LOCUS       NM_005469               1154 bp    mRNA    linear   PRI 04-APR-2024
DEFINITION  Homo sapiens acyl-CoA thioesterase 8 (ACOT8), mRNA.
ACCESSION   NM_005469
VERSION     NM_005469.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (bases 1 to 1154)
  AUTHORS   Lim,S.H., Snider,J., Birimberg-Schwartz,L., Ip,W., Serralha,J.C.,
            Botelho,H.M., Lopes-Pacheco,M., Pinto,M.C., Moutaoufik,M.T.,
            Zilocchi,M., Laselva,O., Esmaeili,M., Kotlyar,M., Lyakisheva,A.,
            Tang,P., Lopez Vazquez,L., Akula,I., Aboualizadeh,F., Wong,V.,
            Grozavu,I., Opacak-Bernardi,T., Yao,Z., Mendoza,M., Babu,M.,
            Jurisica,I., Gonska,T., Bear,C.E., Amaral,M.D. and Stagljar,I.
  TITLE     CFTR interactome mapping using the mammalian membrane two-hybrid
            high-throughput screening system
  JOURNAL   Mol Syst Biol 18 (2), e10629 (2022)
   PUBMED   35156780
REFERENCE   2  (bases 1 to 1154)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (bases 1 to 1154)
  AUTHORS   Hung,Y.H., Chan,Y.S., Chang,Y.S., Lee,K.T., Hsu,H.P., Yen,M.C.,
            Chen,W.C., Wang,C.Y. and Lai,M.D.
  TITLE     Fatty acid metabolic enzyme acyl-CoA thioesterase 8 promotes the
            development of hepatocellular carcinoma
  JOURNAL   Oncol Rep 31 (6), 2797-2803 (2014)
   PUBMED   24788990
  REMARK    GeneRIF: In summary, lipolytic enzyme ACOT8 is frequently
            upregulated in HCC clinical specimens. More importantly, ACOT8
            silencing leads to inhibition of cell growth in HCC in vitro.
REFERENCE   4  (bases 1 to 1154)
  AUTHORS   Jung,W.Y., Kim,Y.H., Ryu,Y.J., Kim,B.H., Shin,B.K., Kim,A. and
            Kim,H.K.
  TITLE     Acyl-CoA thioesterase 8 is a specific protein related to nodal
            metastasis and prognosis of lung adenocarcinoma
  JOURNAL   Pathol Res Pract 209 (5), 276-283 (2013)
   PUBMED   23540296
  REMARK    GeneRIF: Acyl-CoA thioesterase 8 is a specific protein related to
            nodal metastasis and prognosis of lung adenocarcinoma.
REFERENCE   5  (bases 1 to 1154)
  AUTHORS   Jager,S., Cimermancic,P., Gulbahce,N., Johnson,J.R., McGovern,K.E.,
            Clarke,S.C., Shales,M., Mercenne,G., Pache,L., Li,K., Hernandez,H.,
            Jang,G.M., Roth,S.L., Akiva,E., Marlett,J., Stephens,M., D'Orso,I.,
            Fernandes,J., Fahey,M., Mahon,C., O'Donoghue,A.J., Todorovic,A.,
            Morris,J.H., Maltby,D.A., Alber,T., Cagney,G., Bushman,F.D.,
            Young,J.A., Chanda,S.K., Sundquist,W.I., Kortemme,T.,
            Hernandez,R.D., Craik,C.S., Burlingame,A., Sali,A., Frankel,A.D.
            and Krogan,N.J.
  TITLE     Global landscape of HIV-human protein complexes
  JOURNAL   Nature 481 (7381), 365-370 (2011)
   PUBMED   22190034
  REMARK    Publication Status: Online-Only
REFERENCE   6  (bases 1 to 1154)
  AUTHORS   Jones,J.M. and Gould,S.J.
  TITLE     Identification of PTE2, a human peroxisomal long-chain acyl-CoA
            thioesterase
  JOURNAL   Biochem Biophys Res Commun 275 (1), 233-240 (2000)
   PUBMED   10944470
REFERENCE   7  (bases 1 to 1154)
  AUTHORS   Cohen,G.B., Rangan,V.S., Chen,B.K., Smith,S. and Baltimore,D.
  TITLE     The human thioesterase II protein binds to a site on HIV-1 Nef
            critical for CD4 down-regulation
  JOURNAL   J Biol Chem 275 (30), 23097-23105 (2000)
   PUBMED   10807905
REFERENCE   8  (bases 1 to 1154)
  AUTHORS   Jones,J.M., Nau,K., Geraghty,M.T., Erdmann,R. and Gould,S.J.
  TITLE     Identification of peroxisomal acyl-CoA thioesterases in yeast and
            humans
  JOURNAL   J Biol Chem 274 (14), 9216-9223 (1999)
   PUBMED   10092594
REFERENCE   9  (bases 1 to 1154)
  AUTHORS   Watanabe,H., Shiratori,T., Shoji,H., Miyatake,S., Okazaki,Y.,
            Ikuta,K., Sato,T. and Saito,T.
  TITLE     A novel acyl-CoA thioesterase enhances its enzymatic activity by
            direct binding with HIV Nef
  JOURNAL   Biochem Biophys Res Commun 238 (1), 234-239 (1997)
   PUBMED   9299485
REFERENCE   10 (bases 1 to 1154)
  AUTHORS   Liu,L.X., Margottin,F., Le Gall,S., Schwartz,O., Selig,L.,
            Benarous,R. and Benichou,S.
  TITLE     Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with
            Nef-mediated CD4 down-regulation
  JOURNAL   J Biol Chem 272 (21), 13779-13785 (1997)
   PUBMED   9153233
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB470803.3, X86032.1,
            BC117157.1 and BM986979.1.
            
            On Nov 22, 2018 this sequence version replaced NM_005469.3.
            
            Summary: The protein encoded by this gene is a peroxisomal
            thioesterase that appears to be involved more in the oxidation of
            fatty acids rather than in their formation. The encoded protein can
            bind to the human immunodeficiency virus-1 protein Nef, and mediate
            Nef-induced down-regulation of CD4 in T-cells. [provided by RefSeq,
            Oct 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.330817.1,
                                           SRR5189667.88385.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2152474, SAMEA2152798
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000217455.9/ ENSP00000217455.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
            COMPLETENESS: full length.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-9                 DB470803.3         18-26
            10-947              X86032.1           1-938
            948-1126            BC117157.1         893-1071
            1127-1154           BM986979.1         18-45               c
FEATURES             Location/Qualifiers
     source          1..1154
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.12"
     gene            1..1154
                     /gene="ACOT8"
                     /gene_synonym="hACTE-III; HNAACTE; hTE; NAP1; PTE-1;
                     PTE-2; PTE1; PTE2"
                     /note="acyl-CoA thioesterase 8"
                     /db_xref="GeneID:10005"
                     /db_xref="HGNC:HGNC:15919"
                     /db_xref="MIM:608123"
     exon            1..205
                     /gene="ACOT8"
                     /gene_synonym="hACTE-III; HNAACTE; hTE; NAP1; PTE-1;
                     PTE-2; PTE1; PTE2"
                     /inference="alignment:Splign:2.1.0"
     CDS             78..1037
                     /gene="ACOT8"
                     /gene_synonym="hACTE-III; HNAACTE; hTE; NAP1; PTE-1;
                     PTE-2; PTE1; PTE2"
                     /EC_number="3.1.2.2"
                     /EC_number="3.1.2.1"
                     /EC_number="3.1.2.27"
                     /EC_number="3.1.2.3"
                     /EC_number="3.1.2.11"
                     /EC_number="3.1.2.5"
                     /note="choloyl-CoA hydrolase; peroxisomal acyl-CoA
                     thioesterase 1; thioesterase III; palmitoyl-CoA hydrolase;
                     long-chain fatty-acyl-CoA hydrolase; peroxisomal
                     acyl-coenzyme A thioester hydrolase 1; peroxisomal
                     long-chain acyl-CoA thioesterase 1; HIV-Nef associated
                     acyl-CoA thioesterase; choloyl-coenzyme A thioesterase;
                     Nef (lentivirus myristoylated factor) associated protein
                     1; peroxisomal acyl-CoA thioesterase 2"
                     /codon_start=1
                     /product="acyl-coenzyme A thioesterase 8"
                     /protein_id="NP_005460.2"
                     /db_xref="CCDS:CCDS13378.1"
                     /db_xref="GeneID:10005"
                     /db_xref="HGNC:HGNC:15919"
                     /db_xref="MIM:608123"
                     /translation="MSSPQAPEDGQGCGDRGDPPGDLRSVLVTTVLNLEPLDEDLFRG
                     RHYWVPAKRLFGGQIVGQALVAAAKSVSEDVHVHSLHCYFVRAGDPKLPVLYQVERTR
                     TGSSFSVRSVKAVQHGKPIFICQASFQQAQPSPMQHQFSMPTVPPPEELLDCETLIDQ
                     YLRDPNLQKRYPLALNRIAAQEVPIEIKPVNPSPLSQLQRMEPKQMFWVRARGYIGEG
                     DMKMHCCVAAYISDYAFLGTALLPHQWQHKVHFMVSLDHSMWFHAPFRADHWMLYECE
                     SPWAGGSRGLVHGRLWRQDGVLAVTCAQEGVIRVKPQVSESKL"
     exon            206..339
                     /gene="ACOT8"
                     /gene_synonym="hACTE-III; HNAACTE; hTE; NAP1; PTE-1;
                     PTE-2; PTE1; PTE2"
                     /inference="alignment:Splign:2.1.0"
     exon            340..565
                     /gene="ACOT8"
                     /gene_synonym="hACTE-III; HNAACTE; hTE; NAP1; PTE-1;
                     PTE-2; PTE1; PTE2"
                     /inference="alignment:Splign:2.1.0"
     exon            566..723
                     /gene="ACOT8"
                     /gene_synonym="hACTE-III; HNAACTE; hTE; NAP1; PTE-1;
                     PTE-2; PTE1; PTE2"
                     /inference="alignment:Splign:2.1.0"
     exon            724..918
                     /gene="ACOT8"
                     /gene_synonym="hACTE-III; HNAACTE; hTE; NAP1; PTE-1;
                     PTE-2; PTE1; PTE2"
                     /inference="alignment:Splign:2.1.0"
     exon            919..1154
                     /gene="ACOT8"
                     /gene_synonym="hACTE-III; HNAACTE; hTE; NAP1; PTE-1;
                     PTE-2; PTE1; PTE2"
                     /inference="alignment:Splign:2.1.0"
     regulatory      1131..1136
                     /regulatory_class="polyA_signal_sequence"
                     /gene="ACOT8"
                     /gene_synonym="hACTE-III; HNAACTE; hTE; NAP1; PTE-1;
                     PTE-2; PTE1; PTE2"
                     /note="hexamer: AATAAA"
     polyA_site      1154
                     /gene="ACOT8"
                     /gene_synonym="hACTE-III; HNAACTE; hTE; NAP1; PTE-1;
                     PTE-2; PTE1; PTE2"
                     /note="major polyA site"
ORIGIN      
        1 gccggaagag tcaggttctg tgtatgtctc cgcgtcttcc gcggagcggg tgtgcagggc
       61 ctgcagcatt gaactagatg tcgtccccgc aggccccaga agatgggcag ggctgtggcg
      121 accgcggcga tccccctggg gacctccgta gcgtcttggt cacgaccgtg ctcaacctcg
      181 agccgctgga cgaggatctc ttcagaggaa ggcattactg ggtaccggcc aagaggctgt
      241 ttggtggtca gatcgtgggc caggccctgg tggctgcagc caagtctgtg agtgaagacg
      301 tccacgtgca ctccctgcac tgctactttg ttcgggcagg ggacccgaag ctgccagtac
      361 tgtaccaagt ggagcggaca cgaacagggt cgagcttctc ggtgcgctct gtgaaggccg
      421 tgcaacatgg gaagcccatc ttcatctgcc aggcctcctt ccagcaggcc cagcccagcc
      481 ccatgcagca ccagttctcc atgcccactg tgccaccacc agaagagctg cttgactgtg
      541 agaccctcat tgaccagtat ttaagggacc ctaacctcca aaagaggtac ccattggcgc
      601 tcaaccgaat tgctgctcag gaggtcccca ttgagatcaa gccagtaaac ccatcccccc
      661 tgagccagct gcagagaatg gagcccaaac agatgttctg ggtgcgagcc cggggctata
      721 ttggcgaggg cgacatgaag atgcactgct gcgtggccgc ctatatctcc gactatgcct
      781 tcttgggcac tgcactgctg cctcaccagt ggcagcacaa ggtgcacttc atggtctcac
      841 tggaccattc catgtggttc cacgccccct tccgagctga ccactggatg ctctatgaat
      901 gcgagagccc ctgggccggt ggctctcggg ggctggtcca tgggcggctg tggcgtcagg
      961 atggagtcct agctgtgacc tgtgcccagg agggcgtgat ccgagtgaag ccccaggtct
     1021 cagagagcaa gctgtagcca gaggtaccag cttcgcctgg ggcttcaaga acctcccatc
     1081 tatccccatt cctgagacag gagttacagt cccttttggc cctcacatcc aataaagaga
     1141 ctgataccac tgga
//
