ID   ABHD1_RAT               Reviewed;         412 AA.
AC   Q5RK23;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
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|RGD:1310988};
GN   Name=Abhd1 {ECO:0000312|RGD:1310988};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 4
CC       family. {ECO:0000305}.
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DR   EMBL; BC086351; AAH86351.1; -; mRNA.
DR   RefSeq; NP_001008520.1; NM_001008520.1.
DR   AlphaFoldDB; Q5RK23; -.
DR   STRING; 10116.ENSRNOP00000009339; -.
DR   ESTHER; ratno-abhd1; abh_upf0017.
DR   GlyGen; Q5RK23; 1 site.
DR   PhosphoSitePlus; Q5RK23; -.
DR   PaxDb; Q5RK23; -.
DR   Ensembl; ENSRNOT00000010403; ENSRNOP00000009339; ENSRNOG00000025689.
DR   GeneID; 313917; -.
DR   KEGG; rno:313917; -.
DR   CTD; 84696; -.
DR   RGD; 1310988; Abhd1.
DR   eggNOG; KOG1838; Eukaryota.
DR   GeneTree; ENSGT00950000182902; -.
DR   HOGENOM; CLU_032487_4_0_1; -.
DR   InParanoid; Q5RK23; -.
DR   OMA; NYCGEEG; -.
DR   OrthoDB; 1162019at2759; -.
DR   PhylomeDB; Q5RK23; -.
DR   TreeFam; TF313195; -.
DR   PRO; PR:Q5RK23; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000025689; Expressed in duodenum and 19 other tissues.
DR   Genevisible; Q5RK23; RN.
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   2: Evidence at transcript 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_0000280206"
FT   TRANSMEM        24..44
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;  45557 MW;  BA73008A6198E82B CRC64;
     MEYLHITKML SSSLSPQNGT WSDAISLLLA LGIALYLGYY WACVPQRPRL VAGPQFLAFL
     EQHCPVTVET FYPTLWCFEG RLQTIFRVLL QSQPVIPYRS EVLQTPDGGQ FLLDWAEQPY
     SSHCPDPTTQ PIVLLLPGIS GSSQEPYILH LVDQALKDGY RAVVFNNRGC RGEELLTHRA
     YCASNTEDLE TVVKHIKHRY SRAPLLAVGI SFGGILVLNY LARTGKAGGL VAGLTMSACW
     DSFETVDSLE TPLNSLLFNQ PLTAGLCRLV ARNRKSIEKV LDVDFAIKAR TIRQLDERYT
     SVAFGYKDCA AYYHASSPRT KVDAICTPVL CLNAADDPFS PVQALPLQAA QKSPYVALLI
     TARGGHIGFL EGLLPWQHCY MNRVLHQYAR AVFQHSVGLP GLGALTPEDG KS