ID   ABH15_MOUSE             Reviewed;         459 AA.
AC   Q5F2F2; Q3V371; Q8C9I5; Q8CF57; Q9CU23;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   29-MAY-2024, entry version 116.
DE   RecName: Full=Protein ABHD15 {ECO:0000305};
DE   AltName: Full=Alpha/beta hydrolase domain-containing protein 15 {ECO:0000305};
DE            Short=Abhydrolase domain-containing protein 15 {ECO:0000312|MGI:MGI:1914727};
DE   Flags: Precursor;
GN   Name=Abhd15 {ECO:0000312|MGI:MGI:1914727};
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=Adipose tissue, Liver, and Thymus;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, and Liver;
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   INDUCTION.
RX   PubMed=24236098; DOI=10.1371/journal.pone.0079134;
RA   Walenta E., Pessentheiner A.R., Pelzmann H.J., Deutsch A., Goeritzer M.,
RA   Kratky D., Hackl H., Oh D.Y., Prokesch A., Bogner-Strauss J.G.;
RT   "alpha/beta-hydrolase domain containing protein 15 (ABHD15)--an adipogenic
RT   protein protecting from apoptosis.";
RL   PLoS ONE 8:e79134-e79134(2013).
RN   [5]
RP   INTERACTION WITH PDE3B, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=29768196; DOI=10.1016/j.celrep.2018.04.055;
RA   Xia W., Pessentheiner A.R., Hofer D.C., Amor M., Schreiber R.,
RA   Schoiswohl G., Eichmann T.O., Walenta E., Itariu B., Prager G., Hackl H.,
RA   Stulnig T., Kratky D., Ruelicke T., Bogner-Strauss J.G.;
RT   "Loss of ABHD15 Impairs the Anti-lipolytic Action of Insulin by Altering
RT   PDE3B Stability and Contributes to Insulin Resistance.";
RL   Cell Rep. 23:1948-1961(2018).
RN   [6]
RP   FUNCTION.
RX   PubMed=31105056; DOI=10.1016/j.molmet.2019.05.002;
RA   Stoeckli J., Zadoorian A., Cooke K.C., Deshpande V., Yau B., Herrmann G.,
RA   Kebede M.A., Humphrey S.J., James D.E.;
RT   "ABHD15 regulates adipose tissue lipolysis and hepatic lipid
RT   accumulation.";
RL   Mol. Metab. 25:83-94(2019).
RN   [7]
RP   ERRATUM OF PUBMED:31105056.
RX   PubMed=33775605; DOI=10.1016/j.molmet.2021.101219;
RA   Stoeckli J., Zadoorian A., Cooke K.C., Deshpande V., Yau B., Herrmann G.,
RA   Kebede M.A., Humphrey S.J., James D.E.;
RT   "Corrigendum to 'ABHD15 regulates adipose tissue lipolysis and hepatic
RT   lipid accumulation' [Molecular Metabolism 25 (2019) p.83-94].";
RL   Mol. Metab. 48:101219-101219(2021).
CC   -!- FUNCTION: May regulate adipocyte lipolysis and liver lipid
CC       accumulation. {ECO:0000269|PubMed:31105056}.
CC   -!- SUBUNIT: Interacts with PDE3B; this interaction regulates PDE3B's
CC       stability and expression and, thereby, impacts the antilipolytic action
CC       of insulin. {ECO:0000269|PubMed:29768196}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Mainly expressed in adipocytes and adipose depots,
CC       followed by a weak expression in liver and pancreas (PubMed:29768196).
CC       In white adipose tissue (WAT), only expressed in mature adipocytes and
CC       primary adipocytes differentiated from stromal vascular cells (SVCs),
CC       but not in undifferentiated SVCs (PubMed:29768196).
CC       {ECO:0000269|PubMed:29768196}.
CC   -!- INDUCTION: Decreased by elevated free fatty acid levels and aging.
CC       {ECO:0000269|PubMed:24236098}.
CC   -!- DISRUPTION PHENOTYPE: Homozygous knockout mice lacking Abhd15 are
CC       fertile and newborn pups exhibit no obvious defects.
CC       {ECO:0000269|PubMed:29768196}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 4
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB31349.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAC25102.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK018696; BAB31349.1; ALT_FRAME; mRNA.
DR   EMBL; AK004929; BAC25102.1; ALT_FRAME; mRNA.
DR   EMBL; AK042032; BAC31138.1; -; mRNA.
DR   EMBL; AK046590; BAE20655.1; -; mRNA.
DR   EMBL; AL591136; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS36234.1; -.
DR   RefSeq; NP_080461.3; NM_026185.4.
DR   AlphaFoldDB; Q5F2F2; -.
DR   BioGRID; 212218; 1.
DR   STRING; 10090.ENSMUSP00000091541; -.
DR   ESTHER; mouse-ABH15; abh_upf0017.
DR   iPTMnet; Q5F2F2; -.
DR   PhosphoSitePlus; Q5F2F2; -.
DR   SwissPalm; Q5F2F2; -.
DR   EPD; Q5F2F2; -.
DR   jPOST; Q5F2F2; -.
DR   MaxQB; Q5F2F2; -.
DR   PaxDb; 10090-ENSMUSP00000091541; -.
DR   ProteomicsDB; 296434; -.
DR   Antibodypedia; 2595; 59 antibodies from 20 providers.
DR   DNASU; 67477; -.
DR   Ensembl; ENSMUST00000094004.5; ENSMUSP00000091541.5; ENSMUSG00000000686.12.
DR   GeneID; 67477; -.
DR   KEGG; mmu:67477; -.
DR   UCSC; uc007kha.1; mouse.
DR   AGR; MGI:1914727; -.
DR   CTD; 116236; -.
DR   MGI; MGI:1914727; Abhd15.
DR   VEuPathDB; HostDB:ENSMUSG00000000686; -.
DR   eggNOG; KOG1838; Eukaryota.
DR   GeneTree; ENSGT00950000182902; -.
DR   HOGENOM; CLU_032487_3_0_1; -.
DR   InParanoid; Q5F2F2; -.
DR   OMA; LPWLYER; -.
DR   OrthoDB; 2944016at2759; -.
DR   PhylomeDB; Q5F2F2; -.
DR   TreeFam; TF332985; -.
DR   BioGRID-ORCS; 67477; 2 hits in 76 CRISPR screens.
DR   ChiTaRS; Abhd15; mouse.
DR   PRO; PR:Q5F2F2; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q5F2F2; Protein.
DR   Bgee; ENSMUSG00000000686; Expressed in brown adipose tissue and 106 other cell types or tissues.
DR   ExpressionAtlas; Q5F2F2; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0047372; F:acylglycerol lipase activity; IBA:GO_Central.
DR   GO; GO:0034338; F:short-chain carboxylesterase activity; IBA:GO_Central.
DR   GO; GO:0060612; P:adipose tissue development; IDA:UniProtKB.
DR   GO; GO:0044255; P:cellular lipid metabolic process; IBA:GO_Central.
DR   GO; GO:0016042; P:lipid catabolic process; IMP:UniProtKB.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR012020; ABHD4.
DR   PANTHER; PTHR10794; ABHYDROLASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10794:SF39; PROTEIN ABHD15; 1.
DR   PIRSF; PIRSF005211; Ab_hydro_YheT; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..459
FT                   /note="Protein ABHD15"
FT                   /id="PRO_0000345396"
FT   ACT_SITE        351
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        382
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         425
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6UXT9"
FT   CONFLICT        106
FT                   /note="P -> L (in Ref. 1; BAB31349)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        147
FT                   /note="L -> H (in Ref. 1; BAE20655)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        305
FT                   /note="L -> V (in Ref. 1; BAB31349)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        308
FT                   /note="F -> C (in Ref. 1; BAB31349)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   459 AA;  51152 MW;  30D897F050943B82 CRC64;
     MPPWAAALAL LLAALALLLL RPWKRAVGAR TSVRDHEEQE VASGGPADQF SDRREALPGG
     CSLICKPSAL AQCLLRALRR SAALEPSPRS WLSGPHLQTF CHFILPVGPG PELAREYLQL
     ADDGLVALDW VIGPCARGRR VTNPGSLPPV LLVIPNAWGR LTRNVLGLCL LALERGYYPV
     IFHRRGHHGC PLVSPRLQPF GDPSDLKEAV TYIRFRHPAA PLFAVSEGSG SALLLSYLGE
     CGSSSYVTGA ACISPVLRCR EWFEAGLPWP YERGFLLHQK ISLSRYASAL EDTVDTGKLF
     RSGSLREFEE TLFCHTKSCP ISWDTYWDLN DPLRDVDEAA VPVLCICSAD DPVCGPPEHT
     LPAELFHSNP YFFLLLSHHG GHCGFLRPEP LPAWSHEVIL ESFRALTEFF RMEERMKGLS
     RRRTSFLGGR RRWGGLQKRE VSPSSNLEEI FNWKRSYTR
//