BACHL_HUMAN
ID BACHL_HUMAN Reviewed; 252 AA.
AC Q6ZUV0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Putative cytosolic acyl coenzyme A thioester hydrolase-like;
DE EC=3.1.2.2;
DE AltName: Full=Acyl-CoA thioesterase 7-like;
GN Name=ACOT7L; Synonyms=BACHL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP TISSUE SPECIFICITY, AND POSSIBLE INVOLVEMENT IN NASOPHARYNGEAL CARCINOMA.
RX PubMed=16423998; DOI=10.1158/0008-5472.can-05-2166;
RA Jiang R.-C., Qin H.-D., Zeng M.-S., Huang W., Feng B.-J., Zhang F.,
RA Chen H.-K., Jia W.-H., Chen L.-Z., Feng Q.-S., Zhang R.-H., Yu X.-J.,
RA Zheng M.-Z., Zeng Y.-X.;
RT "A functional variant in the transcriptional regulatory region of gene
RT LOC344967 cosegregates with disease phenotype in familial nasopharyngeal
RT carcinoma.";
RL Cancer Res. 66:693-700(2006).
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}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2;
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined. Up-regulated in
CC nasopharyngeal carcinoma (at protein level).
CC {ECO:0000269|PubMed:16423998}.
CC -!- DISEASE: Note=A functional variant in the transcriptional regulatory
CC region of in ACOT7L cosegregates with disease phenotype in family
CC affected by nasopharyngeal carcinoma. The variant creates an AP1-
CC binding site that significantly enhances binding of AP1 to the
CC promoter, resulting in up-regulation.
CC -!- CAUTION: Could be the product of a pseudogene. The peptide used to
CC produce antibodies against ACOT7L matches at 85% with ACOT7 and the
CC antibodies may not be specific to ACOT7L. {ECO:0000305}.
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DR EMBL; AK125299; BAC86118.1; -; mRNA.
DR AlphaFoldDB; Q6ZUV0; -.
DR SMR; Q6ZUV0; -.
DR BioMuta; ACOT7L; -.
DR EPD; Q6ZUV0; -.
DR jPOST; Q6ZUV0; -.
DR MassIVE; Q6ZUV0; -.
DR MaxQB; Q6ZUV0; -.
DR PeptideAtlas; Q6ZUV0; -.
DR PRIDE; Q6ZUV0; -.
DR ProteomicsDB; 68371; -.
DR MIM; 611963; gene.
DR neXtProt; NX_Q6ZUV0; -.
DR InParanoid; Q6ZUV0; -.
DR PhylomeDB; Q6ZUV0; -.
DR BioCyc; MetaCyc:G66-33733-MON; -.
DR PathwayCommons; Q6ZUV0; -.
DR Reactome; R-HSA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR Pharos; Q6ZUV0; Tdark.
DR PRO; PR:Q6ZUV0; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q6ZUV0; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IBA:GO_Central.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0036042; F:long-chain fatty acyl-CoA binding; IBA:GO_Central.
DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IBA:GO_Central.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:1900535; P:palmitic acid biosynthetic process; IBA:GO_Central.
DR InterPro; IPR040170; Cytosol_ACT.
DR InterPro; IPR033120; HOTDOG_ACOT.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR006683; Thioestr_dom.
DR PANTHER; PTHR11049; PTHR11049; 1.
DR Pfam; PF03061; 4HBT; 1.
DR SUPFAM; SSF54637; SSF54637; 2.
DR PROSITE; PS51770; HOTDOG_ACOT; 2.
PE 5: Uncertain;
KW Cytoplasm; Hydrolase; Lipid metabolism; Reference proteome; Repeat;
KW Serine esterase.
FT CHAIN 1..252
FT /note="Putative cytosolic acyl coenzyme A thioester
FT hydrolase-like"
FT /id="PRO_0000347058"
FT DOMAIN 1..90
FT /note="HotDog ACOT-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT DOMAIN 146..252
FT /note="HotDog ACOT-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
SQ SEQUENCE 252 AA; 28164 MW; E9C4DF4A82B87717 CRC64;
MIKEAGAIIS TRHCNPQNGD RCVAALARVE CTHFLWPMCI GEVAHVSAEI TYTSKHSVEV
QVNMMSENIL TGAKKLTNKA TLWYAPLSLT NVDKVLEEPP VVYFRQEQEE EGQKRYKTQK
LERMETNWRN GDIVQPVLNP EPNTVSYSQS SLIHLVGPSD CTLHSFVHEG VTMKVMDEVA
GILAARHCKT NLVTASMEAI NFDNKIRKGC IKTISGRMTF TSNKSVEIEV LVDADCVVDS
SQKRYRAASV FT
