IAH1_HUMAN
ID IAH1_HUMAN Reviewed; 248 AA.
AC Q2TAA2; B4DMV3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Isoamyl acetate-hydrolyzing esterase 1 homolog;
DE EC=3.1.-.-;
GN Name=IAH1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Probable lipase. {ECO:0000250}.
CC -!- INTERACTION:
CC Q2TAA2; Q2TAA2: IAH1; NbExp=5; IntAct=EBI-12379171, EBI-12379171;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2TAA2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2TAA2-2; Sequence=VSP_056571;
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family. IAH1
CC subfamily. {ECO:0000305}.
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DR EMBL; AK291984; BAF84673.1; -; mRNA.
DR EMBL; AK297648; BAG60015.1; -; mRNA.
DR EMBL; AC080162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAX00983.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00984.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00985.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00988.1; -; Genomic_DNA.
DR EMBL; BC111025; AAI11026.1; -; mRNA.
DR CCDS; CCDS42651.1; -. [Q2TAA2-1]
DR CCDS; CCDS82418.1; -. [Q2TAA2-2]
DR RefSeq; NP_001034702.1; NM_001039613.2. [Q2TAA2-1]
DR RefSeq; NP_001307787.1; NM_001320858.1.
DR RefSeq; NP_001307788.1; NM_001320859.1. [Q2TAA2-2]
DR RefSeq; NP_001307789.1; NM_001320860.1. [Q2TAA2-2]
DR RefSeq; NP_001307792.1; NM_001320863.1. [Q2TAA2-2]
DR RefSeq; XP_016859367.1; XM_017003878.1.
DR AlphaFoldDB; Q2TAA2; -.
DR SMR; Q2TAA2; -.
DR BioGRID; 130027; 20.
DR IntAct; Q2TAA2; 2.
DR STRING; 9606.ENSP00000417580; -.
DR GlyGen; Q2TAA2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q2TAA2; -.
DR PhosphoSitePlus; Q2TAA2; -.
DR BioMuta; IAH1; -.
DR DMDM; 121941741; -.
DR REPRODUCTION-2DPAGE; IPI00419194; -.
DR EPD; Q2TAA2; -.
DR jPOST; Q2TAA2; -.
DR MassIVE; Q2TAA2; -.
DR MaxQB; Q2TAA2; -.
DR PaxDb; Q2TAA2; -.
DR PeptideAtlas; Q2TAA2; -.
DR PRIDE; Q2TAA2; -.
DR ProteomicsDB; 4645; -.
DR ProteomicsDB; 61453; -. [Q2TAA2-1]
DR Antibodypedia; 47292; 104 antibodies from 23 providers.
DR DNASU; 285148; -.
DR Ensembl; ENST00000470914.5; ENSP00000419224.1; ENSG00000134330.19. [Q2TAA2-2]
DR Ensembl; ENST00000482918.5; ENSP00000419110.1; ENSG00000134330.19. [Q2TAA2-2]
DR Ensembl; ENST00000497473.6; ENSP00000417580.1; ENSG00000134330.19. [Q2TAA2-1]
DR GeneID; 285148; -.
DR KEGG; hsa:285148; -.
DR MANE-Select; ENST00000497473.6; ENSP00000417580.1; NM_001039613.3; NP_001034702.1.
DR UCSC; uc002qzr.4; human. [Q2TAA2-1]
DR CTD; 285148; -.
DR DisGeNET; 285148; -.
DR GeneCards; IAH1; -.
DR HGNC; HGNC:27696; IAH1.
DR HPA; ENSG00000134330; Low tissue specificity.
DR MalaCards; IAH1; -.
DR neXtProt; NX_Q2TAA2; -.
DR OpenTargets; ENSG00000134330; -.
DR PharmGKB; PA162391893; -.
DR VEuPathDB; HostDB:ENSG00000134330; -.
DR eggNOG; KOG3035; Eukaryota.
DR GeneTree; ENSGT00390000008069; -.
DR HOGENOM; CLU_152858_0_0_1; -.
DR InParanoid; Q2TAA2; -.
DR OMA; HEPAWEK; -.
DR OrthoDB; 1226154at2759; -.
DR PhylomeDB; Q2TAA2; -.
DR TreeFam; TF328918; -.
DR PathwayCommons; Q2TAA2; -.
DR SignaLink; Q2TAA2; -.
DR BioGRID-ORCS; 285148; 9 hits in 1070 CRISPR screens.
DR ChiTaRS; IAH1; human.
DR GenomeRNAi; 285148; -.
DR Pharos; Q2TAA2; Tbio.
DR PRO; PR:Q2TAA2; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q2TAA2; protein.
DR Bgee; ENSG00000134330; Expressed in secondary oocyte and 185 other tissues.
DR ExpressionAtlas; Q2TAA2; baseline and differential.
DR Genevisible; Q2TAA2; HS.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR045136; Iah1-like.
DR InterPro; IPR013830; SGNH_hydro.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR PANTHER; PTHR14209; PTHR14209; 1.
DR Pfam; PF13472; Lipase_GDSL_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome.
FT CHAIN 1..248
FT /note="Isoamyl acetate-hydrolyzing esterase 1 homolog"
FT /id="PRO_0000315723"
FT ACT_SITE 24
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P41734"
FT ACT_SITE 196
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P41734"
FT ACT_SITE 199
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:0000250|UniProtKB:Q9DB29"
FT VAR_SEQ 1..113
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056571"
SQ SEQUENCE 248 AA; 27599 MW; B21C1C0EC9F69778 CRC64;
MALCEAAGCG SALLWPRLLL FGDSITQFSF QQGGWGASLA DRLVRKCDVL NRGFSGYNTR
WAKIILPRLI RKGNSLDIPV AVTIFFGAND SALKDENPKQ HIPLEEYAAN LKSMVQYLKS
VDIPENRVIL ITPTPLCETA WEEQCIIQGC KLNRLNSVVG EYANACLQVA QDCGTDVLDL
WTLMQDSQDF SSYLSDGLHL SPKGNEFLFS HLWPLIEKKV SSLPLLLPYW RDVAEAKPEL
SLLGDGDH
