ABHD2_DROME
ID ABHD2_DROME Reviewed; 398 AA.
AC Q24093; Q9VQM6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Abhydrolase domain-containing protein 2;
DE EC=3.1.1.-;
GN Name=Hydr2; Synonyms=anon-23D, anon-23Da; ORFNames=CG3488;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chartoff E.H., Gelbart W.M.;
RT "Identification of a Drosophila gene with sequence similarity to human
RT pHPS1-2.";
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION, AND DEVELOPMENTAL STAGE.
RX PubMed=12612838; DOI=10.1007/s00239-002-2411-4;
RA Wisotzkey R.G., Johnson A.N., Takaesu N.T., Newfeld S.J.;
RT "Alpha/beta hydrolase2, a predicated gene adjacent to mad in Drosophila
RT melanogaster, belongs to a new global multigene family and is associated
RT with obesity.";
RL J. Mol. Evol. 56:351-361(2003).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos.
CC {ECO:0000269|PubMed:12612838}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 4
CC family. {ECO:0000305}.
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DR EMBL; U29170; AAA99735.1; -; mRNA.
DR EMBL; AE014134; AAF51139.1; -; Genomic_DNA.
DR EMBL; BT010082; AAQ22551.1; -; mRNA.
DR RefSeq; NP_001245852.1; NM_001258923.2.
DR RefSeq; NP_608751.2; NM_134907.4.
DR AlphaFoldDB; Q24093; -.
DR BioGRID; 59747; 4.
DR DIP; DIP-17906N; -.
DR IntAct; Q24093; 1.
DR STRING; 7227.FBpp0300634; -.
DR ESTHER; drome-abhd2; abh_upf0017.
DR PaxDb; Q24093; -.
DR DNASU; 33532; -.
DR EnsemblMetazoa; FBtr0077576; FBpp0077265; FBgn0014906.
DR EnsemblMetazoa; FBtr0308315; FBpp0300634; FBgn0014906.
DR GeneID; 33532; -.
DR KEGG; dme:Dmel_CG3488; -.
DR UCSC; CG3488-RA; d. melanogaster.
DR CTD; 33532; -.
DR FlyBase; FBgn0014906; Hydr2.
DR VEuPathDB; VectorBase:FBgn0014906; -.
DR eggNOG; KOG1838; Eukaryota.
DR GeneTree; ENSGT00950000182902; -.
DR InParanoid; Q24093; -.
DR OMA; YGHTDDY; -.
DR OrthoDB; 1033151at2759; -.
DR PhylomeDB; Q24093; -.
DR BioGRID-ORCS; 33532; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33532; -.
DR PRO; PR:Q24093; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0014906; Expressed in seminal fluid secreting gland and 12 other tissues.
DR ExpressionAtlas; Q24093; baseline and differential.
DR Genevisible; Q24093; DM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0036126; C:sperm flagellum; IBA:GO_Central.
DR GO; GO:0097524; C:sperm plasma membrane; IBA:GO_Central.
DR GO; GO:0008126; F:acetylesterase activity; IBA:GO_Central.
DR GO; GO:0047372; F:acylglycerol lipase activity; IBA:GO_Central.
DR GO; GO:0016298; F:lipase activity; IMP:FlyBase.
DR GO; GO:0034338; F:short-chain carboxylesterase activity; IBA:GO_Central.
DR GO; GO:0046464; P:acylglycerol catabolic process; IBA:GO_Central.
DR GO; GO:0044255; P:cellular lipid metabolic process; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IMP:FlyBase.
DR GO; GO:0051792; P:medium-chain fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0051793; P:medium-chain fatty acid catabolic process; IBA:GO_Central.
DR GO; GO:0048240; P:sperm capacitation; IBA:GO_Central.
DR GO; GO:0043401; P:steroid hormone mediated signaling pathway; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000952; AB_hydrolase_4_CS.
DR InterPro; IPR012020; ABHD4.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF005211; Ab_hydro_YheT; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS01133; UPF0017; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Membrane; Reference proteome; Serine esterase; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..398
FT /note="Abhydrolase domain-containing protein 2"
FT /id="PRO_0000212459"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..22
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..398
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 113..365
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 192
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 328
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 359
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CONFLICT 211
FT /note="D -> N (in Ref. 1; AAA99735)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="Y -> I (in Ref. 1; AAA99735)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 45402 MW; 89A2F30F8DE3ECDD CRC64;
MSTAFLTLIA VIVCILFRIL NVHSQPLKPS VWCLDAHFLD CLYKIAPVLR EPYIPPRLWG
FSGHVQTVLH SIVGRVRCPW PLGERVYMSL KDGSTLTYDL YQPLNEQEDD ITVAICPGIA
NSSESVYIRT FVHLAQCNGY RCAVLNHIGA LRSVQVTSTR IFTYGHTEDF AAMVEHLHQK
YRQSRIVAVG FSLGGNLVTK YMGEDQKTKP DKVIGGISIC QGYNAVEGTK WLLNWQNFRR
FYLYIMTENV KSIILRHRHI LLSDEVKARH NLNEREIIAA ATLPELDEAY TRRVYNFPST
QELYKWSSSL FYFDTIKKPM IFINAKDDPL IPEDLLHPIK EYATTRQNTA YVEVAHGGHL
GFYEGGFLYP NPVTWLDRTL VAMVGSLVMM HEVGKVAP
