ID A0A2K5V147_MACFA Unreviewed; 354 AA.
AC A0A2K5V147;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Abasic site processing protein HMCES {ECO:0000256|ARBA:ARBA00015888, ECO:0000256|RuleBase:RU364100};
DE Short=ES cell-specific 5hmC-binding protein {ECO:0000256|RuleBase:RU364100};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU364100};
DE AltName: Full=Embryonic stem cell-specific 5-hydroxymethylcytosine-binding protein {ECO:0000256|ARBA:ARBA00030390, ECO:0000256|RuleBase:RU364100};
DE AltName: Full=Peptidase HMCES {ECO:0000256|ARBA:ARBA00030898, ECO:0000256|RuleBase:RU364100};
DE AltName: Full=SRAP domain-containing protein 1 {ECO:0000256|ARBA:ARBA00031130, ECO:0000256|RuleBase:RU364100};
GN Name=HMCES {ECO:0000313|Ensembl:ENSMFAP00000018425.1};
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 {ECO:0000313|Ensembl:ENSMFAP00000018425.1, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000018425.1, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000018425.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Sensor of abasic sites in single-stranded DNA (ssDNA)
CC required to preserve genome integrity by promoting error-free repair of
CC abasic sites. Acts as an enzyme that recognizes and binds abasic sites
CC in ssDNA at replication forks and chemically modifies the lesion by
CC forming a covalent cross-link with DNA: forms a stable thiazolidine
CC linkage between a ring-opened abasic site and the alpha-amino and
CC sulfhydryl substituents of its N-terminal catalytic cysteine residue.
CC The HMCES DNA-protein cross-link is then degraded by the proteasome.
CC Promotes error-free repair of abasic sites by acting as a 'suicide'
CC enzyme that is degraded, thereby protecting abasic sites from
CC translesion synthesis (TLS) polymerases and endonucleases that are
CC error-prone and would generate mutations and double-strand breaks. Has
CC preference for ssDNA, but can also accommodate double-stranded DNA with
CC 3' or 5' overhang (dsDNA), and dsDNA-ssDNA 3' junction.
CC {ECO:0000256|RuleBase:RU364100}.
CC -!- SIMILARITY: Belongs to the SOS response-associated peptidase family.
CC {ECO:0000256|ARBA:ARBA00008136, ECO:0000256|RuleBase:RU364100}.
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 RefSeq; XP_005571788.1; XM_005571731.2.
DR AlphaFoldDB; A0A2K5V147; -.
DR SMR; A0A2K5V147; -.
DR STRING; 9541.ENSMFAP00000018425; -.
DR Ensembl; ENSMFAT00000068970.2; ENSMFAP00000018425.1; ENSMFAG00000032291.2.
DR GeneID; 102133139; -.
DR KEGG; mcf:102133139; -.
DR CTD; 56941; -.
DR VEuPathDB; HostDB:ENSMFAG00000032291; -.
DR GeneTree; ENSGT00390000018439; -.
DR OMA; SYNKGPQ; -.
DR OrthoDB; 204678at2759; -.
DR Proteomes; UP000233100; Chromosome 2.
DR Bgee; ENSMFAG00000032291; Expressed in lymph node and 13 other cell types or tissues.
DR GO; GO:0005657; C:replication fork; IEA:Ensembl.
DR GO; GO:0140431; F:DNA-(abasic site) binding; IEA:Ensembl.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0036297; P:interstrand cross-link repair; IEA:Ensembl.
DR GO; GO:0106300; P:protein-DNA covalent cross-linking repair; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; IEA:Ensembl.
DR Gene3D; 3.90.1680.10; SOS response associated peptidase-like; 1.
DR InterPro; IPR003738; SRAP.
DR InterPro; IPR036590; SRAP-like.
DR PANTHER; PTHR13604:SF0; ABASIC SITE PROCESSING PROTEIN HMCES; 1.
DR PANTHER; PTHR13604; DC12-RELATED; 1.
DR Pfam; PF02586; SRAP; 1.
DR SUPFAM; SSF143081; BB1717-like; 1.
PE 3: Inferred from homology;
KW Covalent protein-DNA linkage {ECO:0000256|ARBA:ARBA00023124};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364100};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364100};
KW Reference proteome {ECO:0000313|Proteomes:UP000233100}.
FT REGION 292..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 354 AA; 40529 MW; 00487B2C346D3615 CRC64;
MCGRTSCHLP RDVLTRACAY QDRRGQQRLP EWRDPDKYCP SYNKSPQSNS PVLLSRLHFE
KDADSSERII APMRWGLVPS WFKESDPSKL QFNTTNCRSD TIMEKRSFKV PLGKGRRCVV
LADGFYEWQR CQGTNQRQPY FIYFPQIKTE KSGSTGAADS PENWEKVWDN WRLLTMAGIF
DCWEPPEGGD VLYSYTIITV DSCKGLSDIH HRMPAILDGE EAVSKWLDFG EVSTQEALKL
IHSTENITFH AVSSVVNNSR NNTPECLAPV DLVVKKELKA SGSSQRMLQW LATKSPKKED
SKTPQKEESD VPQWSSQFLQ KSSLPTKRGT AGLLEQWLKR EKEEEPVAKR PYSQ
//