ID   RAD17_PONAB             Reviewed;         681 AA.
AC   Q5R652;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Cell cycle checkpoint protein RAD17;
GN   Name=RAD17;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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-646 and Ser-656 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; CR860644; CAH92764.1; -; mRNA.
DR   RefSeq; NP_001129002.1; NM_001135530.1.
DR   AlphaFoldDB; Q5R652; -.
DR   STRING; 9601.ENSPPYP00000017352; -.
DR   GeneID; 100190842; -.
DR   KEGG; pon:100190842; -.
DR   CTD; 5884; -.
DR   eggNOG; KOG1970; Eukaryota.
DR   InParanoid; Q5R652; -.
DR   Proteomes; UP000001595; Unplaced.
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   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; DNA damage; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..681
FT                   /note="Cell cycle checkpoint protein RAD17"
FT                   /id="PRO_0000209950"
FT   REGION          42..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..681
FT                   /note="Interaction with MCM7"
FT                   /evidence="ECO:0000250"
FT   REGION          606..681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..664
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         137..144
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         55
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XT62"
FT   MOD_RES         71
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75943"
FT   MOD_RES         86
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75943"
FT   MOD_RES         359
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75943"
FT   MOD_RES         646
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75943"
FT   MOD_RES         656
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75943"
SQ   SEQUENCE   681 AA;  77232 MW;  00D50E4CB9B1A230 CRC64;
     MSKTFLRPKV SSTKVTDWVD PSFDDFLECR DVSTITATSL GVNNSSHRRK NGPSTLESSR
     FPARKRGNLS SLEQIYGLEN SKEYLSENEP WVDKYKPETQ HELAVHKKKI EEVETWLKAQ
     VLERQPKQGG SILLITGPPG CGKTTTIKIL SKEHGIQVQE WINPVLPDFQ KDDFKGMFNT
     ESSFHMFPYQ SQIAVFKEFL LRATKYNKLQ MLGDDLRTDK KIILVEDLPN QFYRDSHTLH
     EVLRKYVRIG RCPLIFIISD SLSGDNNQRL LFPKEIQEEC SISNISFNPV APTIMMKFLN
     RIVTIEANKN GGKITVPDKT SLELLCQGCS GDIRSAINSL QFSSSKGENN LWPRKKGMSL
     KSDAVLSKSK QRKKPDRVFE NQEVQAIGGK DVSLFLFRAL GKILYCKRAS LTELDSPRLP
     SHLSEYERDT LLVEPEEVVE MSHMPGDLFN LYLHQNYIDF FMEIDDIVRA SEFLSFADIL
     SGDWNTRSLL REYSTSIATR GVMHSNKARG YAHCQGGGSS FRPLHKPQWF LINKKYRENY
     LAAKALFPDF CLPALCLQTQ LLPYLALLTI PMRNQAQISF IQDIGRLPLK RHFGRLKMEA
     LTDREHGMID PDSGDEAQLN GGHSAEESLG EPTQATALET WSLPLSQNSA SELPASQPQP
     FSAQGDMEEN IIIEDYESDG T