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HEM1_MOUSE
ID   HEM1_MOUSE              Reviewed;         642 AA.
AC   Q8VC19; Q64453;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=5-aminolevulinate synthase, non-specific, mitochondrial;
DE            Short=ALAS-H;
DE            EC=2.3.1.37 {ECO:0000250|UniProtKB:P13196};
DE   AltName: Full=5-aminolevulinic acid synthase 1;
DE   AltName: Full=Delta-ALA synthase 1;
DE   AltName: Full=Delta-aminolevulinate synthase 1;
DE   Flags: Precursor;
GN   Name=Alas1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 188-642.
RC   STRAIN=DBA/2J; TISSUE=Liver;
RA   Young E.G., Dierks P.M.;
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, and Liver;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent
CC       condensation of succinyl-CoA and glycine to form aminolevulinic acid
CC       (ALA), with CoA and CO2 as by-products. {ECO:0000250|UniProtKB:P13196}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO2 + CoA;
CC         Xref=Rhea:RHEA:12921, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:356416; EC=2.3.1.37;
CC         Evidence={ECO:0000250|UniProtKB:P13196};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12922;
CC         Evidence={ECO:0000250|UniProtKB:P13196};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P13196};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from glycine: step 1/1.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts (hydroxylated form) with
CC       VHL (By similarity). {ECO:0000250|UniProtKB:P13196,
CC       ECO:0000250|UniProtKB:P22557}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P22557}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P22557}. Note=Localizes to the matrix side of
CC       the mitochondrion inner membrane. {ECO:0000250|UniProtKB:P22557}.
CC   -!- PTM: In normoxia, is hydroxylated at Pro-578, promoting interaction
CC       with VHL, initiating ubiquitination and subsequent degradation via the
CC       proteasome. {ECO:0000250|UniProtKB:P13196}.
CC   -!- PTM: Ubiquitinated; in normoxia following hydroxylation and interaction
CC       with VHL, leading to its subsequent degradation via the proteasome.
CC       {ECO:0000250|UniProtKB:P13196}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; BC022110; AAH22110.1; -; mRNA.
DR   EMBL; M63245; AAA91867.1; -; mRNA.
DR   CCDS; CCDS40756.2; -.
DR   RefSeq; NP_001278764.1; NM_001291835.1.
DR   RefSeq; NP_065584.2; NM_020559.2.
DR   AlphaFoldDB; Q8VC19; -.
DR   SMR; Q8VC19; -.
DR   BioGRID; 198058; 2.
DR   STRING; 10090.ENSMUSP00000108143; -.
DR   iPTMnet; Q8VC19; -.
DR   PhosphoSitePlus; Q8VC19; -.
DR   SwissPalm; Q8VC19; -.
DR   MaxQB; Q8VC19; -.
DR   PaxDb; Q8VC19; -.
DR   PRIDE; Q8VC19; -.
DR   ProteomicsDB; 269693; -.
DR   Antibodypedia; 4303; 306 antibodies from 34 providers.
DR   DNASU; 11655; -.
DR   Ensembl; ENSMUST00000112524; ENSMUSP00000108143; ENSMUSG00000032786.
DR   Ensembl; ENSMUST00000141118; ENSMUSP00000117014; ENSMUSG00000032786.
DR   GeneID; 11655; -.
DR   KEGG; mmu:11655; -.
DR   UCSC; uc009rjj.2; mouse.
DR   CTD; 211; -.
DR   MGI; MGI:87989; Alas1.
DR   VEuPathDB; HostDB:ENSMUSG00000032786; -.
DR   eggNOG; KOG1360; Eukaryota.
DR   GeneTree; ENSGT00940000156030; -.
DR   HOGENOM; CLU_015846_6_1_1; -.
DR   InParanoid; Q8VC19; -.
DR   OMA; RAYFSGM; -.
DR   OrthoDB; 930001at2759; -.
DR   PhylomeDB; Q8VC19; -.
DR   TreeFam; TF300724; -.
DR   Reactome; R-MMU-189451; Heme biosynthesis.
DR   UniPathway; UPA00251; UER00375.
DR   BioGRID-ORCS; 11655; 6 hits in 76 CRISPR screens.
DR   ChiTaRS; Alas1; mouse.
DR   PRO; PR:Q8VC19; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q8VC19; protein.
DR   Bgee; ENSMUSG00000032786; Expressed in adrenal gland and 270 other tissues.
DR   ExpressionAtlas; Q8VC19; baseline and differential.
DR   Genevisible; Q8VC19; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0003870; F:5-aminolevulinate synthase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0048821; P:erythrocyte development; IBA:GO_Central.
DR   GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
DR   GO; GO:0042541; P:hemoglobin biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:1903412; P:response to bile acid; ISS:UniProtKB.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR010961; 4pyrrol_synth_NH2levulA_synth.
DR   InterPro; IPR015118; 5aminolev_synth_preseq.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   Pfam; PF09029; Preseq_ALAS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01821; 5aminolev_synth; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Heme biosynthesis; Hydroxylation; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Pyridoxal phosphate; Reference proteome;
KW   Transferase; Transit peptide; Ubl conjugation.
FT   TRANSIT         1..56
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:P07997"
FT   CHAIN           57..642
FT                   /note="5-aminolevulinate synthase, non-specific,
FT                   mitochondrial"
FT                   /id="PRO_0000001231"
FT   REGION          50..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        447
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   BINDING         219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   BINDING         336
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   BINDING         355
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   BINDING         388
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   BINDING         416
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   BINDING         444
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   BINDING         476
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   BINDING         477
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   BINDING         564
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   MOD_RES         447
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P18079"
FT   MOD_RES         578
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P13196"
FT   CONFLICT        192
FT                   /note="L -> S (in Ref. 2; AAA91867)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        391
FT                   /note="Missing (in Ref. 1; AAH22110)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        463
FT                   /note="I -> T (in Ref. 2; AAA91867)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        501
FT                   /note="A -> P (in Ref. 2; AAA91867)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        602
FT                   /note="E -> V (in Ref. 2; AAA91867)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        625
FT                   /note="E -> V (in Ref. 2; AAA91867)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   642 AA;  71018 MW;  34E0CBEB8599CFE5 CRC64;
     METVVRRCPF LSRVPQAFLQ KAGKSLLFYA QNCPKMMEVG AKPAPRTLST SAVHCQQVKE
     TPPANEKEKT AKAAVQQAPD ESQMAQTPDG TQLPSGHPSP ATSQGSGSKC PFLAAQLSQT
     GSSVFRKASL ELQEDVQEMH AVRKEAAQSP VPPSLVNVKT DGEDPSRLLK NFQDIMRKQR
     PERVSHLLQD NLPKSVSTFQ YDHFFEKKID EKKNDHTYRV FKTVNRRAQI FPMADDYTDS
     LITKKQVSVW CSNDYLGMSR HPRVCGAVME TVKQHGAGAG GTRNISGTSK FHVELEQALA
     DLHGKDAALL FSSCFVANDS TLFTLAKMMP GCEIYSDSGN HASMIQGIRN SRVPKYIFRH
     NDVNHLRELL QRSDPSVPKI VAFETVHSMD GAVCPLEELC DVAHEFGAIT FVDEVHAVGL
     YGARGGGIGD RDGVMPKMDI ISGTLGKAFG CVGGYIASTS LLIDTVRSYA AGFIFTTSLP
     PMLLAGALES VRILKSSEGR ALRRQHQRNV KLLRQMLMDA GLPVIHCPSH IIPVRVADAA
     KNTEICDELM TRHNIYVQAI NYPTVPRGEE LLRIAPTPHH TPQMMNFFVE KLLVTWKRVG
     LELKPHSSAE CNFCRRPLHF EVMSEREKAY FSGMSKMVSA QA
 
 
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