ID   SASB_ANAPL              Reviewed;         557 AA.
AC   Q04791;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Fatty acyl-CoA hydrolase precursor, medium chain;
DE            EC=3.1.2.-;
DE   AltName: Full=Thioesterase B;
DE   Flags: Precursor;
OS   Anas platyrhynchos (Mallard) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8839;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 26-65.
RC   TISSUE=Uropygial gland;
RX   PubMed=8314791; DOI=10.1016/s0021-9258(19)85238-9;
RA   Hwang C.-S., Kolattukudy P.E.;
RT   "Molecular cloning and sequencing of thioesterase B cDNA and stimulation of
RT   expression of the thioesterase B gene associated with hormonal induction of
RT   peroxisome proliferation.";
RL   J. Biol. Chem. 268:14278-14284(1993).
CC   -!- FUNCTION: Fatty acid biosynthesis chain termination and release of the
CC       free fatty acid product is achieved by hydrolysis of the thio ester by
CC       a thioesterase. This thioesterase may be associated with peroxisome
CC       proliferation and may play a role in the production of 3-hydroxy fatty
CC       acid diester pheromones.
CC   -!- TISSUE SPECIFICITY: Highest levels in uropygial gland, much lower in
CC       liver and kidney.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; L05493; AAA49223.1; -; mRNA.
DR   PIR; A47162; A47162.
DR   RefSeq; NP_001297334.1; NM_001310405.1.
DR   AlphaFoldDB; Q04791; -.
DR   SMR; Q04791; -.
DR   ESTHER; anapl-thioe; Carb_B_Chordata.
DR   MEROPS; S09.962; -.
DR   GeneID; 101790670; -.
DR   KEGG; apla:101790670; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Glycoprotein; Hydrolase; Lipid biosynthesis;
KW   Lipid metabolism; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:8314791"
FT   CHAIN           26..557
FT                   /note="Fatty acyl-CoA hydrolase precursor, medium chain"
FT                   /id="PRO_0000008634"
FT   ACT_SITE        227
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        345
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        460
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        476
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        93..122
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   557 AA;  61637 MW;  03E35D90A037F6B0 CRC64;
     MATEKNTLLS LILTAGITAL VATGQKAEQP EVVTNYGSVR GYQVKVNAAE RSVNVFLGLP
     FAKPPVGPLR FSEPQPPEPW KGVRDAASYP PMCLQDKVLG QYLSDAITNR KEKVRLQISE
     DCLYLNVYTP VSTEEQEKLP VFVWIHGGGL VSGAASSYDG SALAAFDNVV VVTIQYRLGI
     AGYFSTGDKH ARGNWGYLDQ VAALQWIQEN IIHFRGDPGS VTIFGESAGG VSVSALVLSP
     LAKGLFHKAI SESGTAVRIL FTEQPEEQAQ RIAAAAGCEK SSSAALVECL REKTEAEMEQ
     ITLKMPPMFI SASLDGVFFP KSPRQLLSEK VINAVPYIIG VNNCEFGWIL PRMMKFPEFT
     EGLEKDVARQ VLQSTLALSF KGAPSDIVDL VYNEYIGVAE NRAQVRDGLL DSIADPLFVF
     SAVEVARHHR DAGNPVYFYE FQHRPSSAAG VVPEFVKADH ADEIAFVFGK PFLAGNATEE
     EAKLSRTVMK YWTNFARNGN PNGEGLVHWP QYDMDERYLE IDLTQKAAKK LKERKMEFWM
     QLTEQIMSDR RRKHTDL