLSTPP PSRTTTAIVT PKTEPTARRK NLKKRTVSPV DVGRPATRGM
QRLTRSAETK INSKYLKHRS LDDVKRSFPR RVKLEGNQTP RSSKQIVKQE PKSKVGQEKK
QKTVDVPAQG TAKRKPGRPR KCQTKTEDLG KTKTKPNSKH LPPTPQVLSG SSLSSEYMQC
AQRIPDNLDA IESPAFRVPF TPQQTPMLLT LPSTHNLLND SEVVSIPLYK DPVETVVINS
SHDECSPQDP SQSRRTKALK RKRKPVTSVN SSFGGGLGLP PAKRSANKSP DLFSISSEHS
QIPLAQPRPS SPFEGFKIFG SEVKQFQQQL AKVNISVPKK KRDRSCLDIL EQMFEPRQQQ
SAKTSPKVLP TLPLTQKDDA ESTITQRRRT LLEDDFFEIT NNGQFGSRMR LNSSGEVSPV
QPDQQSVRPS QANKITNYLI GSGITQERTQ PSNGNRNSIL ASLRKSPKSP KQGAKSTQAT
KLTRWFGSVF GGGASQTSSV ESVSAPSTPV NSSTSAAACQ TRSARSGGAS GPTKRKRLEL
FK
