ABHD8_MOUSE
ID ABHD8_MOUSE Reviewed; 439 AA.
AC Q8R0P8; Q9DC79; Q9JMF5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Protein ABHD8 {ECO:0000305};
DE EC=3.-.-.-;
DE AltName: Full=Alpha/beta hydrolase domain-containing protein 8 {ECO:0000305};
DE Short=Abhydrolase domain-containing protein 8 {ECO:0000312|MGI:MGI:1918946};
GN Name=Abhd8 {ECO:0000312|MGI:MGI:1918946};
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 [MRNA].
RC TISSUE=Brain;
RX PubMed=10679242; DOI=10.1006/bbrc.2000.2170;
RA Inoue S., Sano H., Ohta M.;
RT "Growth suppression of Escherichia coli by induction of expression of
RT mammalian genes with transmembrane or ATPase domains.";
RL Biochem. Biophys. Res. Commun. 268:553-561(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Spleen;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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).
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-7 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AB030191; BAA92755.1; -; mRNA.
DR EMBL; AK003090; BAB22558.1; -; mRNA.
DR EMBL; AK155503; BAE33297.1; -; mRNA.
DR EMBL; BC026540; AAH26540.1; -; mRNA.
DR CCDS; CCDS40382.1; -.
DR RefSeq; NP_071864.2; NM_022419.3.
DR AlphaFoldDB; Q8R0P8; -.
DR SMR; Q8R0P8; -.
DR IntAct; Q8R0P8; 1.
DR STRING; 10090.ENSMUSP00000008094; -.
DR ESTHER; mouse-Abhd8; ABHD8.
DR MEROPS; S33.011; -.
DR iPTMnet; Q8R0P8; -.
DR PhosphoSitePlus; Q8R0P8; -.
DR EPD; Q8R0P8; -.
DR PaxDb; Q8R0P8; -.
DR PRIDE; Q8R0P8; -.
DR ProteomicsDB; 286054; -.
DR Antibodypedia; 51446; 132 antibodies from 25 providers.
DR DNASU; 64296; -.
DR Ensembl; ENSMUST00000008094; ENSMUSP00000008094; ENSMUSG00000007950.
DR GeneID; 64296; -.
DR KEGG; mmu:64296; -.
DR UCSC; uc009mdf.2; mouse.
DR CTD; 79575; -.
DR MGI; MGI:1918946; Abhd8.
DR VEuPathDB; HostDB:ENSMUSG00000007950; -.
DR eggNOG; KOG2382; Eukaryota.
DR GeneTree; ENSGT00390000007336; -.
DR HOGENOM; CLU_057347_0_0_1; -.
DR InParanoid; Q8R0P8; -.
DR OMA; HCQRRIT; -.
DR OrthoDB; 729023at2759; -.
DR PhylomeDB; Q8R0P8; -.
DR TreeFam; TF331708; -.
DR BioGRID-ORCS; 64296; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Abhd8; mouse.
DR PRO; PR:Q8R0P8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8R0P8; protein.
DR Bgee; ENSMUSG00000007950; Expressed in perirhinal cortex and 198 other tissues.
DR Genevisible; Q8R0P8; MM.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IBA:GO_Central.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..439
FT /note="Protein ABHD8"
FT /id="PRO_0000281384"
FT DOMAIN 169..271
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT REGION 54..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..72
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 244
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 362
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 390
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CONFLICT 84
FT /note="R -> P (in Ref. 2; BAB22558)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="S -> F (in Ref. 1; BAA92755)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 48229 MW; A3FDE2A1174C2481 CRC64;
MTSEHTMLTG VTDGFFCCLL GTPPNAVRPL ESVESSDGYT FVEVKPGRVL RVKHAGPAPI
PTPPPPPPED DPGVKTGLVR CQRRITVYRN GRLVVENLGR APRADLQGRS GSGDPPAALE
VELAEPAGGD TRANPGSGRR RRPRRPKRTI HIDCEQRITS CKGAQADVVL FFIHGVGGSL
AIWKEQLDFF VRLGYEVVAP DLAGHGASSA PQVAAAYTFY ALAEDMRAIF TRYAKKRNVL
IGHSYGVSFC TFLAHEYPDL VHKVIMINGG GPTALEPSLC SIFNMPTCVL HCLSPCLAWS
FLKAGFARQG AKEKQLLKEG NAFNVSSFVL RAMMSGQYWP EGDEVYHAEL TVPVLLVHGM
HDKFVPVEED QRMAEILLLA FLKLIEEGSH MVMLECPETV NTLLHEFLLW EPEPEAEPKL
EPKPKPQLLQ PEPAPGEEK
