HDDC2_BOVIN
ID HDDC2_BOVIN Reviewed; 205 AA.
AC Q0P565;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=5'-deoxynucleotidase HDDC2 {ECO:0000305};
DE EC=3.1.3.89 {ECO:0000250|UniProtKB:P53144};
DE AltName: Full=HD domain-containing protein 2;
GN Name=HDDC2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the dephosphorylation of the nucleoside 5'-
CC monophosphates deoxyadenosine monophosphate (dAMP), deoxycytidine
CC monophosphate (dCMP), deoxyguanosine monophosphate (dGMP) and
CC deoxythymidine monophosphate (dTMP). {ECO:0000250|UniProtKB:P53144}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-
CC deoxyribonucleoside + phosphate; Xref=Rhea:RHEA:36167,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:18274, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:65317; EC=3.1.3.89;
CC Evidence={ECO:0000250|UniProtKB:P53144};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P53144};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:P53144};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P53144};
CC Note=Binds 2 divalent metal cations (By similarity). Shows activity
CC with Mn(2+), Co(2+) and Mg(2+) but shows no activity with Zn(2+) (By
CC similarity). {ECO:0000250|UniProtKB:P53144,
CC ECO:0000250|UniProtKB:Q7Z4H3};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P53144}.
CC -!- SIMILARITY: Belongs to the HDDC2 family. {ECO:0000305}.
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DR EMBL; BC120449; AAI20450.1; -; mRNA.
DR RefSeq; NP_001068869.1; NM_001075401.1.
DR AlphaFoldDB; Q0P565; -.
DR SMR; Q0P565; -.
DR STRING; 9913.ENSBTAP00000004334; -.
DR PaxDb; Q0P565; -.
DR PRIDE; Q0P565; -.
DR Ensembl; ENSBTAT00000004334; ENSBTAP00000004334; ENSBTAG00000003340.
DR GeneID; 509282; -.
DR KEGG; bta:509282; -.
DR CTD; 51020; -.
DR VEuPathDB; HostDB:ENSBTAG00000003340; -.
DR VGNC; VGNC:29785; HDDC2.
DR eggNOG; KOG3197; Eukaryota.
DR GeneTree; ENSGT00390000009937; -.
DR HOGENOM; CLU_039453_2_2_1; -.
DR InParanoid; Q0P565; -.
DR OMA; YEKRDNI; -.
DR OrthoDB; 1363142at2759; -.
DR TreeFam; TF313855; -.
DR Proteomes; UP000009136; Chromosome 9.
DR Bgee; ENSBTAG00000003340; Expressed in caput epididymis and 104 other tissues.
DR ExpressionAtlas; Q0P565; baseline.
DR GO; GO:0002953; F:5'-deoxynucleotidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR039356; YfbR/HDDC2.
DR PANTHER; PTHR11845; PTHR11845; 1.
DR Pfam; PF13023; HD_3; 1.
DR SMART; SM00471; HDc; 1.
DR PROSITE; PS51831; HD; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cobalt; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT CHAIN 2..205
FT /note="5'-deoxynucleotidase HDDC2"
FT /id="PRO_0000311388"
FT DOMAIN 47..149
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT BINDING 50
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT BINDING 78
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT BINDING 79
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT BINDING 82
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT BINDING 87
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT BINDING 88
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT BINDING 144
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
SQ SEQUENCE 205 AA; 23323 MW; C71E9CA9E249FC5C CRC64;
MASASPVATM SGRGARNLLQ FLRLVGQLKR VPRTGWVYRN VQKPESVSDH MYRMAVMALV
TKDEHLNKDR CVRLALVHDM AECIVGDIAP ADNVPREEKH RREEEAMKQL TQLLPEDLQK
ELYELWEEYE TQSSAEAKFV KQLDQCEMIL QASEYEDLEN KPGRLQDFYD STAGKFSHPE
IVQLVSELEA ERNANIAGAA SEPCS
