ID IAH1_MOUSE Reviewed; 249 AA.
AC Q9DB29;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 142.
DE RecName: Full=Isoamyl acetate-hydrolyzing esterase 1 homolog;
DE EC=3.1.-.-;
GN Name=Iah1;
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].
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].
RC TISSUE=Brain, and Kidney;
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, 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 [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-63, 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).
CC -!- FUNCTION: Probable lipase. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family. IAH1
CC subfamily. {ECO:0000305}.
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DR EMBL; AK005287; BAB23934.1; -; mRNA.
DR EMBL; BC060949; AAH60949.1; -; mRNA.
DR EMBL; BC087901; AAH87901.1; -; mRNA.
DR CCDS; CCDS25835.1; -.
DR RefSeq; NP_080623.2; NM_026347.3.
DR AlphaFoldDB; Q9DB29; -.
DR SMR; Q9DB29; -.
DR IntAct; Q9DB29; 1.
DR MINT; Q9DB29; -.
DR STRING; 10090.ENSMUSP00000076090; -.
DR iPTMnet; Q9DB29; -.
DR PhosphoSitePlus; Q9DB29; -.
DR SwissPalm; Q9DB29; -.
DR REPRODUCTION-2DPAGE; IPI00119004; -.
DR EPD; Q9DB29; -.
DR jPOST; Q9DB29; -.
DR MaxQB; Q9DB29; -.
DR PaxDb; 10090-ENSMUSP00000076090; -.
DR PeptideAtlas; Q9DB29; -.
DR ProteomicsDB; 267035; -.
DR Pumba; Q9DB29; -.
DR Antibodypedia; 47292; 124 antibodies from 23 providers.
DR DNASU; 67732; -.
DR Ensembl; ENSMUST00000076813.8; ENSMUSP00000076090.7; ENSMUSG00000062054.8.
DR GeneID; 67732; -.
DR KEGG; mmu:67732; -.
DR UCSC; uc007nds.1; mouse.
DR AGR; MGI:1914982; -.
DR CTD; 285148; -.
DR MGI; MGI:1914982; Iah1.
DR VEuPathDB; HostDB:ENSMUSG00000062054; -.
DR eggNOG; KOG3035; Eukaryota.
DR GeneTree; ENSGT00390000008069; -.
DR HOGENOM; CLU_051989_0_2_1; -.
DR InParanoid; Q9DB29; -.
DR OMA; HEPAWEK; -.
DR OrthoDB; 1106721at2759; -.
DR PhylomeDB; Q9DB29; -.
DR TreeFam; TF328918; -.
DR BioGRID-ORCS; 67732; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Iah1; mouse.
DR PRO; PR:Q9DB29; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9DB29; Protein.
DR Bgee; ENSMUSG00000062054; Expressed in right kidney and 248 other cell types or tissues.
DR ExpressionAtlas; Q9DB29; baseline and differential.
DR Genevisible; Q9DB29; MM.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd01838; Isoamyl_acetate_hydrolase_like; 1.
DR Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR045136; Iah1-like.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR PANTHER; PTHR14209; ISOAMYL ACETATE-HYDROLYZING ESTERASE 1; 1.
DR PANTHER; PTHR14209:SF19; ISOAMYL ACETATE-HYDROLYZING ESTERASE 1 HOMOLOG; 1.
DR Pfam; PF00657; Lipase_GDSL; 1.
DR SUPFAM; SSF52266; SGNH hydrolase; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Lipid degradation; Lipid metabolism; Reference proteome.
FT CHAIN 1..249
FT /note="Isoamyl acetate-hydrolyzing esterase 1 homolog"
FT /id="PRO_0000315724"
FT ACT_SITE 24
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P41734"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P41734"
FT ACT_SITE 200
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P41734"
FT SITE 56
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P41734"
FT SITE 89
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P41734"
FT MOD_RES 63
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 249 AA; 27974 MW; 45E9C8FE068F8423 CRC64;
MSLCERAASG SALLWPRVLL FGDSITQFSF QQGGWGSLLA DRLVRKCDVL NRGFSGYNTR
WAKIILPRLI RKGPGMENPV AVTIFFGAND SSLKDENPKQ HVPLDEYSAN LRDMVQYLRS
VDVPRERVIL ITPPPLCEAA WEKECVLKGC KLNRLNSVVG EYANACLQVA RDCGTDVLDL
WTLMQKDSQD FSSYLSDGLH LSPMGNEFLF LNLCPLLDKK VSSLPWLLPY WKDVEEAKPE
LSLLGDGDY
//
