ID   TE2_HUMLU               Reviewed;         437 AA.
AC   S4TDL2;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2013, sequence version 1.
DT   29-SEP-2021, entry version 12.
DE   RecName: Full=Acyl-coenzyme A thioesterase 2, chloroplastic {ECO:0000303|PubMed:23300257};
DE            Short=Acyl-CoA thioesterase 2 {ECO:0000303|PubMed:23300257};
DE            Short=HlTE2 {ECO:0000303|PubMed:23300257};
DE            EC=3.1.2.- {ECO:0000250|UniProtKB:Q32MW3};
DE   AltName: Full=Acyl-CoA thioester hydrolase 2 {ECO:0000303|PubMed:23300257};
DE   Flags: Precursor;
GN   Name=TE2 {ECO:0000303|PubMed:23300257};
OS   Humulus lupulus (European hop).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Cannabaceae; Humulus.
OX   NCBI_TaxID=3486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GENE FAMILY, AND
RP   NOMENCLATURE.
RC   STRAIN=cv. Nugget;
RX   PubMed=23300257; DOI=10.1093/mp/sst004;
RA   Xu H., Zhang F., Liu B., Huhman D.V., Sumner L.W., Dixon R.A., Wang G.;
RT   "Characterization of the formation of branched short-chain fatty acid:CoAs
RT   for bitter acid biosynthesis in hop glandular trichomes.";
RL   Mol. Plant 6:1301-1317(2013).
CC   -!- FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze
CC       the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A
CC       (CoASH), providing the potential to regulate intracellular levels of
CC       acyl-CoAs, free fatty acids and CoASH. {ECO:0000250|UniProtKB:S4TF94}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed at low levels in glandular
CC       trichomes (lupulin glands), and, to a lower extent, in stems, leaves,
CC       flowers and cones. {ECO:0000269|PubMed:23300257}.
CC   -!- SIMILARITY: Belongs to the acyl coenzyme A hydrolase family.
CC       {ECO:0000305}.
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DR   EMBL; JX878392; AGA17932.1; -; mRNA.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR033120; HOTDOG_ACOT.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   SUPFAM; SSF54637; SSF54637; 2.
DR   PROSITE; PS51770; HOTDOG_ACOT; 2.
PE   2: Evidence at transcript level;
KW   Chloroplast; Hydrolase; Plastid; Repeat; Transit peptide.
FT   TRANSIT         1..13
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           14..437
FT                   /note="Acyl-coenzyme A thioesterase 2, chloroplastic"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000452961"
FT   DOMAIN          89..211
FT                   /note="HotDog ACOT-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT   DOMAIN          287..404
FT                   /note="HotDog ACOT-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
SQ   SEQUENCE   437 AA;  49163 MW;  AD38D018AA9A1C63 CRC64;
     MDLSSSPNHP ITVVSTFASP FEGPPSVGDS NSSARKPISL WPGMYHSPVT NALWEARCKI
     FERLLDPPKD APPQSELLTK TPSQSRTTIL YNFSTDYILR EQYRDPWNEV RIGKLLEDLD
     ALAGTISVKH CSDDDSTTRP LLLVTASVDK IVLKKPISVD IDLKIVGAVI WVGRSSIEIQ
     LEVSQSTKEG SNAADDVALS ANFIFVARDS KTAKAAPVNR LSPETEQEKL LFDEAEARSS
     MRKRKRGDQE RREFENGEAN RLQTLLAEGR IFCDMPALAD RDSILLRDTR QENSLICQPQ
     QRNIHGRIFG GFLLHRAFEL AFSTAYAFAG LVPYFLEIDH VDFXRPVDVG DFLRLKSCVL
     YTELHNPDQP LINIEVVAHV TRPELRSSEV SNTFYFTFTV RPEAKATKNG YRIRNVVPAT
     EEEARRILER MDAEACI