RAD1_PONAB
ID RAD1_PONAB Reviewed; 282 AA.
AC Q5R7X9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Cell cycle checkpoint protein RAD1;
DE EC=3.1.11.2;
DE AltName: Full=DNA repair exonuclease rad1 homolog;
GN Name=RAD1;
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: 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. Possesses 3'->5' double-stranded DNA exonuclease
CC 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. RAD1 interacts with POLB, FEN1,
CC HUS1, HUS1B, RAD9A and RAD9B. Interacts with DNAJC7 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the rad1 family. {ECO:0000305}.
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DR EMBL; CR859979; CAH92131.1; -; mRNA.
DR RefSeq; NP_001126246.1; NM_001132774.1.
DR RefSeq; XP_009238895.1; XM_009240620.1.
DR AlphaFoldDB; Q5R7X9; -.
DR SMR; Q5R7X9; -.
DR STRING; 9601.ENSPPYP00000017189; -.
DR Ensembl; ENSPPYT00000053099; ENSPPYP00000027894; ENSPPYG00000031706.
DR GeneID; 100173217; -.
DR KEGG; pon:100173217; -.
DR CTD; 5810; -.
DR eggNOG; KOG3194; Eukaryota.
DR GeneTree; ENSGT00500000044913; -.
DR HOGENOM; CLU_035332_2_1_1; -.
DR InParanoid; Q5R7X9; -.
DR OMA; QITMSPE; -.
DR OrthoDB; 1440961at2759; -.
DR TreeFam; TF101211; -.
DR Proteomes; UP000001595; Chromosome 5.
DR GO; GO:0005694; C:chromosome; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:Ensembl.
DR GO; GO:0008853; F:exodeoxyribonuclease III activity; IEA:UniProtKB-EC.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IEA:Ensembl.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:Ensembl.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0051598; P:meiotic recombination checkpoint signaling; IEA:Ensembl.
DR InterPro; IPR003011; Cell_cycle_checkpoint_Rad1.
DR InterPro; IPR003021; Rad1_Rec1_Rad17.
DR PANTHER; PTHR10870; PTHR10870; 1.
DR Pfam; PF02144; Rad1; 1.
DR PRINTS; PR01245; RAD1REC1.
DR PRINTS; PR01246; RAD1REPAIR.
PE 2: Evidence at transcript level;
KW DNA damage; DNA repair; Exonuclease; Hydrolase; Nuclease; Nucleus;
KW Reference proteome.
FT CHAIN 1..282
FT /note="Cell cycle checkpoint protein RAD1"
FT /id="PRO_0000225007"
SQ SEQUENCE 282 AA; 31827 MW; 075FBD4CF8A4FDB2 CRC64;
MPLLTQQIQD EDDQYSLVAS LDNVRNLSTI LKAIHFREHA TCFATKNGIK VTVENAKCVQ
ANAFIQAGIF QEFKVQEESV TFRINLTVLL DCLSIFGSSP MPGTLTALRM CYQGYGYPLM
LFLEEGGVVT VCKINTQEPE ETLDFDFCST NVINKIILQS EGLREAFSEL DMTSEVLQIT
MSPDKPYFRL STFGNAGSSH LDYPKDSDLM EAFHCNQTQV NRYKISLLKP STKALVLSCK
VSIRTDNRGF LSLQYMIRNE DGQICFVEYY CCPDEEVPES ES