HMCES_CHICK
ID HMCES_CHICK Reviewed; 336 AA.
AC Q5ZJT1;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Abasic site processing protein HMCES {ECO:0000250|UniProtKB:Q96FZ2};
DE AltName: Full=Embryonic stem cell-specific 5-hydroxymethylcytosine-binding protein;
DE Short=ES cell-specific 5hmC-binding protein {ECO:0000250|UniProtKB:Q96FZ2};
DE AltName: Full=Peptidase HMCES {ECO:0000250|UniProtKB:Q8R1M0};
DE EC=3.4.-.- {ECO:0000250|UniProtKB:Q8R1M0};
DE AltName: Full=SRAP domain-containing protein 1 {ECO:0000250|UniProtKB:Q96FZ2};
GN Name=HMCES {ECO:0000250|UniProtKB:Q96FZ2};
GN Synonyms=SRAPD1 {ECO:0000250|UniProtKB:Q96FZ2};
GN ORFNames=RCJMB04_15p13 {ECO:0000303|PubMed:15642098};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 (By similarity).
CC Acts as a protease: mediates autocatalytic processing of its N-terminal
CC methionine in order to expose the catalytic cysteine (By similarity).
CC {ECO:0000250|UniProtKB:Q8R1M0, ECO:0000250|UniProtKB:Q96FZ2}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q96FZ2}.
CC Note=Recruited to chromatin following DNA damage. Localizes to
CC replication forks. {ECO:0000250|UniProtKB:Q96FZ2}.
CC -!- DOMAIN: Glu-127 is involved in sensing abasic sites in single-stranded
CC DNA (ssDNA). His-202 stabilizes the abasic sites by forming a hydrogen
CC bond with the O4' hydroxyl group. {ECO:0000250|UniProtKB:P76318}.
CC -!- SIMILARITY: Belongs to the SOS response-associated peptidase family.
CC {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; AJ720353; CAG32012.1; -; mRNA.
DR RefSeq; NP_001006137.1; NM_001006137.1.
DR AlphaFoldDB; Q5ZJT1; -.
DR SMR; Q5ZJT1; -.
DR STRING; 9031.ENSGALP00000009476; -.
DR PaxDb; Q5ZJT1; -.
DR GeneID; 416015; -.
DR KEGG; gga:416015; -.
DR CTD; 56941; -.
DR VEuPathDB; HostDB:geneid_416015; -.
DR eggNOG; KOG2618; Eukaryota.
DR InParanoid; Q5ZJT1; -.
DR OrthoDB; 1487237at2759; -.
DR PhylomeDB; Q5ZJT1; -.
DR PRO; PR:Q5ZJT1; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005657; C:replication fork; ISS:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0097681; P:double-strand break repair via alternative nonhomologous end joining; IEA:Ensembl.
DR GO; GO:0045830; P:positive regulation of isotype switching; ISS:UniProtKB.
DR GO; GO:0018142; P:protein-DNA covalent cross-linking; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1680.10; -; 1.
DR InterPro; IPR003738; SRAP.
DR InterPro; IPR036590; SRAP-like.
DR PANTHER; PTHR13604; PTHR13604; 1.
DR Pfam; PF02586; SRAP; 1.
DR SUPFAM; SSF143081; SSF143081; 1.
PE 2: Evidence at transcript level;
KW Autocatalytic cleavage; Chromosome; Covalent protein-DNA linkage;
KW DNA damage; DNA-binding; Hydrolase; Protease; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8R1M0"
FT CHAIN 2..336
FT /note="Abasic site processing protein HMCES"
FT /id="PRO_0000164398"
FT REGION 29..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q96FZ2"
FT SITE 127
FT /note="Required for sensing abasic sites"
FT /evidence="ECO:0000250|UniProtKB:P76318"
FT SITE 202
FT /note="Required to stabilize abasic sites"
FT /evidence="ECO:0000250|UniProtKB:P76318"
FT MOD_RES 2
FT /note="Thiazolidine linkage to a ring-opened DNA abasic
FT site"
FT /evidence="ECO:0000250|UniProtKB:Q96FZ2"
SQ SEQUENCE 336 AA; 38221 MW; E0DA4759B7E97DD6 CRC64;
MCGRTACSLG AARLRRACAY RDRQGRRQQP EWLREGRYRP SYNKGPQSSG PVLLSRKHVQ
QDADSSERVL MDMRWGLVPS WFKEDDPSKM QFKTSNCRSD TMLSKSSYKG PLLKGKRCVV
LADGFYEWQQ RGGGKQPYFI YFPQNKKHPA EEEEDSDEEW RGWRLLTMAG IFDCWEPPKG
GEPLYTYTII TVDASEDVSF IHHRMPAILD GDEAIEKWLD FAEVPTREAM KLIRPAENIA
FHPVSTFVNS VRNDTPECLV PIELGVPKEV KATASSKAML GWLKSSQEGS PQKKEDTLPR
WKSQFIHSPS PKKSSAGILR QWLGQEGGPP AKKQKA
