ABHD1_MOUSE
ID ABHD1_MOUSE Reviewed; 412 AA.
AC Q9QZC8;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Protein ABHD1 {ECO:0000305};
DE EC=3.1.1.-;
DE AltName: Full=Alpha/beta hydrolase domain-containing protein 1 {ECO:0000305};
DE Short=Abhydrolase domain-containing protein 1 {ECO:0000312|MGI:MGI:1931013};
DE AltName: Full=Lung alpha/beta hydrolase 1;
DE Short=MmLABH1;
GN Name=Abhd1 {ECO:0000312|MGI:MGI:1931013}; Synonyms=Labh1;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Lung;
RX PubMed=11922611; DOI=10.1006/bbrc.2002.6692;
RA Edgar A.J., Polak J.M.;
RT "Cloning and tissue distribution of three murine alpha/beta hydrolase fold
RT protein cDNAs.";
RL Biochem. Biophys. Res. Commun. 292:617-625(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=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=Colon;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, 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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in liver.
CC {ECO:0000269|PubMed:11922611}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryos from 7 dpc to 17 dpc.
CC {ECO:0000269|PubMed:11922611}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 4
CC family. {ECO:0000305}.
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DR EMBL; AF189764; AAF01068.2; -; mRNA.
DR EMBL; AK156413; BAE33704.1; -; mRNA.
DR EMBL; BC013505; AAH13505.1; -; mRNA.
DR RefSeq; NP_067279.2; NM_021304.3.
DR AlphaFoldDB; Q9QZC8; -.
DR ESTHER; mouse-abhd1; abh_upf0017.
DR GlyGen; Q9QZC8; 1 site.
DR PhosphoSitePlus; Q9QZC8; -.
DR SwissPalm; Q9QZC8; -.
DR MaxQB; Q9QZC8; -.
DR PeptideAtlas; Q9QZC8; -.
DR PRIDE; Q9QZC8; -.
DR ProteomicsDB; 285825; -.
DR DNASU; 57742; -.
DR GeneID; 57742; -.
DR KEGG; mmu:57742; -.
DR UCSC; uc008wwp.1; mouse.
DR CTD; 84696; -.
DR MGI; MGI:1931013; Abhd1.
DR InParanoid; Q9QZC8; -.
DR PhylomeDB; Q9QZC8; -.
DR BioGRID-ORCS; 57742; 2 hits in 17 CRISPR screens.
DR PRO; PR:Q9QZC8; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9QZC8; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008126; F:acetylesterase activity; IBA:GO_Central.
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:0044255; P:cellular lipid metabolic process; IBA:GO_Central.
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 Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR012020; ABHD4.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF005211; Ab_hydro_YheT; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Membrane; Reference proteome; Serine esterase;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..412
FT /note="Protein ABHD1"
FT /id="PRO_0000280205"
FT TRANSMEM 25..45
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 131..372
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 211
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 337
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 366
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 412 AA; 45725 MW; 22C8C41ECCBB9213 CRC64;
MEYPYTTKML SSSLSPQNGT WSDTISLLLA LGVALYLGYY WACVPQRPRL VAGPQFLAFL
EQHCPVTVET FYPTLWCFEG RLQTIFRVLL QSQPVVPYRS EVLQTPDGGQ FLLDWAEQPN
STHYPDPTTQ PIVLLLPGIS GSSQEPYILH LVNQALKDGY RAVVFNNRGC RGEELLTHRA
YCASNTEDLE TVVKHIKRRY SQAPLLAVGI SFGGILVLNY LAQTGKAGGL VAGLTMSACW
DSFETVDSLE TPLNSLLFNQ PLTAGLCRLV ARNRKPIEKV LDVDFAIKAR TIRQLDERYT
SVAFGYKDCA AYYQAASPRT KVDAIHTPVL CLNAADDPFS PVHAFPLQAA QKSPYVALLI
TARGGHIGFL EGLMPWQHCY MNRVLHQYAR AIFQHSVGLP DLGVLTPEDG KS
