HAGHL_MOUSE
ID HAGHL_MOUSE Reviewed; 283 AA.
AC Q9DB32; Q8C8C4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Hydroxyacylglutathione hydrolase-like protein;
DE EC=3.1.2.-;
GN Name=Haghl;
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; TISSUE=Cerebellum;
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 STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Hydrolase acting on ester bonds. {ECO:0000305}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DB32-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DB32-2; Sequence=VSP_030057, VSP_030058;
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000305}.
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DR EMBL; AK005274; BAB23924.1; -; mRNA.
DR EMBL; AK047517; BAC33079.1; -; mRNA.
DR EMBL; BC030466; AAH30466.1; -; mRNA.
DR EMBL; BC083322; AAH83322.1; -; mRNA.
DR CCDS; CCDS28527.1; -. [Q9DB32-1]
DR CCDS; CCDS70773.1; -. [Q9DB32-2]
DR RefSeq; NP_001258362.1; NM_001271433.1. [Q9DB32-1]
DR RefSeq; NP_001258364.1; NM_001271435.1. [Q9DB32-2]
DR RefSeq; NP_081173.1; NM_026897.3. [Q9DB32-1]
DR AlphaFoldDB; Q9DB32; -.
DR SMR; Q9DB32; -.
DR BioGRID; 213153; 6.
DR STRING; 10090.ENSMUSP00000119647; -.
DR PhosphoSitePlus; Q9DB32; -.
DR MaxQB; Q9DB32; -.
DR PaxDb; Q9DB32; -.
DR PeptideAtlas; Q9DB32; -.
DR PRIDE; Q9DB32; -.
DR ProteomicsDB; 269710; -. [Q9DB32-1]
DR ProteomicsDB; 269711; -. [Q9DB32-2]
DR Antibodypedia; 59077; 165 antibodies from 13 providers.
DR DNASU; 68977; -.
DR Ensembl; ENSMUST00000077938; ENSMUSP00000077091; ENSMUSG00000061046. [Q9DB32-1]
DR Ensembl; ENSMUST00000140738; ENSMUSP00000116841; ENSMUSG00000061046. [Q9DB32-2]
DR Ensembl; ENSMUST00000150324; ENSMUSP00000119647; ENSMUSG00000061046. [Q9DB32-1]
DR GeneID; 68977; -.
DR KEGG; mmu:68977; -.
DR UCSC; uc008bbr.2; mouse. [Q9DB32-1]
DR UCSC; uc033hby.1; mouse. [Q9DB32-2]
DR CTD; 84264; -.
DR MGI; MGI:1919877; Haghl.
DR VEuPathDB; HostDB:ENSMUSG00000061046; -.
DR eggNOG; KOG0813; Eukaryota.
DR GeneTree; ENSGT00940000161924; -.
DR HOGENOM; CLU_030571_4_0_1; -.
DR InParanoid; Q9DB32; -.
DR OMA; CKERARF; -.
DR OrthoDB; 961826at2759; -.
DR PhylomeDB; Q9DB32; -.
DR TreeFam; TF105273; -.
DR BioGRID-ORCS; 68977; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Haghl; mouse.
DR PRO; PR:Q9DB32; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9DB32; protein.
DR Bgee; ENSMUSG00000061046; Expressed in ventral horn of spinal cord and 214 other tissues.
DR ExpressionAtlas; Q9DB32; baseline and differential.
DR Genevisible; Q9DB32; MM.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IEA:InterPro.
DR CDD; cd07723; hydroxyacylglutathione_hydrolase_MBL-fold; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR HAMAP; MF_01374; Glyoxalase_2; 1.
DR InterPro; IPR035680; Clx_II_MBL.
DR InterPro; IPR032282; HAGH_C.
DR InterPro; IPR017782; Hydroxyacylglutathione_Hdrlase.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF16123; HAGH_C; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR TIGRFAMs; TIGR03413; GSH_gloB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..283
FT /note="Hydroxyacylglutathione hydrolase-like protein"
FT /id="PRO_0000313602"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT VAR_SEQ 229..240
FT /note="EDAVRAFTGQVA -> QLQPRRLSSHCL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030057"
FT VAR_SEQ 241..283
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030058"
SQ SEQUENCE 283 AA; 31490 MW; 366329A46EF0C441 CRC64;
MKVKVIPVLE DNYMYLIIEE HTREAVAIDV AVAERLLEIA GREGVSLTMV LSTHHHWDHT
RGNAELAHIL PGLAVLGADE RICALTRRLE HGEGLQFGAI HVRCLLTPGH TSGHMSYFLW
EDDCPDSPAL FSGDALSVAG CGWHLEDTAQ QMYQSLAKTL GTLPPETKVF CGHEHTLSNL
EFAQKVEPCN EHVQAKLSWA QERDDEDIPT VPSTLGEELM YNPFLRVTED AVRAFTGQVA
PAQVLEALCR ERARFQPAVE PPQPQVRALL ALQWGLLSTH QKK
