HDHD2_MOUSE
ID HDHD2_MOUSE Reviewed; 259 AA.
AC Q3UGR5; Q3U8M0; Q6PEB2; Q9CXN1; Q9DCF2;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Haloacid dehalogenase-like hydrolase domain-containing protein 2;
GN Name=Hdhd2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, Head, Kidney, Melanocyte, and Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 9-33; 63-80 AND 183-190, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-50, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2-259 IN COMPLEX WITH MAGNESIUM
RP AND PHOSPHATE IONS.
RG Center for eukaryotic structural genomics (CESG);
RT "Crystal structure of protein from mouse mm.236127.";
RL Submitted (AUG-2006) to the PDB data bank.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UGR5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UGR5-2; Sequence=VSP_025374, VSP_025375;
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB22395.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK002837; BAB22395.1; ALT_FRAME; mRNA.
DR EMBL; AK014208; BAB29206.1; -; mRNA.
DR EMBL; AK137285; BAE23293.1; -; mRNA.
DR EMBL; AK147794; BAE28142.1; -; mRNA.
DR EMBL; AK151285; BAE30270.1; -; mRNA.
DR EMBL; AK152162; BAE30997.1; -; mRNA.
DR EMBL; AK152259; BAE31078.1; -; mRNA.
DR EMBL; BC058177; AAH58177.1; -; mRNA.
DR CCDS; CCDS37863.1; -. [Q3UGR5-1]
DR CCDS; CCDS37864.1; -. [Q3UGR5-2]
DR RefSeq; NP_001034290.1; NM_001039201.1. [Q3UGR5-1]
DR RefSeq; NP_001034291.1; NM_001039202.1. [Q3UGR5-2]
DR RefSeq; NP_084102.1; NM_029826.2. [Q3UGR5-1]
DR RefSeq; XP_006526505.1; XM_006526442.3.
DR PDB; 2HO4; X-ray; 2.20 A; A/B=2-259.
DR PDBsum; 2HO4; -.
DR AlphaFoldDB; Q3UGR5; -.
DR SMR; Q3UGR5; -.
DR BioGRID; 218444; 5.
DR IntAct; Q3UGR5; 1.
DR MINT; Q3UGR5; -.
DR STRING; 10090.ENSMUSP00000114212; -.
DR iPTMnet; Q3UGR5; -.
DR PhosphoSitePlus; Q3UGR5; -.
DR EPD; Q3UGR5; -.
DR jPOST; Q3UGR5; -.
DR MaxQB; Q3UGR5; -.
DR PaxDb; Q3UGR5; -.
DR PeptideAtlas; Q3UGR5; -.
DR PRIDE; Q3UGR5; -.
DR ProteomicsDB; 269652; -. [Q3UGR5-1]
DR ProteomicsDB; 269653; -. [Q3UGR5-2]
DR Antibodypedia; 22539; 256 antibodies from 20 providers.
DR DNASU; 76987; -.
DR Ensembl; ENSMUST00000026485; ENSMUSP00000026485; ENSMUSG00000025421. [Q3UGR5-1]
DR Ensembl; ENSMUST00000097521; ENSMUSP00000095128; ENSMUSG00000025421. [Q3UGR5-2]
DR Ensembl; ENSMUST00000097522; ENSMUSP00000095129; ENSMUSG00000025421. [Q3UGR5-1]
DR Ensembl; ENSMUST00000145634; ENSMUSP00000123320; ENSMUSG00000025421. [Q3UGR5-1]
DR Ensembl; ENSMUST00000148955; ENSMUSP00000116243; ENSMUSG00000025421. [Q3UGR5-1]
DR Ensembl; ENSMUST00000150990; ENSMUSP00000114212; ENSMUSG00000025421. [Q3UGR5-1]
DR GeneID; 76987; -.
DR KEGG; mmu:76987; -.
DR UCSC; uc008fqs.1; mouse. [Q3UGR5-2]
DR UCSC; uc008fqt.1; mouse. [Q3UGR5-1]
DR CTD; 84064; -.
DR MGI; MGI:1924237; Hdhd2.
DR VEuPathDB; HostDB:ENSMUSG00000025421; -.
DR eggNOG; KOG3040; Eukaryota.
DR GeneTree; ENSGT00940000155805; -.
DR HOGENOM; CLU_043473_4_0_1; -.
DR InParanoid; Q3UGR5; -.
DR OMA; PNPYFFE; -.
DR OrthoDB; 1088513at2759; -.
DR PhylomeDB; Q3UGR5; -.
DR TreeFam; TF314344; -.
DR BioGRID-ORCS; 76987; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Hdhd2; mouse.
DR EvolutionaryTrace; Q3UGR5; -.
DR PRO; PR:Q3UGR5; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q3UGR5; protein.
DR Bgee; ENSMUSG00000025421; Expressed in right kidney and 159 other tissues.
DR Genevisible; Q3UGR5; MM.
DR GO; GO:0019899; F:enzyme binding; ISS:CAFA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd07509; HAD_PPase; 1.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006357; HAD-SF_hydro_IIA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006355; LHPP/HDHD2.
DR Pfam; PF13344; Hydrolase_6; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01460; HAD-SF-IIA; 1.
DR TIGRFAMs; TIGR01458; HAD-SF-IIA-hyp3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Direct protein sequencing;
KW Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..259
FT /note="Haloacid dehalogenase-like hydrolase domain-
FT containing protein 2"
FT /id="PRO_0000287204"
FT COILED 47..72
FT /evidence="ECO:0000255"
FT BINDING 13..15
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|Ref.6"
FT BINDING 15
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|Ref.6"
FT BINDING 46..47
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="substrate"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 50
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 133..145
FT /note="LLLDGAPLIAIHK -> RKQRGQEEENSDSH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025374"
FT VAR_SEQ 146..259
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025375"
FT CONFLICT 52
FT /note="S -> T (in Ref. 2; AAH58177)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="L -> P (in Ref. 1; BAB22395)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="A -> T (in Ref. 1; BAE28142)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="P -> S (in Ref. 1; BAB22395)"
FT /evidence="ECO:0000305"
FT STRAND 9..18
FT /evidence="ECO:0007829|PDB:2HO4"
FT HELIX 28..36
FT /evidence="ECO:0007829|PDB:2HO4"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:2HO4"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:2HO4"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:2HO4"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2HO4"
FT HELIX 75..86
FT /evidence="ECO:0007829|PDB:2HO4"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:2HO4"
FT HELIX 96..102
FT /evidence="ECO:0007829|PDB:2HO4"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:2HO4"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:2HO4"
FT HELIX 124..135
FT /evidence="ECO:0007829|PDB:2HO4"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:2HO4"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:2HO4"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:2HO4"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:2HO4"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:2HO4"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:2HO4"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:2HO4"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:2HO4"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:2HO4"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:2HO4"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:2HO4"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:2HO4"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:2HO4"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:2HO4"
FT HELIX 247..257
FT /evidence="ECO:0007829|PDB:2HO4"
SQ SEQUENCE 259 AA; 28730 MW; C8E34D5F0D6C9AE8 CRC64;
MAARRALKAV LVDLNGTLHI EDAAVPGAQE ALKRLRATSV MVRFVTNTTK ESKKDLLERL
KKLEFEISED EIFTSLTAAR NLIEQKQVRP MLLVDDRALP EFTGVQTQDP NAVVIGLAPE
HFHYQLLNQA FRLLLDGAPL IAIHKARYYK RKDGLALGPG PFVTALEYAT DTKAMVVGKP
EKTFFLEALR DADCAPEEAV MIGDDCRDDV DGAQNIGMLG ILVKTGKYKA ADEEKINPPP
YLTCESFPHA VDHILQHLL
