HDDC2_DANRE
ID HDDC2_DANRE Reviewed; 200 AA.
AC Q1LUI2; Q502C2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=5'-deoxynucleotidase HDDC2;
DE EC=3.1.3.89 {ECO:0000250|UniProtKB:P53144};
DE AltName: Full=HD domain-containing protein 2;
GN Name=hddc2; ORFNames=si:ch211-208c9.2, zgc:112330;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2005) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH95766.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX936317; CAK04454.1; -; Genomic_DNA.
DR EMBL; BC095766; AAH95766.1; ALT_INIT; mRNA.
DR RefSeq; NP_001038696.1; NM_001045231.1.
DR AlphaFoldDB; Q1LUI2; -.
DR STRING; 7955.ENSDARP00000050728; -.
DR PaxDb; Q1LUI2; -.
DR Ensembl; ENSDART00000050729; ENSDARP00000050728; ENSDARG00000034957.
DR GeneID; 554129; -.
DR KEGG; dre:554129; -.
DR CTD; 51020; -.
DR ZFIN; ZDB-GENE-050522-394; hddc2.
DR eggNOG; KOG3197; Eukaryota.
DR GeneTree; ENSGT00390000009937; -.
DR HOGENOM; CLU_039453_2_1_1; -.
DR InParanoid; Q1LUI2; -.
DR OMA; YEKRDNI; -.
DR OrthoDB; 1363142at2759; -.
DR PhylomeDB; Q1LUI2; -.
DR TreeFam; TF313855; -.
DR PRO; PR:Q1LUI2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000034957; Expressed in mature ovarian follicle and 28 other tissues.
DR ExpressionAtlas; Q1LUI2; 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 Cobalt; Hydrolase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..200
FT /note="5'-deoxynucleotidase HDDC2"
FT /id="PRO_0000311391"
FT DOMAIN 33..135
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT BINDING 36
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT BINDING 64
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT BINDING 65
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT BINDING 68
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT BINDING 73
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT BINDING 74
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
FT BINDING 130
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4H3"
SQ SEQUENCE 200 AA; 22919 MW; 3165976D8A764C47 CRC64;
MDNMLQFMKL VGQLKRVPRT GWVYRNIKQP ESVSDHMYRM SMMALTIQDI SVNKERCMKL
ALVHDLAECI VGDIAPADNV SKAEKHRREK DAMVHITGLL DDGLRKEIYN LWEEYETQSS
PEAKLVKELD NLEMIIQAHE YEELEGKPGR LQEFFVSTEG KFHHPEVLGL LKSLNEERAR
HIAAGGEKTT DTDSLTLAKP
