LOCUS       NM_007260               1635 bp    mRNA    linear   PRI 11-FEB-2025
DEFINITION  Homo sapiens lysophospholipase 2 (LYPLA2), mRNA.
ACCESSION   NM_007260
VERSION     NM_007260.3
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 1635)
  AUTHORS   Abrami,L., Audagnotto,M., Ho,S., Marcaida,M.J., Mesquita,F.S.,
            Anwar,M.U., Sandoz,P.A., Fonti,G., Pojer,F., Dal Peraro,M. and van
            der Goot,F.G.
  TITLE     Palmitoylated acyl protein thioesterase APT2 deforms membranes to
            extract substrate acyl chains
  JOURNAL   Nat Chem Biol 17 (4), 438-447 (2021)
   PUBMED   33707782
  REMARK    GeneRIF: Palmitoylated acyl protein thioesterase APT2 deforms
            membranes to extract substrate acyl chains.
REFERENCE   2  (bases 1 to 1635)
  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 1635)
  AUTHORS   Wepy,J.A., Galligan,J.J., Kingsley,P.J., Xu,S., Goodman,M.C.,
            Tallman,K.A., Rouzer,C.A. and Marnett,L.J.
  TITLE     Lysophospholipases cooperate to mediate lipid homeostasis and
            lysophospholipid signaling
  JOURNAL   J Lipid Res 60 (2), 360-374 (2019)
   PUBMED   30482805
  REMARK    GeneRIF: LYPLA1 and LYPLA2 are each able to account for the loss of
            the other to maintain lipid homeostasis in cells
            Erratum:[J Lipid Res. 2019 Jul;60(7):1345. doi:
            10.1194/jlr.ERR119000139.. PMID: 31262966]
REFERENCE   4  (bases 1 to 1635)
  AUTHORS   Kathayat,R.S., Cao,Y., Elvira,P.D., Sandoz,P.A., Zaballa,M.E.,
            Springer,M.Z., Drake,L.E., Macleod,K.F., van der Goot,F.G. and
            Dickinson,B.C.
  TITLE     Active and dynamic mitochondrial S-depalmitoylation revealed by
            targeted fluorescent probes
  JOURNAL   Nat Commun 9 (1), 334 (2018)
   PUBMED   29362370
  REMARK    Publication Status: Online-Only
REFERENCE   5  (bases 1 to 1635)
  AUTHORS   Abrami,L., Dallavilla,T., Sandoz,P.A., Demir,M., Kunz,B.,
            Savoglidis,G., Hatzimanikatis,V. and van der Goot,F.G.
  TITLE     Identification and dynamics of the human ZDHHC16-ZDHHC6
            palmitoylation cascade
  JOURNAL   Elife 6, e27826 (2017)
   PUBMED   28826475
  REMARK    Publication Status: Online-Only
REFERENCE   6  (bases 1 to 1635)
  AUTHORS   Kong,E., Peng,S., Chandra,G., Sarkar,C., Zhang,Z., Bagh,M.B. and
            Mukherjee,A.B.
  TITLE     Dynamic palmitoylation links cytosol-membrane shuttling of
            acyl-protein thioesterase-1 and acyl-protein thioesterase-2 with
            that of proto-oncogene H-ras product and growth-associated
            protein-43
  JOURNAL   J Biol Chem 288 (13), 9112-9125 (2013)
   PUBMED   23396970
  REMARK    GeneRIF: Dynamic palmitoylation links cytosol-membrane shuttling of
            acyl-protein thioesterase-1 and acyl-protein thioesterase-2 with
            that of proto-oncogene H-ras product and growth-associated
            protein-43
REFERENCE   7  (bases 1 to 1635)
  AUTHORS   Tomatis,V.M., Trenchi,A., Gomez,G.A. and Daniotti,J.L.
  TITLE     Acyl-protein thioesterase 2 catalyzes the deacylation of peripheral
            membrane-associated GAP-43
  JOURNAL   PLoS One 5 (11), e15045 (2010)
   PUBMED   21152083
  REMARK    GeneRIF: Results demonstrate that APT-2 is the protein thioesterase
            involved in the acylation/deacylation cycle operating in GAP-43
            subcellular distribution.
            Publication Status: Online-Only
REFERENCE   8  (bases 1 to 1635)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (bases 1 to 1635)
  AUTHORS   Ma,J., Dempsey,A.A., Stamatiou,D., Marshall,K.W. and Liew,C.C.
  TITLE     Identifying leukocyte gene expression patterns associated with
            plasma lipid levels in human subjects
  JOURNAL   Atherosclerosis 191 (1), 63-72 (2007)
   PUBMED   16806233
REFERENCE   10 (bases 1 to 1635)
  AUTHORS   Wang,A. and Dennis,E.A.
  TITLE     Mammalian lysophospholipases
  JOURNAL   Biochim Biophys Acta 1439 (1), 1-16 (1999)
   PUBMED   10395961
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL031295.1.
            
            On Nov 26, 2018 this sequence version replaced NM_007260.2.
            
            Summary: Lysophospholipases are enzymes that act on biological
            membranes to regulate the multifunctional lysophospholipids. There
            are alternatively spliced transcript variants described for this
            gene but the full length nature is not known yet. [provided by
            RefSeq, Jul 2008].
            
            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 :: SRR3476690.871189.1,
                                           SRR3476690.314866.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374514.8/ ENSP00000363638.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
            COMPLETENESS: full length.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-106               AL031295.1         90283-90388
            107-210             AL031295.1         91795-91898
            211-242             AL031295.1         92146-92177
            243-308             AL031295.1         92289-92354
            309-356             AL031295.1         92843-92890
            357-427             AL031295.1         92998-93068
            428-501             AL031295.1         93201-93274
            502-603             AL031295.1         93362-93463
            604-777             AL031295.1         93565-93738
            778-1635            AL031295.1         93820-94677
FEATURES             Location/Qualifiers
     source          1..1635
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     gene            1..1635
                     /gene="LYPLA2"
                     /gene_synonym="APT-2; APT2; DJ886K2.4"
                     /note="lysophospholipase 2"
                     /db_xref="GeneID:11313"
                     /db_xref="HGNC:HGNC:6738"
                     /db_xref="MIM:616143"
     exon            1..106
                     /gene="LYPLA2"
                     /gene_synonym="APT-2; APT2; DJ886K2.4"
                     /inference="alignment:Splign:2.1.0"
     exon            107..210
                     /gene="LYPLA2"
                     /gene_synonym="APT-2; APT2; DJ886K2.4"
                     /inference="alignment:Splign:2.1.0"
     CDS             133..828
                     /gene="LYPLA2"
                     /gene_synonym="APT-2; APT2; DJ886K2.4"
                     /EC_number="3.1.2.22"
                     /note="LPL-II; lysoPLA II; testicular tissue protein Li 3;
                     lysophospholipase II; palmitoyl-protein hydrolase"
                     /codon_start=1
                     /product="acyl-protein thioesterase 2"
                     /protein_id="NP_009191.1"
                     /db_xref="CCDS:CCDS241.1"
                     /db_xref="GeneID:11313"
                     /db_xref="HGNC:HGNC:6738"
                     /db_xref="MIM:616143"
                     /translation="MCGNTMSVPLLTDAATVSGAERETAAVIFLHGLGDTGHSWADAL
                     STIRLPHVKYICPHAPRIPVTLNMKMVMPSWFDLMGLSPDAPEDEAGIKKAAENIKAL
                     IEHEMKNGIPANRIVLGGFSQGGALSLYTALTCPHPLAGIVALSCWLPLHRAFPQAAN
                     GSAKDLAILQCHGELDPMVPVRFGALTAEKLRSVVTPARVQFKTYPGVMHSSCPQEMA
                     AVKEFLEKLLPPV"
     exon            211..242
                     /gene="LYPLA2"
                     /gene_synonym="APT-2; APT2; DJ886K2.4"
                     /inference="alignment:Splign:2.1.0"
     exon            243..308
                     /gene="LYPLA2"
                     /gene_synonym="APT-2; APT2; DJ886K2.4"
                     /inference="alignment:Splign:2.1.0"
     exon            309..356
                     /gene="LYPLA2"
                     /gene_synonym="APT-2; APT2; DJ886K2.4"
                     /inference="alignment:Splign:2.1.0"
     exon            357..427
                     /gene="LYPLA2"
                     /gene_synonym="APT-2; APT2; DJ886K2.4"
                     /inference="alignment:Splign:2.1.0"
     exon            428..501
                     /gene="LYPLA2"
                     /gene_synonym="APT-2; APT2; DJ886K2.4"
                     /inference="alignment:Splign:2.1.0"
     exon            502..603
                     /gene="LYPLA2"
                     /gene_synonym="APT-2; APT2; DJ886K2.4"
                     /inference="alignment:Splign:2.1.0"
     exon            604..777
                     /gene="LYPLA2"
                     /gene_synonym="APT-2; APT2; DJ886K2.4"
                     /inference="alignment:Splign:2.1.0"
     exon            778..1635
                     /gene="LYPLA2"
                     /gene_synonym="APT-2; APT2; DJ886K2.4"
                     /inference="alignment:Splign:2.1.0"
     regulatory      1618..1623
                     /regulatory_class="polyA_signal_sequence"
                     /gene="LYPLA2"
                     /gene_synonym="APT-2; APT2; DJ886K2.4"
                     /note="hexamer: AAGAAA"
     polyA_site      1635
                     /gene="LYPLA2"
                     /gene_synonym="APT-2; APT2; DJ886K2.4"
                     /note="major polyA site"
ORIGIN      
        1 gggactcgaa cggaagttcc ggcgggggcg gccgaggggg aagagtgtgt ctgcgggaga
       61 aagaggagaa tcgcccaagc ggcctcggaa gtcccaggga gtggaggccc ccgccgtgga
      121 gccgtgtggt gtatgtgtgg taacaccatg tctgtgcccc tgctcaccga tgctgccacc
      181 gtgtctggag ctgagcggga aacggccgcg gttatttttt tacatggact tggagacaca
      241 gggcacagct gggctgacgc cctctccacc atccggctcc ctcacgtcaa gtacatctgt
      301 ccccatgcgc ctaggatccc tgtgaccctc aacatgaaga tggtgatgcc ctcctggttt
      361 gacctgatgg ggctgagtcc agatgcccca gaggacgagg ctggcatcaa gaaggcagca
      421 gagaacatca aggccttgat tgagcatgaa atgaagaacg ggatccctgc caatcgaatc
      481 gtcctgggag gcttttcaca gggcggggcc ctgtccctct acacggccct cacctgcccc
      541 caccctctgg ctggcatcgt ggcgttgagc tgctggctgc ctctgcaccg ggccttcccc
      601 caggcagcta atggcagtgc caaggacctg gccatactcc agtgccatgg ggagctggac
      661 cccatggtgc ccgtacggtt tggggccctg acggctgaga agctccggtc tgttgtcaca
      721 cctgccaggg tccagttcaa gacatacccg ggtgtcatgc acagctcctg tcctcaggag
      781 atggcagctg tgaaggaatt tcttgagaag ctgctgcctc ctgtctaact agtcgctggc
      841 cccagtgcag taccccagct catgggggac tcagcaagca agcgtggcac catcttggat
      901 ctgagccggt cgagcccctg tccccaccct tcctgacctg tccttttccc acaggcctct
      961 gggggcaggt ggcaaggcct ggccgggcct tccttcctgg ccttagccac ctggctctgt
     1021 ctgcagcagg ggcaggctgc tttcttatcc atttccctgg aggcgggccc ccctggcagc
     1081 agtattggag gggctacagg cagctggaga aaggggccca gccgctgacc cactcactca
     1141 ggacctcact cactagcccc gctttgggcc ccctcctgtg acctcagggt ttggcccatg
     1201 gggccccccc aggcccctgc cccaactgat tctgcccaga taatcgtgtc tcctgcctcc
     1261 actcagctgc ttctcagtca tgaatgtggc catggccccg gggtcccctt gctgctgtgg
     1321 gctccctgtc cctgggcagg agtgctggtg aggaggtgga gccttttgag gggggccttc
     1381 cctcagctgt ttccccacac tggggggctg ggccctgcct ccccgttacc ctccttccct
     1441 gcaggcctgg agcctgtagg gctggactga ggttcaggtc tccccccagc tgtctcaccc
     1501 ccactttgtc cccactctag agcagggagg cagtggggga ggagttgtgt ctcgtcttct
     1561 gtctccatgt ggtttttggg tgtttttctt gttgtgtcct ggattccgat aaaattaaag
     1621 aaattgcttc ctcaa
//
