LOCUS       NP_038958                926 aa            linear   ROD 24-SEP-2024
DEFINITION  alpha-aminoadipic semialdehyde synthase, mitochondrial [Mus
            musculus].
ACCESSION   NP_038958
VERSION     NP_038958.2
DBSOURCE    REFSEQ: accession NM_013930.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 926)
  AUTHORS   Yang,J., Liang,J., Huang,C., Wu,Z. and Lei,Y.
  TITLE     Hyperactivation of succinate dehydrogenase promotes pyroptosis of
            macrophage via ROS-induced GSDMD oligomerization in acute liver
            failure
  JOURNAL   Mol Immunol 169, 86-98 (2024)
   PUBMED   38552285
  REMARK    GeneRIF: Hyperactivation of succinate dehydrogenase promotes
            pyroptosis of macrophage via ROS-induced GSDMD oligomerization in
            acute liver failure.
REFERENCE   2  (residues 1 to 926)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 926)
  AUTHORS   Barzi,M., Johnson,C.G., Chen,T., Rodriguiz,R.M., Hemmingsen,M.,
            Gonzalez,T.J., Rosales,A., Beasley,J., Peck,C.K., Ma,Y.,
            Stiles,A.R., Wood,T.C., Maeso-Diaz,R., Diehl,A.M., Young,S.P.,
            Everitt,J.I., Wetsel,W.C., Lagor,W.R., Bissig-Choisat,B.,
            Asokan,A., El-Gharbawy,A. and Bissig,K.D.
  TITLE     Rescue of glutaric aciduria type I in mice by liver-directed
            therapies
  JOURNAL   Sci Transl Med 15 (692), eadf4086 (2023)
   PUBMED   37075130
REFERENCE   4  (residues 1 to 926)
  AUTHORS   Guo,Y., Wu,J., Wang,M., Wang,X., Jian,Y., Yang,C. and Guo,W.
  TITLE     The Metabolite Saccharopine Impairs Neuronal Development by
            Inhibiting the Neurotrophic Function of Glucose-6-Phosphate
            Isomerase
  JOURNAL   J Neurosci 42 (13), 2631-2646 (2022)
   PUBMED   35135854
REFERENCE   5  (residues 1 to 926)
  AUTHORS   Leandro,J., Dodatko,T., DeVita,R.J., Chen,H., Stauffer,B., Yu,C.
            and Houten,S.M.
  TITLE     Deletion of 2-aminoadipic semialdehyde synthase limits metabolite
            accumulation in cell and mouse models for glutaric aciduria type 1
  JOURNAL   J Inherit Metab Dis 43 (6), 1154-1164 (2020)
   PUBMED   32567100
REFERENCE   6  (residues 1 to 926)
  AUTHORS   Cleveland,B.M., Kiess,A.S. and Blemings,K.P.
  TITLE     Alpha-aminoadipate delta-semialdehyde synthase mRNA knockdown
            reduces the lysine requirement of a mouse hepatic cell line
  JOURNAL   J Nutr 138 (11), 2143-2147 (2008)
   PUBMED   18936211
  REMARK    GeneRIF: These results indicate AASS knockdown decreases the lysine
            requirement of the cell via a reduction of lysine catabolism
            through the saccharopine pathway.
REFERENCE   7  (residues 1 to 926)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   8  (residues 1 to 926)
  AUTHORS   Papes,F., Surpili,M.J., Langone,F., Trigo,J.R. and Arruda,P.
  TITLE     The essential amino acid lysine acts as precursor of glutamate in
            the mammalian central nervous system
  JOURNAL   FEBS Lett 488 (1-2), 34-38 (2001)
   PUBMED   11163791
REFERENCE   9  (residues 1 to 926)
  AUTHORS   Papes,F., Kemper,E.L., Cord-Neto,G., Langone,F. and Arruda,P.
  TITLE     Lysine degradation through the saccharopine pathway in mammals:
            involvement of both bifunctional and monofunctional
            lysine-degrading enzymes in mouse
  JOURNAL   Biochem J 344 Pt 2 (Pt 2), 555-563 (1999)
   PUBMED   10567240
REFERENCE   10 (residues 1 to 926)
  AUTHORS   Gleiberman,L.
  TITLE     Nativity and race
  JOURNAL   Hypertension 34 (5), e7 (1999)
   PUBMED   10567204
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CJ074697.1, AK149400.1 and
            AC133599.3.
            
            On Jun 19, 2003 this sequence version replaced NP_038958.1.
            
            Summary: This gene encodes a bifunctional mitochondrial protein
            that catalyzes the first two steps in the lysine degradation
            pathway. The N-terminus contains lysine-ketoglutarate reductase
            activity and converts lysine to saccharopine, whereas the
            C-terminus contains saccharopine dehydrogenase activity and
            converts saccharopine to alpha-aminoadipate semialdehyde. Mutations
            in a human gene encoding a highly similar protein are associated
            with familial hyperlysinemia. [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 :: AK149400.1, AK044323.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164135 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..926
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 10.27 cM"
     Protein         1..926
                     /product="alpha-aminoadipic semialdehyde synthase,
                     mitochondrial"
                     /EC_number="1.5.1.8"
                     /EC_number="1.5.1.9"
                     /note="saccharopine dehydrogenase; lysine oxoglutarate
                     reductase"
                     /calculated_mol_wt=102844
     Region          25..916
                     /region_name="PLN02819"
                     /note="lysine-ketoglutarate reductase/saccharopine
                     dehydrogenase"
                     /db_xref="CDD:215439"
     Region          25..466
                     /region_name="LKR_SDH_like"
                     /note="bifunctional lysine ketoglutarate reductase
                     /saccharopine dehydrogenase enzyme; cd12189"
                     /db_xref="CDD:240665"
     Region          28..455
                     /region_name="Lysine-ketoglutarate reductase.
                     /evidence=ECO:0000303|PubMed:10567240"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99K67.1)"
     Site            48
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99K67.1)"
     Site            52
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99K67.1)"
     Site            56
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99K67.1)"
     Site            93
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99K67.1)"
     Site            128
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99K67.1)"
     Site            138
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99K67.1)"
     Site            order(223,225..226,246..248,309..311)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240665"
     Site            286
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99K67.1)"
     Site            458
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99K67.1)"
     Region          477..926
                     /region_name="Saccharopine dehydrogenase.
                     /evidence=ECO:0000303|PubMed:10567240"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99K67.1)"
     Site            523
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99K67.1)"
     Site            535
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99K67.1)"
     Site            584
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99K67.1)"
     Site            707
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99K67.1)"
     Site            739
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99K67.1)"
     Site            761
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99K67.1)"
     Site            778
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99K67.1)"
     Site            780
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q99K67.1)"
     CDS             1..926
                     /gene="Aass"
                     /gene_synonym="LKR; LKR/SDH; LOR; LOR/SDH; Lorsdh; SDH"
                     /coded_by="NM_013930.4:122..2902"
                     /db_xref="CCDS:CCDS19937.1"
                     /db_xref="GeneID:30956"
                     /db_xref="MGI:MGI:1353573"
ORIGIN      
        1 mlraqrprla rlraclsrgl hhkpvmalrr edvnawerra plapkhikgi tklgykvliq
       61 psnrraihdk eyvraggilq editeaclil gvkrppeekl mskktyaffs htikaqeanm
      121 nlldevlkqe irlidyekmv dhrgsrivaf gqwagvagmi nilhgmglrl lalghhtpfm
      181 hlgmahnyrn ssqavqavrd agyeislglm pksigpltfv ftgtgnvskg aqevfnelpc
      241 eyvephelre vsktgdlrkv ygtvlsrhhh lvrktdgvyd pveyekyper ytsrfntdia
      301 pyttclingi yweqntprll trqdaqsllv pvkssvvpve gcpelphklv aicdisadtg
      361 gsidfmtect tierpfcmyd adqqiihdsv egsgilmcsi dnlpaqlpie ateyfgdmly
      421 pyveemllsd asqplesqnf spvvrdavit snglltdkyk yiqklresre riqflsmstk
      481 kkvlvlgsgy vsgpvleyls rdnnieitlg sdmtnqmqql skkyninpvs ltvgkqeakl
      541 qslvesqdlv isllpyvlhp vvakaciesr vnmvtasyit pamkeleksv ddagitvige
      601 lgldpgldhm lametidtak elgatvesyv sycgglpape hsdnplrykf swspvgvlmn
      661 imqpasylln gkvvnvtggv sflnsvtpmd yfpglnlegy pnrdsikyae iygissahtl
      721 lrgtlrykgy skalngfvkl glinreaypa lrpeanpltw kqllcdlvgi srsspceklk
      781 evvftklggd ntqleaaewl gllgdeqvpq aesivdafsk hlvsklsygp eekdmivmrd
      841 sfgirhpsgh lenktidlvv ygdfngfsam aktvglptam aakmlldgei eakglmgpft
      901 keiygpiler ikaegivfnt qstikl
//
