ID   RAD17_CHLAE             Reviewed;         670 AA.
AC   Q9XT62;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Cell cycle checkpoint protein RAD17;
GN   Name=RAD17;
OS   Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=9534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10232579;
RA   Bao S., Chang M.-S., Auclair D., Sun Y., Wang Y., Wong W.-K., Zhang J.,
RA   Liu Y., Qian X., Sutherland R., Magi-Galluzi C., Weisberg E., Cheng E.Y.S.,
RA   Hao L., Sasaki H., Campbell M.S., Kraeft S.-K., Loda M., Lo K.-M.,
RA   Chen L.B.;
RT   "HRad17, a human homologue of the Schizosaccharomyces pombe checkpoint gene
RT   rad17, is overexpressed in colon carcinoma.";
RL   Cancer Res. 59:2023-2028(1999).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-44, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=17494752; DOI=10.1073/pnas.0701103104;
RA   Wang Y., Ding S.-J., Wang W., Jacobs J.M., Qian W.-J., Moore R.J., Yang F.,
RA   Camp D.G. II, Smith R.D., Klemke R.L.;
RT   "Profiling signaling polarity in chemotactic cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8328-8333(2007).
CC   -!- FUNCTION: Essential for sustained cell growth, maintenance of
CC       chromosomal stability, and ATR-dependent checkpoint activation upon DNA
CC       damage. Has a weak ATPase activity required for binding to chromatin.
CC       Participates in the recruitment of the RAD1-RAD9-HUS1 complex and RHNO1
CC       onto chromatin, and in CHEK1 activation. May also serve as a sensor of
CC       DNA replication progression, and may be involved in homologous
CC       recombination (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Part of a DNA-binding complex containing RFC2, RFC3, RFC4 and
CC       RFC5. Interacts with RAD1 and RAD9 within the RAD1-RAD9-HUS1 complex.
CC       Interacts with RAD9B, POLE, SNU13 and MCM7. DNA damage promotes
CC       interaction with ATR or ATM and disrupts interaction with the RAD1-
CC       RAD9-HUS1 complex (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Phosphorylated form
CC       redistributes to discrete nuclear foci upon DNA damage. {ECO:0000250}.
CC   -!- PTM: Phosphorylated. Phosphorylation on Ser-635 and Ser-645 is cell
CC       cycle-regulated, enhanced by genotoxic stress, and required for
CC       activation of checkpoint signaling. Phosphorylation on both sites is
CC       required for interaction with RAD1 but dispensable for interaction with
CC       RFC3 or RFC4 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the rad17/RAD24 family. {ECO:0000305}.
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DR   EMBL; AF106067; AAD42177.1; -; mRNA.
DR   AlphaFoldDB; Q9XT62; -.
DR   IntAct; Q9XT62; 3.
DR   MINT; Q9XT62; -.
DR   iPTMnet; Q9XT62; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031389; C:Rad17 RFC-like complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003689; F:DNA clamp loader activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR004582; Checkpoint_prot_Rad17_Rad24.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR018324; Rad17/Rad24_fun/met.
DR   PANTHER; PTHR12172; PTHR12172; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00602; rad24; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; DNA damage; Nucleotide-binding; Nucleus;
KW   Phosphoprotein.
FT   CHAIN           1..670
FT                   /note="Cell cycle checkpoint protein RAD17"
FT                   /id="PRO_0000209947"
FT   REGION          31..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..670
FT                   /note="Interaction with MCM7"
FT                   /evidence="ECO:0000250"
FT   REGION          593..670
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..611
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..653
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         126..133
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         44
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:17494752"
FT   MOD_RES         60
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75943"
FT   MOD_RES         75
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75943"
FT   MOD_RES         348
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75943"
FT   MOD_RES         635
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75943"
FT   MOD_RES         645
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75943"
SQ   SEQUENCE   670 AA;  76066 MW;  2D881F567CF3DE25 CRC64;
     MNQVTDWVDP SFDDFLECRD ISTITATSLG VNNSSHRRKN GPSTLESSKF PVRKRGNLSS
     LEQIYSLENS KESLSENEPW VDKYKPETQH ELAVHKKKIE EVETWLKAQV LERQPKQGGS
     ILLITGPPGC GKTTTIKVLS KEHGIQVQEW INPVLPDFQK DDFREIFNTE SSFHMFPYQS
     QIAVFKEFLL RATKYNKLQM LGDDLRTDKK IILVEDLPNQ FYRDSHTLHE VLRKYVRIGR
     CPLIFVISDS LSGDNNQRLL FPKEIQEECS ISNISFNPVA PTIMMKFLNR IVTIEANKNG
     GKITVPDKTS LELLCQGCSG DIRSAINSLQ FSSSKGENNL WPRKKGMSLK SDAVLSKSKR
     RKKPDRVFEN QEVQAIGGKD VSLFLFRALG KILYCKRASL TELDSPRLPS HLSEYERDTL
     LVEPEEVVEM SHMPGDLFNL YLHQNYIDFF MDIDDIVRAS EFLSFADILS GDWNTCSLLR
     EYSTSIATRG VIHSNKARGY AHCQGGGSSF RPLHKPQWFL IYKKYRENCL AAKALFPDFC
     LPALCLQTQL LPYLALLTIP MRNQAQISFI QDIGRLPLKR HFGRLKMEAL TDREHGMIDP
     DSGDEAQLNG RHSTEESLGE PTQASAPETW SLPLSQNSAS ELPASQPQPF SAQGDMEENI
     IIEDYESDGT