RAD9A_MACFA
ID RAD9A_MACFA Reviewed; 379 AA.
AC Q4R5X9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Cell cycle checkpoint control protein RAD9A;
DE EC=3.1.11.2;
DE AltName: Full=DNA repair exonuclease rad9 homolog A;
GN Name=RAD9A; ORFNames=QtsA-19913;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the 9-1-1 cell-cycle checkpoint response complex
CC that plays a major role in DNA repair. The 9-1-1 complex is recruited
CC to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp
CC loader complex. Acts then as a sliding clamp platform on DNA for
CC several proteins involved in long-patch base excision repair (LP-BER).
CC The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by
CC increasing its affinity for the 3'-OH end of the primer-template and
CC stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1
CC cleavage activity on substrates with double, nick, or gap flaps of
CC distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch
CC base excision repair substrates. The 9-1-1 complex is necessary for the
CC recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring
CC during the S phase. RAD9A possesses 3'->5' double stranded DNA
CC exonuclease activity (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.11.2;
CC -!- SUBUNIT: Component of the toroidal 9-1-1 (RAD9-RAD1-HUS1) complex,
CC composed of RAD9A, RAD1 and HUS1. The 9-1-1 complex associates with
CC LIG1, POLB, FEN1, RAD17, HDAC1, RPA1 and RPA2. The 9-1-1 complex
CC associates with the RAD17-RFC complex. RAD9A interacts with BCL2L1,
CC FEN1, PRKCD, RAD9B, HUS1, RAD1, ABL1, RPA1, ATAD5 and RPA2. Interacts
CC with DNAJC7 and RHNO1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Constitutively phosphorylated on serine and threonine amino acids
CC in absence of DNA damage. Hyperphosphorylated by PRKCD and ABL1 upon
CC DNA damage. Its phosphorylation by PRKCD may be required for the
CC formation of the 9-1-1 complex (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the rad9 family. {ECO:0000305}.
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; AB169413; BAE01496.1; -; mRNA.
DR RefSeq; NP_001271905.1; NM_001284976.1.
DR AlphaFoldDB; Q4R5X9; -.
DR SMR; Q4R5X9; -.
DR STRING; 9541.XP_005577141.1; -.
DR GeneID; 101926088; -.
DR CTD; 5883; -.
DR eggNOG; KOG2810; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0030896; C:checkpoint clamp complex; IEA:InterPro.
DR GO; GO:0008853; F:exodeoxyribonuclease III activity; IEA:UniProtKB-EC.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR InterPro; IPR026584; Rad9.
DR InterPro; IPR007268; Rad9/Ddc1.
DR PANTHER; PTHR15237; PTHR15237; 1.
DR Pfam; PF04139; Rad9; 1.
DR PIRSF; PIRSF009303; Cell_cycle_RAD9; 1.
PE 2: Evidence at transcript level;
KW DNA damage; Exonuclease; Hydrolase; Nuclease; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..379
FT /note="Cell cycle checkpoint control protein RAD9A"
FT /id="PRO_0000225002"
FT REGION 40..80
FT /note="Possesses 3'-5' exonuclease activity"
FT /evidence="ECO:0000250"
FT REGION 255..379
FT /note="Sufficient for interaction with ABL1"
FT /evidence="ECO:0000250"
FT REGION 257..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q99638"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99638"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99638"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99638"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99638"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99638"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99638"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99638"
SQ SEQUENCE 379 AA; 41370 MW; E49C1EE09FAA1576 CRC64;
MLGKAVHSLS RIGDELYLEP LEDGLSLRTV NSSRSAYACF LFAPLFFQQY QAATPGQDLL
RCKILMKSFL SVFRSLAMLE KTVEKCCISL NGRSSRLVVQ LHCKFGVRKT HNLSFQDCES
LQAVFDPASC PHMLRAPARV LGEAVLPFPP ALAEVTLGIG RGRRVILRSY HEEEADSTAK
AMVTEMCLGE EDFQQLQAQE GVAITFCLKE FRGLLSFAES ANLNLSIHFD APGRPAIFTI
KDSLLDGHFV LATLSDTDSH SQDLGSPERH QPVPQLQAHS IPHPDDFAND DIDSYMIAME
TTIGNEGSRV LPSISLSPGP QHPESPGLHS EEDEAEPSTV PGTPPPKKFR SLFFGSILAP
ARSPQGPSPV LAEDSEGEG
